The Enzyme Database

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EC 2.4.1.256     
Accepted name: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = dolichyl phosphate + α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG10; Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol α-1,2-glucosyltransferase (configuration-retaining)
Comments: This eukaryotic enzyme performs the final step in the synthesis of the lipid-linked oligosaccharide, attaching D-glucose in an α-1,2-linkage to the outermost D-glucose in the long branch. The lipid-linked oligosaccharide is involved in N-linked protein glycosylation of selected asparagine residues of nascent polypeptide chains in eukaryotic cells.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Burda, P. and Aebi, M. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8 (1998) 455–462. [DOI] [PMID: 9597543]
[EC 2.4.1.256 created 2011, modified 2012]
 
 
EC 2.4.1.257     
Accepted name: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
Reaction: GDP-α-D-mannose + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase
Systematic name: GDP-α-D-mannose:α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900–11912. [DOI] [PMID: 19282279]
2.  O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
[EC 2.4.1.257 created 2011, modified 2012]
 
 
EC 2.4.1.258     
Accepted name: dolichyl-P-Man:Man5GlcNAc2-PP-dolichol α-1,3-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): Man5GlcNAc2-PP-Dol mannosyltransferase; ALG3; dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase; Not56-like protein; Alg3 α-1,3-mannosyl transferase; Dol-P-Man:Man5GlcNAc2-PP-Dol α-1,3-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-mannosyltransferase (configuration-inverting)
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl β-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sharma, C.B., Knauer, R. and Lehle, L. Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase. Biol. Chem. 382 (2001) 321–328. [DOI] [PMID: 11308030]
2.  Cipollo, J.F. and Trimble, R.B. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Δalg9 mutant reveals a regulatory role for the Alg3p α1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J. Biol. Chem. 275 (2000) 4267–4277. [DOI] [PMID: 10660594]
[EC 2.4.1.258 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.258, modified 2012]
 
 
EC 2.4.1.259     
Accepted name: dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man6GlcNAc2-PP-Dol α-1,2-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,2-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues - the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [PMID: 19451548]
2.  Cipollo, J.F. and Trimble, R.B. The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Δalg9 mutant reveals a regulatory role for the Alg3p α1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J. Biol. Chem. 275 (2000) 4267–4277. [DOI] [PMID: 10660594]
3.  Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]
[EC 2.4.1.259 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.259, modified 2012]
 
 
EC 2.4.1.260     
Accepted name: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-α-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG12; ALG12 mannosyltransferase; ALG12 α1,6mannosyltransferase; dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase; dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl α6-mannosyltransferase; EBS4; Dol-P-Man:Man7GlcNAc2-PP-Dol α-1,6-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,6-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→6)]-β-D-Man-β-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-inverting)
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]
2.  Hong, Z., Jin, H., Fitchette, A.C., Xia, Y., Monk, A.M., Faye, L. and Li, J. Mutations of an α1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis. Plant Cell 21 (2009) 3792–3802. [DOI] [PMID: 20023196]
3.  Cipollo, J.F. and Trimble, R.B. The Saccharomyces cerevisiae alg12δ mutant reveals a role for the middle-arm α1,2Man- and upper-arm α1,2Manα1,6Man- residues of Glc3Man9GlcNAc2-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus. Glycobiology 12 (2002) 749–762. [PMID: 12460943]
4.  Grubenmann, C.E., Frank, C.G., Kjaergaard, S., Berger, E.G., Aebi, M. and Hennet, T. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum. Mol. Genet. 11 (2002) 2331–2339. [DOI] [PMID: 12217961]
[EC 2.4.1.260 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.160, modified 2012]
 
 
EC 2.4.1.261     
Accepted name: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: dolichyl β-D-mannosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG9; ALG9 α1,2 mannosyltransferase; dolichylphosphomannose-dependent ALG9 mannosyltransferase; ALG9 mannosyltransferase; Dol-P-Man:Man8GlcNAc2-PP-Dol α-1,2-mannosyltransferase; dolichyl β-D-mannosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase
Systematic name: dolichyl β-D-mannosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-inverting)
Comments: The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl β-D-mannosyl phosphate. ALG9 mannosyltransferase catalyses the addition of two different α-1,2-mannose residues: the addition of α-1,2-mannose to Man6GlcNAc2-PP-Dol (EC 2.4.1.259) and the addition of α-1,2-mannose to Man8GlcNAc2-PP-Dol (EC 2.4.1.261).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vleugels, W., Keldermans, L., Jaeken, J., Butters, T.D., Michalski, J.C., Matthijs, G. and Foulquier, F. Quality control of glycoproteins bearing truncated glycans in an ALG9-defective (CDG-IL) patient. Glycobiology 19 (2009) 910–917. [DOI] [PMID: 19451548]
2.  Frank, C.G. and Aebi, M. ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis. Glycobiology 15 (2005) 1156–1163. [DOI] [PMID: 15987956]
[EC 2.4.1.261 created 1976 as EC 2.4.1.130, part transferred 2011 to EC 2.4.1.261, modified 2012]
 
 
EC 2.4.1.265     
Accepted name: dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG8; Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Glc-α-(1→3)-D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Stagljar, I., te Heesen, S. and Aebi, M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl. Acad. Sci. USA 91 (1994) 5977–5981. [DOI] [PMID: 8016100]
2.  Runge, K.W. and Robbins, P.W. A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues. J. Biol. Chem. 261 (1986) 15582–15590. [PMID: 3536907]
3.  Chantret, I., Dancourt, J., Dupre, T., Delenda, C., Bucher, S., Vuillaumier-Barrot, S., Ogier de Baulny, H., Peletan, C., Danos, O., Seta, N., Durand, G., Oriol, R., Codogno, P. and Moore, S.E. A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl α3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. J. Biol. Chem. 278 (2003) 9962–9971. [DOI] [PMID: 12480927]
[EC 2.4.1.265 created 2011, modified 2012]
 
 
EC 2.4.1.267     
Accepted name: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase
Reaction: dolichyl β-D-glucosyl phosphate + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol + dolichyl phosphate
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG6; Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase; dolichyl β-D-glucosyl phosphate:D-Man-α-(1→2)-D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→3)-[D-Man-α-(1→2)-D-Man-α-(1→6)]-D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-1,3-glucosyltransferase
Systematic name: dolichyl β-D-glucosyl-phosphate:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-glucosyltransferase (configuration-inverting)
Comments: The successive addition of three glucose residues by EC 2.4.1.267, EC 2.4.1.265 (Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase) and EC 2.4.1.256 (Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol α-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Reiss, G., te Heesen, S., Zimmerman, J., Robbins, P.W. and Aebi, M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology 6 (1996) 493–498. [DOI] [PMID: 8877369]
2.  Runge, K.W., Huffaker, T.C. and Robbins, P.W. Two yeast mutations in glucosylation steps of the asparagine glycosylation pathway. J. Biol. Chem. 259 (1984) 412–417. [PMID: 6423630]
3.  Westphal, V., Xiao, M., Kwok, P.Y. and Freeze, H.H. Identification of a frequent variant in ALG6, the cause of congenital disorder of glycosylation-Ic. Hum. Mutat. 22 (2003) 420–421. [DOI] [PMID: 14517965]
[EC 2.4.1.267 created 2011, modified 2012]
 
 
EC 2.4.1.285     
Accepted name: UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + ribostamycin = UDP + 2′′′-acetyl-6′′′-hydroxyneomycin C
Other name(s): neoK (gene name)
Systematic name: UDP-N-acetyl-α-D-glucosamine:ribostamycin N-acetylglucosaminyltransferase
Comments: Involved in biosynthesis of the aminoglycoside antibiotic neomycin. Requires a divalent metal ion, optimally Mg2+, Mn2+ or Co2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744]
[EC 2.4.1.285 created 2012]
 
 
EC 2.4.1.303     
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbbD; WbbD β3Gal-transferase; UDP-Gal:GlcNAc-R β1,3-galactosyltransferase; UDP-Gal:GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase; UDP-Gal:GlcNAc-R galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-β-galactosyltransferase (configuration-inverting)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O7:K1 (VW187). Requires Mn2+. cf. EC 2.4.1.343, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Riley, J.G., Menggad, M., Montoya-Peleaz, P.J., Szarek, W.A., Marolda, C.L., Valvano, M.A., Schutzbach, J.S. and Brockhausen, I. The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal: GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase involved in the biosynthesis of O7-specific lipopolysaccharide. Glycobiology 15 (2005) 605–613. [DOI] [PMID: 15625181]
2.  Brockhausen, I., Riley, J.G., Joynt, M., Yang, X. and Szarek, W.A. Acceptor substrate specificity of UDP-Gal: GlcNAc-R β1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1. Glycoconj. J. 25 (2008) 663–673. [DOI] [PMID: 18536883]
[EC 2.4.1.303 created 2013, modified 2017]
 
 
EC 2.4.1.304     
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→4)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfeD; UDP-Gal:GlcNAc-R 1,4-Gal-transferase; UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,4-galactosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn2+ or to a lesser extent by Mg2+, Ca2+, Ni2+ or Pb2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xu, C., Liu, B., Hu, B., Han, Y., Feng, L., Allingham, J.S., Szarek, W.A., Wang, L. and Brockhausen, I. Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis. J. Bacteriol. 193 (2011) 449–459. [DOI] [PMID: 21057010]
[EC 2.4.1.304 created 2013]
 
 
EC 2.4.1.305     
Accepted name: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase
Reaction: UDP-α-D-glucose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Glc-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WfaP; WfgD; UDP-Glc:GlcNAc-pyrophosphate-lipid β-1,3-glucosyltransferase; UDP-Glc:GlcNAc-diphosphate-lipid β-1,3-glucosyltransferase
Systematic name: UDP-α-D-glucose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,3-glucosyltransferase
Comments: The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brockhausen, I., Hu, B., Liu, B., Lau, K., Szarek, W.A., Wang, L. and Feng, L. Characterization of two β-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152. J. Bacteriol. 190 (2008) 4922–4932. [DOI] [PMID: 18487334]
[EC 2.4.1.305 created 2013]
 
 
EC 2.4.1.313     
Accepted name: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]
For diagram of glycoprotein biosynthesis, click here
Other name(s): B3GALNT2
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl-threonyl-[protein] 3-β-N-acetyl-D-galactosaminyltransferase
Comments: The human protein is specific for UDP-N-acetyl-α-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hiruma, T., Togayachi, A., Okamura, K., Sato, T., Kikuchi, N., Kwon, Y.D., Nakamura, A., Fujimura, K., Gotoh, M., Tachibana, K., Ishizuka, Y., Noce, T., Nakanishi, H. and Narimatsu, H. A novel human β1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcβ1-3GlcNAc. J. Biol. Chem. 279 (2004) 14087–14095. [DOI] [PMID: 14724282]
2.  Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]
[EC 2.4.1.313 created 2013]
 
 
EC 2.4.1.343     
Accepted name: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): wclR (gene name)
Systematic name: UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-galactosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O3. Requires a divalent metal ion (Mn2+, Mg2+ or Fe2+). cf. EC 2.4.1.303, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, C., Liu, B., Xu, Y., Utkina, N., Zhou, D., Danilov, L., Torgov, V., Veselovsky, V. and Feng, L. Biochemical characterization of the novel α-1, 3-galactosyltransferase WclR from Escherichia coli O3. Carbohydr. Res. 430 (2016) 36–43. [DOI] [PMID: 27196310]
[EC 2.4.1.343 created 2017]
 
 
EC 2.4.1.371     
Accepted name: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosylpolymerase
Reaction: (1) 2 GDP-α-D-mannose + [α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = 2 GDP + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
(2) 2 GDP-α-D-mannose + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = 2 GDP + [α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n+1-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdA
Systematic name: GDP-α-D-mannose:α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosyltransferase (configuration-retaining)
Comments: The enzyme is involved in the biosynthesis of polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. The enzymes consists of two domains that are responsible for the 1→2 and 1→3 linkages, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Greenfield, L.K., Richards, M.R., Li, J., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases. J. Biol. Chem. 287 (2012) 35078–35091. [DOI] [PMID: 22875852]
2.  Greenfield, L.K., Richards, M.R., Vinogradov, E., Wakarchuk, W.W., Lowary, T.L. and Whitfield, C. Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens. J. Biol. Chem. 287 (2012) 38135–38149. [PMID: 22989876]
3.  Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075–1085. [DOI] [PMID: 25422321]
[EC 2.4.1.371 created 2019]
 
 
EC 2.4.1.386     
Accepted name: GlcNAc-β-1,3-Gal β-1,6-N-acetylglucosaminyltransferase (distally acting)
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Other name(s): UDP-GlcNAc:GlcNAcβ1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase; dIGnT; C2GnT2 (misleading)
Systematic name: UDP-N-acetyl-α-D-glucosamine:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: Involved in the production of milk oligosaccharides in the lacto-N-triose (LNT) series. Cf. EC 2.4.1.150 (N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase; cIGnT) and EC 2.4.1.148 (acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658]
2.  Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862]
[EC 2.4.1.386 created 2021]
 
 
EC 2.4.2.38     
Accepted name: glycoprotein 2-β-D-xylosyltransferase
Reaction: UDP-α-D-xylose + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] = UDP + N4-{β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[β-D-GlcNAc-(1→2)-α-D-Man-(1→6)]-[β-D-Xyl-(1→2)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein]
For diagram of mannosyl-glycoprotein fucosyl and xylosyl transferases, click here
Other name(s): β1,2-xylosyltransferase; UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of 4-N-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase; UDP-D-xylose:glycoprotein (D-xylose to the 3,6-disubstituted mannose of N4-{N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→3)-[N-acetyl-β-D-glucosaminyl-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-β-D-glucosaminyl}asparagine) 2-β-D-xylosyltransferase
Systematic name: UDP-α-D-xylose:N4-{β-D-GlcNAc-(1→2)-α-D-mannosyl-(1→3)-[β-D-GlcNAc-(1→2)-α-D-mannosyl-(1→6)]-β-D-mannosyl-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-L-asparaginyl-[protein] 2-β-D-xylosyltransferase (configuration-inverting)
Comments: Specific for N-linked oligosaccharides (N-glycans).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 141256-56-6
References:
1.  Zeng, Y., Bannon, G., Thomas, V.H., Rice, K., Drake, R. and Elbein, A. Purification and specificity of β1,2-xylosyltransferase, an enzyme that contributes to the allergenicity of some plant proteins. J. Biol. Chem. 272 (1997) 31340–31347. [DOI] [PMID: 9395463]
2.  Strasser, R., Mucha, J., Mach, L., Altmann, F., Wilson, I.B., Glössl, J. and Steinkellner, H. Molecular cloning and functional expression of β1,2-xylosyltransferase cDNA from Arabidopsis thaliana. FEBS Lett. 472 (2000) 105–108. [DOI] [PMID: 10781814]
[EC 2.4.2.38 created 2001]
 
 
EC 2.4.2.61     
Accepted name: α-dystroglycan β1,4-xylosyltransferase
Reaction: UDP-α-D-xylose + 3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] = UDP + 3-O-[β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein]
Other name(s): TMEM5 (gene name)
Systematic name: UDP-α-D-xylose:3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] xylosyltransferase
Comments: This eukaryotic enzyme catalyses a step in the biosynthesis of the glycan moiety of the membrane protein α-dystroglycan. It is specific for the second ribitol 5-phosphate in the nascent glycan chain as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vuillaumier-Barrot, S., Bouchet-Seraphin, C., Chelbi, M., Devisme, L., Quentin, S., Gazal, S., Laquerriere, A., Fallet-Bianco, C., Loget, P., Odent, S., Carles, D., Bazin, A., Aziza, J., Clemenson, A., Guimiot, F., Bonniere, M., Monnot, S., Bole-Feysot, C., Bernard, J.P., Loeuillet, L., Gonzales, M., Socha, K., Grandchamp, B., Attie-Bitach, T., Encha-Razavi, F. and Seta, N. Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly. Am. J. Hum. Genet. 91 (2012) 1135–1143. [PMID: 23217329]
2.  Manya, H., Yamaguchi, Y., Kanagawa, M., Kobayashi, K., Tajiri, M., Akasaka-Manya, K., Kawakami, H., Mizuno, M., Wada, Y., Toda, T. and Endo, T. The muscular dystrophy gene TMEM5 encodes a ribitol β1,4-xylosyltransferase required for the functional glycosylation of dystroglycan. J. Biol. Chem. 291 (2016) 24618–24627. [PMID: 27733679]
[EC 2.4.2.61 created 2018]
 
 
EC 2.4.3.5     
Accepted name: galactosyldiacylglycerol α-2,3-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + 1,2-diacyl-3-β-D-galactosyl-sn-glycerol = CMP + 1,2-diacyl-3-[3-(N-acetyl-α-D-neuraminyl)-β-D-galactosyl]-sn-glycerol
Systematic name: CMP-N-acetyl-β-neuraminate:1,2-diacyl-3-β-D-galactosyl-sn-glycerol N-acetylneuraminyltransferase
Comments: The β-D-galactosyl residue of the oligosaccharide of glycoproteins may also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 80237-98-5
References:
1.  Pieringer, J., Keech, S. and Pieringer, R.A. Biosynthesis in vitro of sialosylgalactosyldiacylglycerol by mouse brain microsomes. J. Biol. Chem. 256 (1981) 12306–12309. [PMID: 7298658]
2.  Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. Purification of a Gal β1→4GlcNAc α2→6 sialyltransferase and a Gal β1→3(4)GlcNAc α2→3 sialyltransferase to homogeneity from rat liver. J. Biol. Chem. 257 (1982) 13835–13844. [PMID: 7142179]
3.  Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Gal β1→3(4)GlcNAc α2→3 sialyltransferase and a Gal β1→4GlcNAc α2→6 sialyltransferase from rat liver. J. Biol. Chem. 257 (1982) 13845–13853. [PMID: 7142180]
[EC 2.4.3.5 created 1984 as EC 2.4.99.5, modified 1986, transferred 2022 to EC 2.4.3.5]
 
 
EC 2.4.3.10     
Accepted name: N-acetylglucosaminide α-(2,6)-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl-R = CMP + N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-[N-acetyl-α-neuraminyl-(2→6)]-N-acetyl-β-D-glucosaminyl-R
Other name(s): α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylglucosaminide 6-α-sialyltransferase; N-acetylglucosaminide (α 2→6)-sialyltransferase; ST6GlcNAc
Systematic name: CMP-N-acetylneuraminate:N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminide N-acetyl-β-D-glucosamine-6-α-N-acetylneuraminyltransferase (configuration-inverting)
Comments: Attaches N-acetylneuraminic acid in α-2,6-linkage to N-acetyl-β-D-glucosamine. The enzyme from rat liver also acts on β-D-galactosyl-(1→3)-N-acetyl-β-D-glucosaminyl residues, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Paulson, J.C., Weinstein, J. and de Souza-e-Silva, U. Biosynthesis of a disialylated sequence in N-linked oligosaccharides: identification of an N-acetylglucosaminide (α 2→6)-sialyltransferase in Golgi apparatus from rat liver. Eur. J. Biochem. 140 (1984) 523–530. [PMID: 6547092]
[EC 2.4.3.10 created 2020 as EC 2.4.99.22, transferred 2022 to EC 2.4.3.10]
 
 
EC 2.4.99.5      
Transferred entry: galactosyldiacylglycerol α-2,3-sialyltransferase. Now EC 2.4.3.5, galactosyldiacylglycerol α-2,3-sialyltransferase
[EC 2.4.99.5 created 1984, modified 1986, deleted 2022]
 
 
EC 2.4.99.18     
Accepted name: dolichyl-diphosphooligosaccharide—protein glycotransferase
Reaction: dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-β-D-glycosyl linkage to a protein L-asparagine
For diagram of glycoprotein biosynthesis, click here
Other name(s): dolichyldiphosphooligosaccharide-protein glycosyltransferase; asparagine N-glycosyltransferase; dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase; dolichylpyrophosphodiacetylchitobiose-protein glycosyltransferase; oligomannosyltransferase; oligosaccharide transferase; dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase; dolichyl-diphosphooligosaccharide:protein-L-asparagine oligopolysaccharidotransferase; STT3
Systematic name: dolichyl-diphosphooligosaccharide:protein-L-asparagine N-β-D-oligopolysaccharidotransferase
Comments: Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram click here). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref [2] for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the ω end, and the rest of the double-bonds in cis form.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 75302-32-8
References:
1.  Das, R.C. and Heath, E.C. Dolichyldiphosphoryloligosaccharide-protein oligosaccharyltransferase; solubilization, purification, and properties. Proc. Natl. Acad. Sci. USA 77 (1980) 3811–3815. [DOI] [PMID: 6933437]
2.  Song, W., Henquet, M.G., Mentink, R.A., van Dijk, A.J., Cordewener, J.H., Bosch, D., America, A.H. and van der Krol, A.R. N-glycoproteomics in plants: perspectives and challenges. J Proteomics 74 (2011) 1463–1474. [DOI] [PMID: 21605711]
[EC 2.4.99.18 created 1984 as EC 2.4.1.119, transferred 2012 to EC 2.4.99.18]
 
 
EC 2.4.99.22      
Transferred entry: N-acetylglucosaminide α-(2,6)-sialyltransferase. Now EC 2.4.3.10, N-acetylglucosaminide α-(2,6)-sialyltransferase
[EC 2.4.99.22 created 2020, deleted 2022]
 
 
EC 2.4.99.28     
Accepted name: peptidoglycan glycosyltransferase
Reaction: [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
Glossary: Mur2Ac = N-acetylmuramic acid
Other name(s): PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase
Systematic name: [poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-04-2
References:
1.  Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018–5022. [DOI] [PMID: 6802846]
2.  Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079–1093. [DOI] [PMID: 9841666]
3.  van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25. [DOI] [PMID: 11320055]
[EC 2.4.99.28 created 1984 as EC 2.4.1.129, modified 2002, transferred 2023 to EC 2.4.99.28]
 
 
EC 2.6.1.16     
Accepted name: glutamine—fructose-6-phosphate transaminase (isomerizing)
Reaction: L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Other name(s): hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase
Systematic name: L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
Comments: Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-45-9
References:
1.  Ghosh, S., Blumenthal, H.J., Davidson, E. and Roseman, S. Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate. J. Biol. Chem. 235 (1960) 1265–1273. [PMID: 13827775]
2.  Gryder, R.M. and Pogell, B.M. Further studies on glucosamine 6-phosphate synthesis by rat liver enzymes. J. Biol. Chem. 235 (1960) 558–562. [PMID: 13829889]
3.  Leloir, L.F. and Cardini, C.E. The biosynthesis of glucosamine. Biochim. Biophys. Acta 12 (1953) 15–22. [DOI] [PMID: 13115409]
4.  Teplyakov, A., Obmolova, G., Badet-Denisot, M.A. and Badet, B. The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase. Protein Sci. 8 (1999) 596–602. [DOI] [PMID: 10091662]
[EC 2.6.1.16 created 1961, deleted 1972, reinstated 1984, modified 2000 (EC 5.3.1.19 created 1972, incorporated 1984)]
 
 
EC 2.6.1.98     
Accepted name: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
Reaction: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate + 2-oxoglutarate = UDP-2-acetamido-2-deoxy-α-D-ribo-hex-3-uluronate + L-glutamate
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Other name(s): WbpE; WlbC
Systematic name: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5′-phosphate protein. This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the previous enzyme in the pathway, EC 1.1.1.335 (UDP-N-acetyl-2-amino-2-deoxyglucuronate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854–11862. [DOI] [PMID: 19282284]
2.  Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446–5455. [DOI] [PMID: 19348502]
3.  Larkin, A., Olivier, N.B. and Imperiali, B. Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly. Biochemistry 49 (2010) 7227–7237. [DOI] [PMID: 20604544]
[EC 2.6.1.98 created 2012]
 
 
EC 2.7.1.181     
Accepted name: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
Reaction: ATP + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = ADP + 3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdD; ATP:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phosphotransferase
Systematic name: ATP:α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phosphotransferase
Comments: The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the methylation of 3-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.1.1.294, 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709–35718. [DOI] [PMID: 15184370]
2.  Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662–30672. [DOI] [PMID: 19734145]
3.  Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391–41401. [DOI] [PMID: 21990359]
4.  Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075–1085. [DOI] [PMID: 25422321]
[EC 2.7.1.181 created 2014, modified 2017]
 
 
EC 2.7.7.23     
Accepted name: UDP-N-acetylglucosamine diphosphorylase
Reaction: UTP + N-acetyl-α-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-α-D-glucosamine
For diagram of UDP-N-acetylglucosamine biosynthesis, click here
Other name(s): UDP-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine pyrophosphorylase; UTP:2-acetamido-2-deoxy-α-D-glucose-1-phosphate uridylyltransferase; UDP-GlcNAc pyrophosphorylase; GlmU uridylyltransferase; Acetylglucosamine 1-phosphate uridylyltransferase; UDP-acetylglucosamine pyrophosphorylase; uridine diphosphate-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine phosphorylase; acetylglucosamine 1-phosphate uridylyltransferase
Systematic name: UTP:N-acetyl-α-D-glucosamine-1-phosphate uridylyltransferase
Comments: Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-α-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-06-7
References:
1.  Pattabiramin, T.N. and Bachhawat, B.K. Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain. Biochim. Biophys. Acta 50 (1961) 129–134. [DOI] [PMID: 13733356]
2.  Strominger, J.L. and Smith, M.S. Uridine diphosphoacetylglucosamine pyrophosphorylase. J. Biol. Chem. 234 (1959) 1822–1827. [PMID: 13672971]
3.  Mengin-Lecreulx, D. and van Heijenoort, J. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. 176 (1994) 5788–5795. [DOI] [PMID: 8083170]
4.  Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T. and Brown, E.D. Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35 (1996) 579–585. [DOI] [PMID: 8555230]
5.  Wang-Gillam, A., Pastuszak, I. and Elbein, A.D. A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J. Biol. Chem. 273 (1998) 27055–27057. [DOI] [PMID: 9765219]
6.  Olsen, L.R. and Roderick, S.L. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40 (2001) 1913–1921. [DOI] [PMID: 11329257]
7.  Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 20 (2001) 6191–6202. [DOI] [PMID: 11707391]
[EC 2.7.7.23 created 1965, modified 2012]
 
 
EC 2.7.7.83     
Accepted name: UDP-N-acetylgalactosamine diphosphorylase
Reaction: UTP + N-acetyl-α-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-α-D-galactosamine
Systematic name: UTP:N-acetyl-α-D-galactosamine-1-phosphate uridylyltransferase
Comments: The enzyme from plants and animals also has activity toward N-acetyl-α-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Wang-Gillam, A., Pastuszak, I. and Elbein, A.D. A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J. Biol. Chem. 273 (1998) 27055–27057. [DOI] [PMID: 9765219]
2.  Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 20 (2001) 6191–6202. [DOI] [PMID: 11707391]
[EC 2.7.7.83 created 2012]
 
 
EC 2.7.8.15     
Accepted name: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase; UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase; uridine diphosphoacetylglucosamine-dolichyl phosphate acetylglucosamine-1-phosphotransferase; chitobiosylpyrophosphoryldolichol synthase; dolichol phosphate N-acetylglucosamine-1-phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase; UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase
Systematic name: UDP-N-α-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase (configuration-retaining)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70431-08-2
References:
1.  Sharma, C.B., Lehle, L. and Tanner, W. Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast. Eur. J. Biochem. 126 (1982) 319–325. [DOI] [PMID: 6215245]
2.  Villemez, C.L. and Carlo, P.L. Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase. J. Biol. Chem. 255 (1980) 8174–8178. [PMID: 6447695]
[EC 2.7.8.15 created 1983]
 
 
EC 2.7.8.17     
Accepted name: UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
Other name(s): N-acetylglucosaminylphosphotransferase; UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase; uridine diphosphoacetylglucosamine-lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase; uridine diphosphoacetylglucosamine-glycoprotein acetylglucosamine-1-phosphotransferase; lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase; N-acetylglucosaminyl phosphotransferase; UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase; UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase; UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminyl-1-phosphotransferase
Systematic name: UDP-N-acetyl-D-glucosamine:lysosomal-enzyme N-acetylglucosaminephosphotransferase
Comments: Some other glycoproteins with high-mannose can act as acceptors, but much more slowly than lysosomal enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 84012-69-1
References:
1.  Reitman, M.L. and Kornfeld, S. UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase. Proposed enzyme for the phosphorylation of the high mannose oligosaccharide units of lysosomal enzymes. J. Biol. Chem. 256 (1981) 4275–4281. [PMID: 6452459]
2.  Reitman, M.L. and Kornfeld, S. Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes. J. Biol. Chem. 256 (1981) 11977–11980. [PMID: 6457829]
3.  Waheed, A., Hasilik, A. and von Figura, K. UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme. J. Biol. Chem. 257 (1982) 12322–12331. [PMID: 6288715]
4.  Waheed, A., Pohlmann, R., Hasilik, A. and von Figura, K. Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes. J. Biol. Chem. 256 (1981) 4150–4152. [PMID: 6260788]
[EC 2.7.8.17 created 1984]
 
 
EC 2.7.8.33     
Accepted name: UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = lipid I = GlcNAc-pyrophosphorylundecaprenol = ditrans,octacis-undecaprenyl-N-acetyl-α-D-glucosaminyl diphosphate
Other name(s): UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase; UDP-GIcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase; GlcNAc-P-P-Und synthase; GPT (ambiguous); TagO; UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase; UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetylglucosaminephosphotransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-α-D-glucosaminephosphotransferase
Comments: This enzyme catalyses the synthesis of N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 [2] and of teichoic acid in certain Gram-positive bacteria [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Al-Dabbagh, B., Mengin-Lecreulx, D. and Bouhss, A. Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA. J. Bacteriol. 190 (2008) 7141–7146. [DOI] [PMID: 18723618]
2.  Lehrer, J., Vigeant, K.A., Tatar, L.D. and Valvano, M.A. Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide. J. Bacteriol. 189 (2007) 2618–2628. [DOI] [PMID: 17237164]
3.  Rush, J.S., Rick, P.D. and Waechter, C.J. Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli. Glycobiology 7 (1997) 315–322. [DOI] [PMID: 9134438]
4.  Soldo, B., Lazarevic, V. and Karamata, D. tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168. Microbiology 148 (2002) 2079–2087. [DOI] [PMID: 12101296]
[EC 2.7.8.33 created 2011]
 
 
EC 2.7.8.35     
Accepted name: UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + trans,octacis-decaprenyl phosphate = UMP + N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol
For diagram of galactofuranan biosynthesis, click here
Other name(s): GlcNAc-1-phosphate transferase; UDP-GlcNAc:undecaprenyl phosphate GlcNAc-1-phosphate transferase; WecA; WecA transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase
Comments: Isolated from Mycobacterium tuberculosis and Mycobacterium smegmatis. This enzyme catalyses the synthesis of monotrans,octacis-decaprenyl-N-acetyl-α-D-glucosaminyl diphosphate (mycobacterial lipid I), an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. cf. EC 2.7.8.33, UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jin, Y., Xin, Y., Zhang, W. and Ma, Y. Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis. FEMS Microbiol. Lett. 310 (2010) 54–61. [DOI] [PMID: 20637039]
[EC 2.7.8.35 created 2012]
 
 
EC 2.8.2.23     
Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 1
Reaction: 3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
Other name(s): heparin-glucosamine 3-O-sulfotransferase; 3′-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase; glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 1 (3-OST-1, HS3ST1); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
Comments: This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases [EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2) and EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3)] by being the most selective for a precursor of the antithrombin-binding site. It has a minimal acceptor sequence of: → GlcNAc6S→ GlcA→ GlcN2S*+/-6S→ IdoA2S→ GlcN2S→ , the asterisk marking the target (symbols as in 2-Carb-38) using +/- to mean the presence or absence of a substituent, and > to separate a predominant structure from a minor one. Thus Glc(N2S > NAc) means a residue of glucosamine where the N carries a sulfo group mainly but occasionally an acetyl group. [1-4]. It can also modify other precursor sequences within heparan sulfate but this action does not create functional antithrombin-binding sites. These precursors are variants of the consensus sequence: → Glc(N2S > NAc)+/-6S→ GlcA→ GlcN2S*+/-6S→ GlcA > IdoA+/-2S→ Glc(N2S/NAc)+/-6S→ [5]. If the heparan sulfate substrate lacks 2-O-sulfation of GlcA residues, then enzyme specificity is expanded to modify selected glucosamine residues preceded by IdoA as well as GlcA [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 183257-54-7
References:
1.  Kusche, M., Backström, G., Riesenfeld, J., Pepitou, M., Choay, J. and Lindahl, U. Biosynthesis of heparin. O-Sulfation of the antithrombin-binding region. J. Biol. Chem. 263 (1988) 15474–15484. [PMID: 3139669]
2.  Shworak, N.W., Fritze, L.M.S., Liu, J., Butler, L.D. and Rosenberg, R.D. Cell-free synthesis of anticoagulant heparan sulfate reveals a limiting activity which modifies a nonlimiting precursor pool. J. Biol. Chem. 271 (1996) 27063–27071. [DOI] [PMID: 8900197]
3.  Liu, J., Shworak, N.W., Fritze, L.M.S., Edelberg, J.M. and Rosenberg, R.D. Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 271 (1996) 27072–27082. [DOI] [PMID: 8900198]
4.  Shworak, N.W., Liu, J., Fritze, L.M.S., Schwartz, J.J., Zhang, L., Logeart, D. and Rosenberg, R.D. Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. J. Biol. Chem. 272 (1997) 28008–28019. [DOI] [PMID: 9346953]
5.  Zhang, L., Yoshida, K., Liu, J. and Rosenberg, R.D. Anticoagulant heparan sulfate precursor structures in F9 embryonal carcinoma cells. J. Biol. Chem. 274 (1999) 5681–5691. [DOI] [PMID: 10026187]
6.  Zhang, L., Lawrence, R., Schwartz, J.J., Bai, X. , Wei., G, Esko, J.D. and Rosenberg, R.D. The effect of precursor structures on the action of glucosaminyl 3-O-sulfotransferase-1 and the biosynthesis of anticoagulant heparan sulfate. J. Biol. Chem. 276 (2001) 28806–28813. [DOI] [PMID: 11375390]
[EC 2.8.2.23 created 1992, modified 2001]
 
 
EC 2.8.2.29     
Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 2
Reaction: 3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
heparan sulfate: for definition click here
Other name(s): glucosaminyl 3-O-sulfotransferase; heparan sulfate D-glucosaminyl 3-O-sulfotransferase; isoform/isozyme 2 (3-OST-2, HS3ST2); 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
Comments: This enzyme sulfates the residues marked with an asterisk in sequences containing at least → IdoA2S→ GlcN*→ or → GlcA2S→ GlcN*→ (symbols as in 2-Carb-38). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shworak, N.W., Liu, J., Petros, L.M., Copeland, N.G. , Jenkins N.A. and Rosenberg, R.D. Diversity of the extensive heparan sulfate D-glucosaminyl 3-O-sulfotransferase (3-OST) multigene family. J. Biol. Chem. 274 (1999) 5170–5184. [DOI] [PMID: 9988767]
2.  Liu, J., Shworak, N.W., Sina, P., Schwartz, J.J., Zhang, L., Fritze, L.M.S. and Rosenberg, R.D. Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J. Biol. Chem. 274 (1999) 5185–5192. [DOI] [PMID: 9988768]
[EC 2.8.2.29 created 2001]
 
 
EC 2.8.2.30     
Accepted name: [heparan sulfate]-glucosamine 3-sulfotransferase 3
Reaction: 3′-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3′,5′-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Glossary: 3′-phosphoadenylyl sulfate = PAPS
heparan sulfate: for definition click here
Other name(s): 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
Systematic name: 3′-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfonotransferase
Comments: Two major substrates contain the tetrasaccharides: → undetermined 2-sulfo-uronic acid→ GlcN2S→ IdoA2S→ GlcN*→ and → undetermined 2-sulfo-uronic acid→ GlcN2S→ IdoA2S→ GlcN6S*→ (symbols as in 2-Carb-38) with modification of the N-unsubstituted glucosamine residue (shown with an asterisk) [1,4]. Modification of selected sequences containing N-sulfo-glucosamine residues cannot yet be excluded. The 3-O-sulfated heparan sulfate can be utilized by Herpes simplex virus type 1 as an entry receptor to infect the target cells [2]. There are two isozymes, known as 3-OST-3A and 3-OST-3B, which have identical catalytic domains but are encoded by different mammalian genes [3]. The specificity of this enzyme differs from that of the other [heparan sulfate]-glucosamine 3-sulfotransferases. It is inefficient at modifying precursors of the antithrombin binding site [in contrast to EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1)] and it does not modify glucosamine preceded by GlcA2S [unlike EC 2.8.2.29 ([heparan sulfate]-glucosamine 3-sulfotransferase 2)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Liu, J., Shriver, Z., Blaiklock, P., Yoshida, K., Sasisekharan, R. and Rosenberg, R.D. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A sulfates N-unsubstituted glucosamine. J. Biol. Chem. 274 (1999) 38155–38162. [DOI] [PMID: 10608887]
2.  Shukla, D., Liu, J., Blaiklock, P., Shworak, N.W., Bai, X., Esko, J.D., Cohen, G.H., Eisenberg, R.J., Rosenberg, R.D. and Spear, P.G. A novel role for 3-O-sulfated heparan sulfate in Herpes simplex virus 1 entry. Cell 99 (1999) 13–22. [DOI] [PMID: 10520990]
3.  Shworak, N.W., Liu, J., Petros, L.M., Copeland, N.G. , Jenkins N.A. and Rosenberg, R.D. Diversity of the extensive heparan sulfate D-glucosaminyl 3-O-sulfotransferase (3-OST) multigene family. J. Biol. Chem. 274 (1999) 5170–5184. [DOI] [PMID: 9988767]
4.  Liu, J., Shworak, N.W., Sina, P., Schwartz, J.J., Zhang, L., Fritze, L.M.S. and Rosenberg, R.D. Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. J. Biol. Chem. 274 (1999) 5185–5192. [DOI] [PMID: 9988768]
[EC 2.8.2.30 created 2001]
 
 
EC 3.1.1.77     
Accepted name: acyloxyacyl hydrolase
Reaction: 3-(acyloxy)acyl group of bacterial toxin + H2O = 3-hydroxyacyl group of bacterial toxin + a fatty acid
For diagram of reaction, click here
Comments: The substrate is lipid A on the reducing end of the toxic lipopolysaccharide (LPS) of Salmonella typhimurium and related organisms. It consists of diglucosamine, β-D-GlcN-(1→ 6)-D-GlcN, attached by glycosylation on O-6 of its non-reducing residue, phosphorylated on O-4 of this residue and on O-1 of its potentially reducing residue. Both residues carry 3-(acyloxy)acyl groups on N-2 and O-3. The enzyme from human leucocytes detoxifies the lipid by hydrolysing the secondary acyl groups from O-3 of the 3-hydroxyacyl groups on the disaccharide (LPS). It also possesses a wide range of phospholipase and acyltransferase activities [e.g. EC 3.1.1.4 (phospholipase A2), EC 3.1.1.5 (lysophospholipase), EC 3.1.1.32 (phospholipase A1) and EC 3.1.1.52 (phosphatidylinositol deacylase)], hydrolysing diacylglycerol and phosphatidyl compounds, but not triacylglycerols. It has a preference for saturated C12-C16 acyl groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 110277-64-0
References:
1.  Erwin, A.L. and Munford, R.S. Deacylation of structurally diverse lipopolysaccharides by human acyloxyacyl hydrolase. J. Biol. Chem. 265 (1990) 16444–16449. [PMID: 2398058]
2.  Hagen, F.S., Grant, F.J., Kuijper, J.L., Slaughter, C.A., Moomaw, C.R., Orth, K., O'Hara, P.J. and Munford, R.S. Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides. Biochemistry 30 (1991) 8415–8423. [PMID: 1883828]
3.  Munford, R.S. and Hunter, J.P. Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro. J. Biol. Chem. 267 (1992) 10116–10121. [PMID: 1577781]
[EC 3.1.1.77 created 2001]
 
 
EC 3.1.1.103     
Accepted name: teichoic acid D-alanine hydrolase
Reaction: [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n D-alanine
Glossary: Rib-ol = ribitol
Other name(s): fmtA (gene name)
Systematic name: teichoic acid D-alanylhydrolase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface. The activity greatly increases methicillin resistance in MRSA strains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Komatsuzawa, H., Sugai, M., Ohta, K., Fujiwara, T., Nakashima, S., Suzuki, J., Lee, C.Y. and Suginaka, H. Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 41 (1997) 2355–2361. [PMID: 9371333]
2.  Qamar, A. and Golemi-Kotra, D. Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis. Antimicrob. Agents Chemother. 56 (2012) 3797–3805. [DOI] [PMID: 22564846]
3.  Rahman, M.M., Hunter, H.N., Prova, S., Verma, V., Qamar, A. and Golemi-Kotra, D. The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino esterase that acts on teichoic acids. MBio 7 (2016) e02070. [DOI] [PMID: 26861022]
[EC 3.1.1.103 created 2018]
 
 
EC 3.1.4.50     
Accepted name: glycosylphosphatidylinositol phospholipase D
Reaction: 6-(α-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(α-D-glucosaminyl)-1D-myo-inositol + 3-sn-phosphatidate
For diagram of glycosylphosphatidyl-myo-inositol biosynthesis, click here
Other name(s): GPI-PLD; glycoprotein phospholipase D; phosphatidylinositol phospholipase D; phosphatidylinositol-specific phospholipase D
Systematic name: glycoprotein-phosphatidylinositol phosphatidohydrolase
Comments: This enzyme is also active when O-4 of the glucosamine is substituted by carrying the oligosaccharide that can link a protein to the structure. It therefore cleaves proteins from the lipid part of the glycosylphosphatidylinositol (GPI) anchors, but does so by hydrolysis, whereas glycosylphosphatidylinositol diacylglycerol-lyase (EC 4.6.1.14) does so by elimination. It acts on plasma membranes only after solubilization of the substrate with detergents or solvents, but it may act on intracellular membranes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113756-14-2
References:
1.  Low, M.G. and Prasad, A.R.S. A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma. Proc. Natl. Acad. Sci. USA 85 (1988) 980–984. [DOI] [PMID: 3422494]
2.  Malik, A.-S. and Low, M.G. Conversion of human placental alkaline phosphatase from a high Mr form to a low Mr form during butanol extraction. An investigation of the role of endogenous phosphoinositide-specific phospholipases. Biochem. J. 240 (1986) 519–527. [PMID: 3028377]
3.  Li, J.Y., Hollfelder, K., Huang, K.S. and Low, M.G. Structural features of GPI-specific phospholipase D revealed by fragmentation and Ca2+ binding studies. J. Biol. Chem. 269 (1994) 28963–28971. [PMID: 7961859]
4.  Deeg, M.A, Vierman, E.L. and Cheung, M.C. GPI-specific phospholipase D associates with an apoA-I- and apoA-IV-containing complex. J. Lipid Res. 42 (2001) 442–451. [PMID: 11254757]
[EC 3.1.4.50 created 1990, modified 2002]
 
 
EC 3.2.1.96     
Accepted name: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase
Reaction: Endohydrolysis of the N,N′-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact
Other name(s): N,N′-diacetylchitobiosyl β-N-acetylglucosaminidase; endo-β-N-acetylglucosaminidase; mannosyl-glycoprotein endo-β-N-acetylglucosamidase; di-N-acetylchitobiosyl β-N-acetylglucosaminidase; endo-β-acetylglucosaminidase; endo-β-(1→4)-N-acetylglucosaminidase; mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase; endoglycosidase S; endo-N-acetyl-β-D-glucosaminidase; endo-N-acetyl-β-glucosaminidase; endo-β-N-acetylglucosaminidase D; endo-β-N-acetylglucosaminidase F; endo-β-N-acetylglucosaminidase H; endo-β-N-acetylglucosaminidase L; glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase; endoglycosidase H
Systematic name: glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase
Comments: A group of related enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-88-9
References:
1.  Chien, S., Weinburg, R., Li, S. and Li, Y. Endo-β-N-acetylglucosaminidase from fig latex. Biochem. Biophys. Res. Commun. 76 (1977) 317–323. [DOI] [PMID: 1027432]
2.  Koide, N. and Muramatsu, T. Endo-β-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae. J. Biol. Chem. 249 (1974) 4897–4904. [PMID: 4152561]
3.  Pierce, R.J., Spik, G. and Montreuil, J. Cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity in rat liver and kidney. Biochem. J. 180 (1979) 673. [PMID: 486141]
4.  Pierce, R.J., Spik, G. and Montreuil, J. Demonstration and cytosolic location of an endo-N-acetyl-β-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver. Biochem. J. 185 (1980) 261–264. [PMID: 7378051]
5.  Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y. and Kobata, A. Structural studies of two ovalbumin glycopeptides in relation to the endo-β-N-acetylglucosaminidase specificity. J. Biol. Chem. 250 (1975) 8569–8575. [PMID: 389]
6.  Tarentino, A.L., Plummer, T.H., Jr. and Maley, F. The release of intact oligosaccharides from specific glycoproteins by endo-β-N-acetylglucosaminidase H. J. Biol. Chem. 249 (1974) 818–824. [PMID: 4204553]
[EC 3.2.1.96 created 1978]
 
 
EC 3.2.1.97     
Accepted name: endo-α-N-acetylgalactosaminidase
Reaction: β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl-[glycoprotein]-L-serine/L-threonine + H2O = β-D-galactosyl-(1→3)-N-acetyl-D-galactosamine + [glycoprotein]-L-serine/L-threonine
Other name(s): endo-α-acetylgalactosaminidase; endo-α-N-acetyl-D-galactosaminidase; mucinaminylserine mucinaminidase; D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase; endo-α-GalNAc-ase; glycopeptide α-N-acetylgalactosaminidase; D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Systematic name: glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase
Comments: The enzyme catalyses the liberation of Gal-(1→3)-β-GalNAc α-linked to serine or threonine residues of mucin-type glycoproteins. EngBF from the bacterium Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1→3)-β-GalNAc. The enzymes from the bacteria Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. they can also release the core 2 trisaccharide Gal-(1→3)-β-(GlcNAc-(1→6)-β)-GalNAc or the core 3 disaccharide GlcNAc-(1→3)-β-GalNAc) [1,2]. The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 59793-96-3
References:
1.  Ashida, H., Maki, R., Ozawa, H., Tani, Y., Kiyohara, M., Fujita, M., Imamura, A., Ishida, H., Kiso, M. and Yamamoto, K. Characterization of two different endo-α-N-acetylgalactosaminidases from probiotic and pathogenic enterobacteria, Bifidobacterium longum and Clostridium perfringens. Glycobiology 18 (2008) 727–734. [DOI] [PMID: 18559962]
2.  Koutsioulis, D., Landry, D. and Guthrie, E.P. Novel endo-α-N-acetylgalactosaminidases with broader substrate specificity. Glycobiology 18 (2008) 799–805. [DOI] [PMID: 18635885]
3.  Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H. and Yamamoto, K. Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biol. Chem. 280 (2005) 37415–37422. [DOI] [PMID: 16141207]
4.  Suzuki, R., Katayama, T., Kitaoka, M., Kumagai, H., Wakagi, T., Shoun, H., Ashida, H., Yamamoto, K. and Fushinobu, S. Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J. Biochem. 146 (2009) 389–398. [DOI] [PMID: 19502354]
5.  Gregg, K.J. and Boraston, A.B. Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 133–135. [DOI] [PMID: 19194003]
6.  Ashida, H., Yamamoto, K., Murata, T., Usui, T. and Kumagai, H. Characterization of endo-α-N-acetylgalactosaminidase from Bacillus sp. and syntheses of neo-oligosaccharides using its transglycosylation activity. Arch. Biochem. Biophys. 373 (2000) 394–400. [DOI] [PMID: 10620364]
7.  Goda, H.M., Ushigusa, K., Ito, H., Okino, N., Narimatsu, H. and Ito, M. Molecular cloning, expression, and characterization of a novel endo-α-N-acetylgalactosaminidase from Enterococcus faecalis. Biochem. Biophys. Res. Commun. 375 (2008) 441–446. [DOI] [PMID: 18725192]
[EC 3.2.1.97 created 1978 (EC 3.2.1.110 created 1984, incorporated 2008), modified 2008, modified 2011]
 
 
EC 3.2.1.106     
Accepted name: mannosyl-oligosaccharide glucosidase
Reaction: Glc3Man9GlcNAc2-[protein] + H2O = Glc2Man9GlcNAc2-[protein] + β-D-glucopyranose
Glossary: Glc3Man9GlcNAc2 = [α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Glc2Man9GlcNAc2-[protein] = [α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Other name(s): Glc3Man9NAc2 oligosaccharide glucosidase; trimming glucosidase I; CWH41 (gene name); MOGS (gene name); mannosyl-oligosaccharide glucohydrolase
Systematic name: Glc3Man9GlcNAc2-[protein] glucohydrolase (configuration-inverting)
Comments: This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal α-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78413-07-7
References:
1.  Elting, J.J., Chen, W.W. and Lennarz, J. Characterization of a glucosidase involved in an initial step in the processing of oligosaccharide chains. J. Biol. Chem. 255 (1980) 2325–2331. [PMID: 7358674]
2.  Grinna, L.S. and Robbins, P.W. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J. Biol. Chem. 254 (1979) 8814–8818. [PMID: 479161]
3.  Kilker, R.D., Saunier, B., Tkacz, J.S. and Herscovics, A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem. 256 (1981) 5299–5603. [PMID: 7014569]
4.  Grinna, L.S. and Robbins, P.W. Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255 (1980) 2255–2258. [PMID: 7358666]
5.  Mark, M.J. and Kornfeld, S. Partial purification and characterization of the glucosidases involved in the processing of asparagine-linked oligosaccharides. Arch. Biochem. Biophys. 199 (1980) 249–258. [DOI] [PMID: 7356331]
[EC 3.2.1.106 created 1984, modified 2018]
 
 
EC 3.2.1.113     
Accepted name: mannosyl-oligosaccharide 1,2-α-mannosidase
Reaction: (1) Man9GlcNAc2-[protein] + 4 H2O = Man5GlcNAc2-[protein] + 4 β-D-mannopyranose (overall reaction)
(1a) Man9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + β-D-mannopyranose
(1b) Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + H2O = Man7GlcNAc2-[protein] (isomer 7A1,2,3B2) + β-D-mannopyranose
(1c) Man7GlcNAc2-[protein] (isomer 7A1,2,3B2) + H2O = Man6GlcNAc2-[protein] (isomer 6A1,2B2) + β-D-mannopyranose
(1d) Man6GlcNAc2-[protein] (isomer 6A1,2B2) + H2O = Man5GlcNAc2-[protein] + β-D-mannopyranose
(2) Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + 3 H2O = Man5GlcNAc2-[protein] + 3 β-D-mannopyranose (overall reaction)
(2a) Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + H2O = Man7GlcNAc2-[protein] (isomer 7A1,2,3B1) + β-D-mannopyranose
(2b) Man7GlcNAc2-[protein] (isomer 7A1,2,3B1) + H2O = Man6GlcNAc2-[protein] (isomer 6A1,2,3) + β-D-mannopyranose
(2c) Man6GlcNAc2-[protein] (isomer 6A1,2,3) + H2O = Man5GlcNAc2-[protein] + β-D-mannopyranose
Glossary: Man9GlcNAc2-[protein] = [α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) = [α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Man5GlcNAc2-[protein] = [α-D-Man-(1→3)-{α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Other name(s): mannosidase 1A; mannosidase 1B; 1,2-α-mannosidase; exo-α-1,2-mannanase; mannose-9 processing α-mannosidase; glycoprotein processing mannosidase I; mannosidase I; Man9-mannosidase; ManI; 1,2-α-mannosyl-oligosaccharide α-D-mannohydrolase; MAN1A1 (gene name); MAN1A2 (gene name); MAN1C1 (gene name); 2-α-mannosyl-oligosaccharide α-D-mannohydrolase
Systematic name: Man9GlcNAc2-[protein] α-2-mannohydrolase (configuration-inverting)
Comments: This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1→2)-linked α-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-α-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-25-1
References:
1.  Tabas, I. and Kornfeld, S. Purification and characterization of a rat liver Golgi α-mannosidase capable of processing asparagine-linked oligosaccharides. J. Biol. Chem. 254 (1979) 11655–11663. [PMID: 500665]
2.  Tulsiani, D.R.P., Hubbard, S.C., Robbins, P.W. and Touster, O. α-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and mannosidases IA and IB are the enzymes converting Man9 precursors to Man5 intermediates. J. Biol. Chem. 257 (1982) 3660–3668. [PMID: 7061502]
3.  Bieberich, E. and Bause, E. Man9-mannosidase from human kidney is expressed in COS cells as a Golgi-resident type II transmembrane N-glycoprotein. Eur. J. Biochem. 233 (1995) 644–649. [PMID: 7588811]
4.  Tremblay, L.O., Campbell Dyke, N. and Herscovics, A. Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human α1,2-mannosidase gene involved in N-glycan maturation. Glycobiology 8 (1998) 585–595. [PMID: 9592125]
5.  Lal, A., Pang, P., Kalelkar, S., Romero, P.A., Herscovics, A. and Moremen, K.W. Substrate specificities of recombinant murine Golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing α1,2-mannosidases. Glycobiology 8 (1998) 981–995. [PMID: 9719679]
6.  Tremblay, L.O. and Herscovics, A. Characterization of a cDNA encoding a novel human Golgi α 1, 2-mannosidase (IC) involved in N-glycan biosynthesis. J. Biol. Chem. 275 (2000) 31655–31660. [PMID: 10915796]
7.  Prien, J.M., Ashline, D.J., Lapadula, A.J., Zhang, H. and Reinhold, V.N. The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS. J. Am. Soc. Mass Spectrom. 20 (2009) 539–556. [DOI] [PMID: 19181540]
[EC 3.2.1.113 created 1986, modified 2019]
 
 
EC 3.2.1.114     
Accepted name: mannosyl-oligosaccharide 1,3-1,6-α-mannosidase
Reaction: Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 α-D-mannopyranose
For diagram of mannosyl-glycoprotein n-acetylglucosaminyltransferases, click here
Glossary: Man5GlcNAc3-[protein] = [β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-{α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)}-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc]-N-Asn-[protein]
Man3GlcNAc3-[protein] = {β-D-GlcNAc-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc}-N-Asn-[protein]
Other name(s): MAN2A1 (gene name); MAN2A2 (gene name); mannosidase II; exo-1,3-1,6-α-mannosidase; α-D-mannosidase II; α-mannosidase II; α1-3,6-mannosidase; GlcNAc transferase I-dependent α1,3[α1,6]mannosidase; Golgi α-mannosidase II; ManII; 1,3(1,6)-α-D-mannosidase; 1,3-(1,6-)mannosyl-oligosaccharide α-D-mannohydrolase; (1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase
Systematic name: (1→3)-(1→6)-mannosyl-oligosaccharide α-D-mannohydrolase (configuration-retaining)
Comments: The enzyme, found in plants and animals, participates in the processing of N-glycans in the Golgi apparatus. It removes two mannosyl residues, one linked by α1,3 linkage, and the other linked by α1,6 linkage, both of which are removed by the same catalytic site. The enzyme is sensitive to swainsonine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82047-77-6
References:
1.  Tulsiani, D.R.P., Opheim, D.J. and Touster, O. Purification and characterization of α-D-mannosidase from rat liver golgi membranes. J. Biol. Chem. 252 (1977) 3227–3233. [PMID: 863880]
2.  Tabas, I. and Kornfeld, S. The synthesis of complex-type oligosaccharides. III. Identification of an α-D-mannosidase activity involved in a late stage of processing of complex-type oligosaccharides. J. Biol. Chem. 253 (1978) 7779–7786. [PMID: 212436]
3.  Harpaz, N. and Schachter, H. Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi α-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: α-D-mannoside β2-N-acetylglucosaminyltransferase I. J. Biol. Chem. 255 (1980) 4894–4902. [PMID: 6445359]
4.  Tulsiani, D.R.P., Hubbard, S.C., Robbins, P.W. and Touster, O. α-D-Mannosidases of rat liver Golgi membranes. Mannosidase II is the GlcNAcMAN5-cleaving enzyme in glycoprotein biosynthesis and mannosidases IA and IB are the enzymes converting Man9 precursors to Man5 intermediates. J. Biol. Chem. 257 (1982) 3660–3668. [PMID: 7061502]
5.  Moremen, K.W. and Robbins, P.W. Isolation, characterization, and expression of cDNAs encoding murine α-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans. J. Cell Biol. 115 (1991) 1521–1534. [PMID: 1757461]
6.  Misago, M., Liao, Y.F., Kudo, S., Eto, S., Mattei, M.G., Moremen, K.W. and Fukuda, M.N. Molecular cloning and expression of cDNAs encoding human α-mannosidase II and a previously unrecognized α-mannosidase IIx isozyme. Proc. Natl. Acad. Sci. USA 92 (1995) 11766–11770. [DOI] [PMID: 8524845]
7.  van den Elsen, J.M., Kuntz, D.A. and Rose, D.R. Structure of Golgi α-mannosidase II: a target for inhibition of growth and metastasis of cancer cells. EMBO J. 20 (2001) 3008–3017. [DOI] [PMID: 11406577]
8.  Athanasopoulos, V.I., Niranjan, K. and Rastall, R.A. The production, purification and characterisation of two novel α-D-mannosidases from Aspergillus phoenicis. Carbohydr. Res. 340 (2005) 609–617. [DOI] [PMID: 15721331]
9.  Shah, N., Kuntz, D.A. and Rose, D.R. Golgi α-mannosidase II cleaves two sugars sequentially in the same catalytic site. Proc. Natl. Acad. Sci. USA 105 (2008) 9570–9575. [DOI] [PMID: 18599462]
10.  Rose, D.R. Structure, mechanism and inhibition of Golgi α-mannosidase II. Curr. Opin. Struct. Biol. 22 (2012) 558–562. [DOI] [PMID: 22819743]
[EC 3.2.1.114 created 1986, modified 2018]
 
 
EC 3.2.1.130     
Accepted name: glycoprotein endo-α-1,2-mannosidase
Reaction: GlcMan9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) + α-D-glucosyl-(1→3)-α-D-mannopyranose
Glossary: GlcMan9GlcNAc2-[protein] = {α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc}-N-Asn-[protein]
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,2) = {α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc}-N-Asn-[protein]
Other name(s): glucosylmannosidase; endo-α-D-mannosidase; endo-α-mannosidase; endomannosidase; glucosyl mannosidase; MANEA (gene name); glycoprotein glucosylmannohydrolase
Systematic name: glycoprotein glucosylmannohydrolase (configuration-retaining)
Comments: The enzyme catalyses the hydrolysis of the terminal α-D-glucosyl-(1→3)-D-mannosyl unit from the GlcMan9(GlcNAc)2 oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus. The name for the isomer is based on a nomenclature proposed by Prien et al [7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 108022-16-8
References:
1.  Lubas, W.A. and Spiro, R.G. Golgi endo-α-D-mannosidase from rat liver, a novel N-linked carbohydrate unit processing enzyme. J. Biol. Chem. 262 (1987) 3775–3781. [PMID: 3818665]
2.  Tulsiani, D.R.P., Coleman, V.P. and Touster, O. Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and endomannosidase (glucosyl mannosidase). Arch. Biochem. Biophys. 277 (1990) 114–121. [DOI] [PMID: 2407194]
3.  Hiraizumi, S., Spohr, U. and Spiro, R.G. Ligand affinity chromatographic purification of rat liver Golgi endomannosidase. J. Biol. Chem. 269 (1994) 4697–4700. [PMID: 8106437]
4.  Spiro, M.J., Bhoyroo, V.D. and Spiro, R.G. Molecular cloning and expression of rat liver endo-α-mannosidase, an N-linked oligosaccharide processing enzyme. J. Biol. Chem. 272 (1997) 29356–29363. [DOI] [PMID: 9361017]
5.  Hamilton, S.R., Li, H., Wischnewski, H., Prasad, A., Kerley-Hamilton, J.S., Mitchell, T., Walling, A.J., Davidson, R.C., Wildt, S. and Gerngross, T.U. Intact α-1,2-endomannosidase is a typical type II membrane protein. Glycobiology 15 (2005) 615–624. [DOI] [PMID: 15677381]
6.  Hardt, B., Volker, C., Mundt, S., Salska-Navarro, M., Hauptmann, M. and Bause, E. Human endo-α1,2-mannosidase is a Golgi-resident type II membrane protein. Biochimie 87 (2005) 169–179. [DOI] [PMID: 15760709]
7.  Prien, J.M., Ashline, D.J., Lapadula, A.J., Zhang, H. and Reinhold, V.N. The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS. J. Am. Soc. Mass Spectrom. 20 (2009) 539–556. [DOI] [PMID: 19181540]
[EC 3.2.1.130 created 1990, modified 2017]
 
 
EC 3.2.1.132     
Accepted name: chitosanase
Reaction: Endohydrolysis of β-(1→4)-linkages between D-glucosamine residues in a partly acetylated chitosan
Systematic name: chitosan N-acetylglucosaminohydrolase
Comments: A whole spectrum of chitosanases are now known (for more details, see http://rbrzezinski.recherche.usherbrooke.ca/). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition [4], while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51570-20-8
References:
1.  Fenton, D.M. and Eveleigh, D.E. Purification and mode of action of a chitosanase from Penicillium islandicum. J. Gen. Microbiol. 126 (1981) 151–165.
2.  Saito, J.-I., Kita, A., Higuchi, Y., Nagata, Y., Ando, A. and Miki, K. Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-Å resolution and its substrate recognition mechanism. J. Biol. Chem. 274 (1999) 30818–30825. [DOI] [PMID: 10521473]
3.  Izume, M., Nagae, S., Kawagishi, H., Mitsutomi, M. and Ohtakara, A. Action pattern of Bacillus sp. No. 7-M chitosanase on partially N-acetylated chitosan. Biosci. Biotechnol. Biochem. 56 (1992) 448–453. [DOI] [PMID: 1368330]
4.  Marcotte, E.M., Monzingo, A.F., Ernst, S.R., Brzezinski, R. and Robertus, J.D. X-ray structure of an anti-fungal chitosanase from Streptomyces N174. Nat. Struct. Biol. 3 (1996) 155–162. [PMID: 8564542]
[EC 3.2.1.132 created 1990, modified 2004]
 
 
EC 3.2.1.140     
Accepted name: lacto-N-biosidase
Reaction: β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc + H2O = β-D-Gal-(1→3)-D-GlcNAc + β-D-Gal-(1→4)-D-Glc
Glossary: β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc = lacto-N-tetraose
β-D-Gal-(1→3)-D-GlcNAc = lacto-N-biose
β-D-Gal-(1→4)-D-Glc = lactose
Systematic name: oligosaccharide lacto-N-biosylhydrolase
Comments: The enzyme from Streptomyces specifically hydrolyses the terminal lacto-N-biosyl residue (β-D-Gal-(1→3)-D-GlcNAc) from the non-reducing end of oligosaccharides with the structure β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→R). Lacto-N-hexaose (β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→3)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is hydrolysed to form first lacto-N-tetraose plus lacto-N-biose, with the subsequent formation of lactose. Oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are not substrates. Asialo GM1 tetraose (β-D-Gal-(1→3)-β-D-GalNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is hydrolysed very slowly, but lacto-N-neotetraose (β-D-Gal-(1→4)-β-D-GalNAc-(1→3)-β-D-Gal-(1→4)-D-Glc) is not a substrate
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 146359-52-6
References:
1.  Sano, M., Hayakawa, K., Kato, I. An enzyme releasing lacto-N-biose from oligosaccharides. Proc. Natl. Acad. Sci. USA 89 (1992) 8512–8516. [DOI] [PMID: 1528855]
2.  Sano, M., Hayakawa, K., Kato, I. Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain. J. Biol. Chem. 268 (1993) 18560–18566. [PMID: 7689556]
[EC 3.2.1.140 created 1999]
 
 
EC 3.2.1.165     
Accepted name: exo-1,4-β-D-glucosaminidase
Reaction: Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini
Glossary: GlcN = D-glucosamine = 2-amino-2-deoxy-D-glucopyranose
GlcNAc = N-acetyl-D-glucosamine
Other name(s): CsxA; GlcNase; exochitosanase; GlmA; exo-β-D-glucosaminidase; chitosan exo-1,4-β-D-glucosaminidase
Systematic name: chitosan exo-(1→4)-β-D-glucosaminidase
Comments: Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues [4]. Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols [1]. The enzyme can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc [3]. A member of the glycoside hydrolase family 2 (GH-2) [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nanjo, F., Katsumi, R. and Sakai, K. Purification and characterization of an exo-β-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis. J. Biol. Chem. 265 (1990) 10088–10094. [PMID: 2351651]
2.  Nogawa, M., Takahashi, H., Kashiwagi, A., Ohshima, K., Okada, H. and Morikawa, Y. Purification and characterization of exo-β-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7. Appl. Environ. Microbiol. 64 (1998) 890–895. [PMID: 16349528]
3.  Fukamizo, T., Fleury, A., Côté, N., Mitsutomi, M. and Brzezinski, R. Exo-β-D-glucosaminidase from Amycolatopsis orientalis: catalytic residues, sugar recognition specificity, kinetics, and synergism. Glycobiology 16 (2006) 1064–1072. [DOI] [PMID: 16877749]
4.  Côté, N., Fleury, A., Dumont-Blanchette, E., Fukamizo, T., Mitsutomi, M. and Brzezinski, R. Two exo-β-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem. J. 394 (2006) 675–686. [DOI] [PMID: 16316314]
5.  Ike, M., Isami, K., Tanabe, Y., Nogawa, M., Ogasawara, W., Okada, H. and Morikawa, Y. Cloning and heterologous expression of the exo-β-D-glucosaminidase-encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7. Appl. Microbiol. Biotechnol. 72 (2006) 687–695. [DOI] [PMID: 16636831]
[EC 3.2.1.165 created 2008]
 
 
EC 3.2.1.169     
Accepted name: protein O-GlcNAcase
Reaction: (1) [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine
(2) [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-theronine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine
Other name(s): OGA; glycoside hydrolase O-GlcNAcase; O-GlcNAcase; BtGH84; O-GlcNAc hydrolase
Systematic name: [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase
Comments: Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gao, Y., Wells, L., Comer, F.I., Parker, G.J. and Hart, G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic β-N-acetylglucosaminidase from human brain. J. Biol. Chem. 276 (2001) 9838–9845. [DOI] [PMID: 11148210]
2.  Wells, L., Gao, Y., Mahoney, J.A., Vosseller, K., Chen, C., Rosen, A. and Hart, G.W. Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase. J. Biol. Chem. 277 (2002) 1755–1761. [PMID: 11788610]
3.  Cetinbas, N., Macauley, M.S., Stubbs, K.A., Drapala, R. and Vocadlo, D.J. Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. Biochemistry 45 (2006) 3835–3844. [DOI] [PMID: 16533067]
4.  Dennis, R.J., Taylor, E.J., Macauley, M.S., Stubbs, K.A., Turkenburg, J.P., Hart, S.J., Black, G.N., Vocadlo, D.J. and Davies, G.J. Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity. Nat. Struct. Mol. Biol. 13 (2006) 365–371. [DOI] [PMID: 16565725]
5.  Kim, E.J., Kang, D.O., Love, D.C. and Hanover, J.A. Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate. Carbohydr. Res. 341 (2006) 971–982. [DOI] [PMID: 16584714]
6.  Dong, D.L. and Hart, G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-β-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269 (1994) 19321–19330. [PMID: 8034696]
[EC 3.2.1.169 created 2011]
 
 
EC 3.2.1.179     
Accepted name: gellan tetrasaccharide unsaturated glucuronosyl hydrolase
Reaction: β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp + H2O = 5-dehydro-4-deoxy-D-glucuronate + β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp
Glossary: 5-dehydro-4-deoxy-D-glucuronate = (4S,5R)-4,5-dihydroxy-2,6-dioxohexanoate
β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc = 3-(4-deoxy-β-D-gluc-4-enuronosyl)-N-acetyl-D-galactosamine = 3-(4-deoxy-α-L-threo-hex-4-enopyranosyluronic acid)-2-acetamido-2-deoxy-D-galactose
Other name(s): UGL (ambiguous); unsaturated glucuronyl hydrolase (ambiguous); gellan tetrasaccharide unsaturated glucuronyl hydrolase
Systematic name: β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp β-D-4-deoxy-Δ4-GlcAp hydrolase
Comments: The enzyme releases 4-deoxy-4(5)-unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases, e.g. the tetrasaccharide β-D-4-deoxy-Δ4-GlcAp-(1→4)-β-D-Glcp-(1→4)-α-L-Rhap-(1→3)-D-Glcp produced by EC 4.2.2.25, gellan lyase. The enzyme can also hydrolyse unsaturated chondroitin and hyaluronate disaccharides (β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc, β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GalNAc6S, β-D-4-deoxy-Δ4-GlcAp2S-(1→3)-D-GalNAc, β-D-4-deoxy-Δ4-GlcAp-(1→3)-D-GlcNAc), preferring the unsulfated disaccharides to the sulfated disaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Itoh, T., Akao, S., Hashimoto, W., Mikami, B. and Murata, K. Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å resolution. J. Biol. Chem. 279 (2004) 31804–31812. [DOI] [PMID: 15148314]
2.  Hashimoto, W., Kobayashi, E., Nankai, H., Sato, N., Miya, T., Kawai, S. and Murata, K. Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch. Biochem. Biophys. 368 (1999) 367–374. [DOI] [PMID: 10441389]
3.  Itoh, T., Hashimoto, W., Mikami, B. and Murata, K. Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1. Biochem. Biophys. Res. Commun. 344 (2006) 253–262. [DOI] [PMID: 16630576]
[EC 3.2.1.179 created 2011, modified 2016]
 
 


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