The Enzyme Database

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EC 2.3.1.251     
Accepted name: lipid IVA palmitoyltransferase
Reaction: (1) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
(2) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IIA = 2-acyl-sn-glycero-3-phosphocholine + lipid IIB
(3) 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + lipid IVA = 2-acyl-sn-glycero-3-phosphocholine + lipid IVB
For diagram of lipid IVB biosynthesis, click here
Glossary: palmitoyl = hexadecanoyl
hexa-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranosyl phosphate
hepta-acyl lipid A = 2-deoxy-2-[(3R)-3-(tetradecanoyloxy)tetradecanamido]-3-O-[(3R)-3-(dodecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IIB = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
lipid IVA = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-hydroxytetradecanamido]-α-D-glucopyranose phosphate
lipid IVB = 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[(3R)-3-(hexadecanoyloxy)tetradecanamido]-α-D-glucopyranosyl phosphate
Other name(s): PagP; crcA (gene name)
Systematic name: 1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine:lipid-IVA palmitoyltransferase
Comments: Isolated from the bacteria Escherichia coli and Salmonella typhimurium. The enzyme prefers phosphatidylcholine with a palmitoyl group at the sn-1 position and palmitoyl or stearoyl groups at the sn-2 position. There is some activity with corresponding phosphatidylserines but only weak activity with other diacylphosphatidyl compounds. The enzyme also acts on Kdo-(2→4)-Kdo-(2→6)-lipid IVA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I. and Raetz, C.R. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19 (2000) 5071–5080. [DOI] [PMID: 11013210]
2.  Cuesta-Seijo, J.A., Neale, C., Khan, M.A., Moktar, J., Tran, C.D., Bishop, R.E., Pomes, R. and Prive, G.G. PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure 18 (2010) 1210–1219. [DOI] [PMID: 20826347]
[EC 2.3.1.251 created 2015]
 
 
EC 2.3.2.16     
Accepted name: lipid II:glycine glycyltransferase
Reaction: MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
Other name(s): N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase; femX (gene name); alanyl-D-alanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase
Systematic name: MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine N6-glycyltransferase
Comments: The enzyme from Staphylococcus aureus catalyses the transfer of glycine from a charged tRNA to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc (lipid II), attaching it to the N6 of the L-Lys at position 3 of the pentapeptide. This is the first step in the synthesis of the pentaglycine interpeptide bridge that is used in S. aureus for the crosslinking of different glycan strands to each other. Four additional Gly residues are subsequently attached by EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase) and EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675–685. [DOI] [PMID: 15228543]
[EC 2.3.2.16 created 2010]
 
 
EC 2.3.2.17     
Accepted name: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Reaction: MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly
Other name(s): femA (gene name); N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Systematic name: MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine glycyltransferase
Comments: This enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to a Gly residue previously attached by EC 2.3.2.16 (lipid II:glycine glycyltransferase) to the N6 of the L-Lys at position 3 of the pentapeptide. This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the crosslinking of different glycan strands to each other. The next step is catalysed by EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This enzyme is essential for methicillin resistance [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Berger-Bachi, B., Barberis-Maino, L., Strassle, A. and Kayser, F.H. FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization. Mol. Gen. Genet. 219 (1989) 263–269. [PMID: 2559314]
2.  Johnson, S., Kruger, D. and Labischinski, H. FemA of Staphylococcus aureus: isolation and immunodetection. FEMS Microbiol. Lett. 132 (1995) 221–228. [DOI] [PMID: 7590176]
3.  Benson, T.E., Prince, D.B., Mutchler, V.T., Curry, K.A., Ho, A.M., Sarver, R.W., Hagadorn, J.C., Choi, G.H. and Garlick, R.L. X-ray crystal structure of Staphylococcus aureus FemA. Structure 10 (2002) 1107–1115. [DOI] [PMID: 12176388]
4.  Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675–685. [DOI] [PMID: 15228543]
[EC 2.3.2.17 created 2010]
 
 
EC 2.3.2.18     
Accepted name: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Reaction: MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly
Other name(s): femB (gene name); N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Systematic name: MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine glycyltransferase
Comments: This Staphylococcus aureus enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc, attaching them to the three Gly molecules that were previously attached to the N6 of the L-Lys at position 3 of the pentapeptide by EC 2.3.2.16 (lipid II:glycine glycyltransferase) and EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This is the last step in the synthesis of the pentaglycine interpeptide bridge that is used in this organism for the crosslinking of different glycan strands to each other.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ehlert, K., Schroder, W. and Labischinski, H. Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol. 179 (1997) 7573–7576. [DOI] [PMID: 9393725]
2.  Rohrer, S. and Berger-Bachi, B. Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins. Microbiology 149 (2003) 2733–2738. [DOI] [PMID: 14523106]
3.  Schneider, T., Senn, M.M., Berger-Bachi, B., Tossi, A., Sahl, H.G. and Wiedemann, I. In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus. Mol. Microbiol. 53 (2004) 675–685. [DOI] [PMID: 15228543]
[EC 2.3.2.18 created 2010]
 
 
EC 2.4.1.325     
Accepted name: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Reaction: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)
Systematic name: dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase
Comments: Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509–6516. [DOI] [PMID: 11673418]
[EC 2.4.1.325 created 2014]
 
 
EC 2.4.2.43     
Accepted name: lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
Reaction: (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-α-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate
For diagram of lipid IIA biosynthesis, click here
Glossary: lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4′-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
Other name(s): undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK; arnT (gene name)
Systematic name: 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl-phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase
Comments: Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122–43131. [DOI] [PMID: 11535604]
2.  Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132–43144. [DOI] [PMID: 11535605]
3.  Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111–43121. [DOI] [PMID: 11535603]
4.  Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33–39. [DOI] [PMID: 16226890]
5.  Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29–35. [DOI] [PMID: 19947657]
[EC 2.4.2.43 created 2010, modified 2011]
 
 
EC 2.7.8.12     
Accepted name: teichoic acid poly(glycerol phosphate) polymerase
Reaction: n CDP-glycerol + 4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): teichoic-acid synthase; cytidine diphosphoglycerol glycerophosphotransferase; poly(glycerol phosphate) polymerase; teichoic acid glycerol transferase; glycerophosphate synthetase; CGPTase; CDP-glycerol glycerophosphotransferase (ambiguous); Tag polymerase; CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase; tagF (gene name); tarF (gene name) (ambiguous)
Systematic name: CDP-glycerol:4-O-[(2R)-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Comments: Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30–50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, teichoic acid glycerol-phosphate transferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-71-5
References:
1.  Burger, M.M. and Glaser, L. The synthesis of teichoic acids. I. Polyglycerophosphate. J. Biol. Chem. 239 (1964) 3168–3177. [PMID: 14245357]
2.  Schertzer, J.W. and Brown, E.D. Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes the polymerization of glycerol phosphate onto a membrane acceptor in vitro. J. Biol. Chem. 278 (2003) 18002–18007. [DOI] [PMID: 12637499]
3.  Schertzer, J.W., Bhavsar, A.P. and Brown, E.D. Two conserved histidine residues are critical to the function of the TagF-like family of enzymes. J. Biol. Chem. 280 (2005) 36683–36690. [DOI] [PMID: 16141206]
4.  Pereira, M.P., Schertzer, J.W., D'Elia, M.A., Koteva, K.P., Hughes, D.W., Wright, G.D. and Brown, E.D. The wall teichoic acid polymerase TagF efficiently synthesizes poly(glycerol phosphate) on the TagB product lipid III. ChemBioChem 9 (2008) 1385–1390. [DOI] [PMID: 18465758]
5.  Sewell, E.W., Pereira, M.P. and Brown, E.D. The wall teichoic acid polymerase TagF is non-processive in vitro and amenable to study using steady state kinetic analysis. J. Biol. Chem. 284 (2009) 21132–21138. [DOI] [PMID: 19520862]
6.  Lovering, A.L., Lin, L.Y., Sewell, E.W., Spreter, T., Brown, E.D. and Strynadka, N.C. Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis. Nat. Struct. Mol. Biol. 17 (2010) 582–589. [DOI] [PMID: 20400947]
7.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.12 created 1972, modified 1982, modified 2017]
 
 
EC 6.3.5.13     
Accepted name: lipid II isoglutaminyl synthase (glutamine-hydrolysing)
Reaction: ATP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol + L-glutamine + H2O = ADP + phosphate + β-D-GlcNAc-(1→4)-MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenol + L-glutamate (overall reaction)
(1a) L-glutamine + H2O = L-glutamate + NH3
(1b) ATP + β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol = ADP + β-D-GlcNAc-(1→4)-MurNAc-L-Ala-γ-D-O-P-Glu-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenol
(1c) β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-O-P-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol + NH3 = β-D-GlcNAc-(1→4)-MurNAc-L-Ala-D-isoglutaminyl-L-Lys-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenol + phosphate
Glossary: lipid II = undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
Other name(s): MurT/GatD; MurT/GatD complex
Systematic name: β-D-GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-ditrans,octacis-undecaprenol:L-glutamine amidoligase (ADP-forming)
Comments: The enzyme complex, found in Gram-positive bacteria, consists of two subunits. A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is channeled to a ligase subunit, which adds it to the activated D-glutamate residue of lipid II, converting it to an isoglutamine residue.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Munch, D., Roemer, T., Lee, S.H., Engeser, M., Sahl, H.G. and Schneider, T. Identification and in vitro analysis of the GatD/MurT enzyme-complex catalyzing lipid II amidation in Staphylococcus aureus. PLoS Pathog. 8:e1002509 (2012). [PMID: 22291598]
2.  Noldeke, E.R., Muckenfuss, L.M., Niemann, V., Muller, A., Stork, E., Zocher, G., Schneider, T. and Stehle, T. Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus. Sci. Rep. 8:12953 (2018). [PMID: 30154570]
3.  Morlot, C., Straume, D., Peters, K., Hegnar, O.A., Simon, N., Villard, A.M., Contreras-Martel, C., Leisico, F., Breukink, E., Gravier-Pelletier, C., Le Corre, L., Vollmer, W., Pietrancosta, N., Havarstein, L.S. and Zapun, A. Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae. Nat. Commun. 9:3180 (2018). [PMID: 30093673]
[EC 6.3.5.13 created 2019]
 
 


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