The Enzyme Database

Displaying entries 101-150 of 1139.

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EC 3.2.1.53     Relevance: 100%
Accepted name: β-N-acetylgalactosaminidase
Reaction: Hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-β-D-galactosaminides
Other name(s): N-acetyl-β-galactosaminidase; N-acetyl-β-D-galactosaminidase; β-acetylgalactosaminidase; β-D-N-acetylgalactosaminidase; N-acetylgalactosaminidase
Systematic name: β-N-acetyl-D-galactosaminide N-acetylgalactosaminohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-43-7
References:
1.  Frohwein, Y.S. and Gatt, S. Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain. Biochemistry 6 (1967) 2775–2782. [PMID: 6055190]
2.  Hoogwinkel, G.J.M., Veltkamp, W.A., Overdijk, B. and Lisman, J.W. Electrophoretic separation of β-N-acetylhexosaminidases of human and bovine brain and liver and of Tay-Sachs brain tissue. Hoppe-Seylers Z. Physiol. Chem. 353 (1972) 839–841. [PMID: 5069351]
[EC 3.2.1.53 created 1972]
 
 
EC 3.2.1.209     Relevance: 99.9%
Accepted name: endoplasmic reticulum Man9GlcNAc2 1,2-α-mannosidase
Reaction: Man9GlcNAc2-[protein] + H2O = Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + 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)-α-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)-α-D-GlcNAc}-N-Asn-[protein]
Other name(s): MAN1B1 (gene name); MNS1 (gene name); MNS3 (gene name)
Systematic name: Man9GlcNAc2-[protein]2-α-mannohydrolase (configuration-inverting)
Comments: The enzyme, located in the endoplasmic reticulum, primarily trims a single α-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7]). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jelinek-Kelly, S. and Herscovics, A. Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the α-mannosidase which removes one specific mannose residue from Man9GlcNAc. J. Biol. Chem. 263 (1988) 14757–14763. [PMID: 3049586]
2.  Ziegler, F.D. and Trimble, R.B. Glycoprotein biosynthesis in yeast: purification and characterization of the endoplasmic reticulum Man9 processing α-mannosidase. Glycobiology 1 (1991) 605–614. [PMID: 1822240]
3.  Gonzalez, D.S., Karaveg, K., Vandersall-Nairn, A.S., Lal, A. and Moremen, K.W. Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J. Biol. Chem. 274 (1999) 21375–21386. [PMID: 10409699]
4.  Herscovics, A., Romero, P.A. and Tremblay, L.O. The specificity of the yeast and human class I ER α 1,2-mannosidases involved in ER quality control is not as strict previously reported. Glycobiology 12 (2002) 14G–15G. [PMID: 12090241]
5.  Avezov, E., Frenkel, Z., Ehrlich, M., Herscovics, A. and Lederkremer, G.Z. Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol. Biol. Cell 19 (2008) 216–225. [PMID: 18003979]
6.  Liebminger, E., Huttner, S., Vavra, U., Fischl, R., Schoberer, J., Grass, J., Blaukopf, C., Seifert, G.J., Altmann, F., Mach, L. and Strasser, R. Class I α-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana. Plant Cell 21 (2009) 3850–3867. [PMID: 20023195]
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 3.2.1.209 created 2019]
 
 
EC 3.2.1.179     Relevance: 99.8%
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]
 
 
EC 3.2.1.146     Relevance: 99.6%
Accepted name: β-galactofuranosidase
Reaction: Hydrolysis of terminal non-reducing β-D-galactofuranosides, releasing galactose
Other name(s): exo-β-galactofuranosidase; exo-β-D-galactofuranosidase; β-D-galactofuranosidase
Systematic name: β-D-galactofuranoside hydrolase
Comments: The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52357-57-0
References:
1.  Rietschel-Berst, M., Jentoft, N.H., Rick, P.D., Pletcher, C., Fang, F. and Gander, J.E. Extracellular exo-β-galactofuranosidase from Penicillium charlesii: isolation, purification, and properties. J. Biol. Chem. 252 (1977) 3219–3226. [PMID: 863879]
2.  Daley, L.S. and Strobel, G.A. β-Galactofuranosidase activity in Helminthosporium sacchari and its relationship to the production of helminthosporoside. Plant Sci. Lett. 30 (1983) 145–154.
3.  Cousin, M.A., Notermans, S., Hoogerhout, P. and Van Boom, J.H. Detection of β-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl β-D-galactofuranoside. J. Appl. Bacteriol. 66 (1989) 311–317. [PMID: 2502527]
4.  Miletti, L.C., Marino, C., Marino, K., de Lederkremer, R.M., Colli, W. and Alves, M.J.M. Immobilized 4-aminophenyl-1-thio-β-D-galactofuranoside as a matrix for affinity purification of an exo-β-D-galactofuranosidase. Carbohydr. Res. 320 (1999) 176–182. [DOI] [PMID: 10573856]
[EC 3.2.1.146 created 2001]
 
 
EC 2.4.99.2      
Transferred entry: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase. Now EC 2.4.3.2, β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
[EC 2.4.99.2 created 1976, modified 1986, deleted 2022]
 
 
EC 2.4.3.2     Relevance: 99%
Accepted name: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R = CMP + an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R
For diagram of ganglioside biosynthesis, click here
Glossary: a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[N-acetyl-α-neuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GD1a
Other name(s): CMP-N-acetylneuraminate:D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-(1↔1)-ceramide N-acetylneuraminyltransferase (ambiguous); monosialoganglioside sialyltransferase; CMP-N-acetylneuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide N-acetyl-β-neuraminyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-R α-(2→3)-N-acetylneuraminyltransferase (configuration-inverting)
Comments: The enzyme recognizes the sequence β-D-galactosyl-(1→3)-N-acetyl-D-galactosaminyl (known as type 1 histo-blood group precursor disaccharide) in non-reducing termini of glycan moieties in glycoproteins and glycolipids [1]. When acting on gangloside GM1a, it forms gangloside GD1a [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60202-12-2
References:
1.  Rearick, J.I., Sadler, J.E., Paulson, J.C. and Hill, R.L. Enzymatic characterization of β D-galactoside α2→3 sialyltransferase from porcine submaxillary gland. J. Biol. Chem. 254 (1979) 4444–4451. [PMID: 438198]
2.  Yip, M.C.M. The enzymic synthesis of disialoganglioside: rat brain cytidine-5′-monophospho-N-acetylneuraminic acid: monosialoganglioside (GM1) sialyltransferase. Biochim. Biophys. Acta 306 (1973) 298–306. [DOI] [PMID: 4351506]
[EC 2.4.3.2 created 1976 as EC 2.4.99.2, modified 1986, modified 2017, transferred 2022 to EC 2.4.3.2]
 
 
EC 3.2.1.92     Relevance: 98.8%
Accepted name: peptidoglycan β-N-acetylmuramidase
Reaction: Hydrolysis of terminal, non-reducing N-acetylmuramic residues
Other name(s): exo-β-N-acetylmuramidase; exo-β-acetylmuramidase; β-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-D-glucoside acetamidodeoxyglucohydrolase
Systematic name: peptidoglycan β-N-acetylmuramoylexohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52219-03-1
References:
1.  Del Rio, L.A. and Berkeley, R.C.W. Exo-β-N-acetylmuramidase - a novel hexosaminidase. Production by Bacillus subtilis B, purification and characterization. Eur. J. Biochem. 65 (1976) 3–12. [DOI] [PMID: 6281]
[EC 3.2.1.92 created 1976]
 
 
EC 3.2.1.26     Relevance: 98.7%
Accepted name: β-fructofuranosidase
Reaction: Hydrolysis of terminal non-reducing β-D-fructofuranoside residues in β-D-fructofuranosides
Other name(s): invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase
Systematic name: β-D-fructofuranoside fructohydrolase
Comments: Substrates include sucrose; also catalyses fructotransferase reactions.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-57-4
References:
1.  Myrbäck, K. Invertases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 379–396.
2.  Neumann, N.P. and Lampen, J.O. Purification and properties of yeast invertase. Biochemistry 6 (1967) 468–475. [PMID: 4963242]
[EC 3.2.1.26 created 1961]
 
 
EC 1.13.11.67     Relevance: 98.5%
Accepted name: 8′-apo-β-carotenoid 14′,13′-cleaving dioxygenase
Reaction: 8′-apo-β-carotenol + O2 = 14′-apo-β-carotenal + an uncharacterized product
For diagram of 8′-apo-β-carotenal metabolites, click here
Other name(s): 8′-apo-β-carotenol:O2 oxidoreductase (14′,13′-cleaving)
Systematic name: 8′-apo-β-carotenol:oxygen oxidoreductase (14′,13′-cleaving)
Comments: A thiol-dependent enzyme isolated from rat and rabbit. Unlike EC 1.13.11.63, β-carotene-15,15′-dioxygenase, it is not active towards β-carotene. The secondary product has not been characterized, but may be (3E,5E)-7-hydroxy-6-methylhepta-3,5-dien-2-one.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 198028-39-6
References:
1.  Dmitrovskii, A.A., Gessler, N.N., Gomboeva, S.B., Ershov, Yu.V. and Bykhovsky, V.Ya. Enzymatic oxidation of β-apo-8′-carotenol to β-apo-14′-carotenal by an enzyme different from β-carotene-15,15′-dioxygenase. Biochemistry (Mosc.) 62 (1997) 787–792. [PMID: 9331970]
[EC 1.13.11.67 created 2000 as EC 1.13.12.12, transferred 2012 to EC 1.13.11.67]
 
 
EC 3.2.1.214     Relevance: 98.5%
Accepted name: exo β-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)
Reaction: [(1→2)-β-D-glucosyl]n + H2O = sophorose + [(1→2)-β-D-glucosyl]n-2
Glossary: sophorose = β-D-glucopyranosyl-(1→2)-D-glucopyranose
Systematic name: exo (1→2)-β-D-glucooligosaccharide sophorohydrolase (non-reducing end)
Comments: The enzyme, characterized from the bacterium Parabacteroides distasonis, specifically hydrolyses (1→2)-β-D-glucooligosaccharides to sophorose. The best substrates are the tetra- and pentasaccharides. The enzyme is not able to cleave the trisaccharide, and activity with longer linear (1→2)-β-D-glucans is quite low. This enzyme acts in exo mode and is not able to hydrolyse cyclic (1→2)-β-D-glucans.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Shimizu, H., Nakajima, M., Miyanaga, A., Takahashi, Y., Tanaka, N., Kobayashi, K., Sugimoto, N., Nakai, H. and Taguchi, H. Characterization and structural analysis of a novel exo-type enzyme acting on β-1,2-glucooligosaccharides from Parabacteroides distasonis. Biochemistry 57 (2018) 3849–3860. [PMID: 29763309]
[EC 3.2.1.214 created 2020]
 
 
EC 2.4.1.27     Relevance: 98.3%
Accepted name: DNA β-glucosyltransferase
Reaction: Transfers a β-D-glucosyl residue from UDP-α-D-glucose to an hydroxymethylcytosine residue in DNA
Other name(s): T4-HMC-β-glucosyl transferase; T4-β-glucosyl transferase; T4 phage β-glucosyltransferase; UDP glucose-DNA β-glucosyltransferase; uridine diphosphoglucose-deoxyribonucleate β-glucosyltransferase; UDP-glucose:DNA β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:DNA β-D-glucosyltransferase (configuration-inverting)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-14-2
References:
1.  Kornberg, S.R., Zimmerman, S.B. and Kornberg, A. Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli. J. Biol. Chem. 236 (1961) 1487–1493. [PMID: 13753193]
[EC 2.4.1.27 created 1965]
 
 
EC 3.2.1.97     Relevance: 98.1%
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 3.2.1.71     Relevance: 97.8%
Accepted name: glucan endo-1,2-β-glucosidase
Reaction: Random hydrolysis of (1→2)-glucosidic linkages in (1→2)-β-D-glucans
Other name(s): endo-1,2-β-glucanase; β-D-1,2-glucanase; endo-(1→2)-β-D-glucanase; 1,2-β-D-glucan glucanohydrolase
Systematic name: 2-β-D-glucan glucanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-49-6
References:
1.  Reese, E.T., Parrish, F.W. and Mandels, M. β-D-1,2-Glucanases in fungi. Can. J. Microbiol. 7 (1961) 309–317. [PMID: 13740314]
[EC 3.2.1.71 created 1972]
 
 
EC 1.5.1.26     Relevance: 97.8%
Accepted name: β-alanopine dehydrogenase
Reaction: β-alanopine + NAD+ + H2O = β-alanine + pyruvate + NADH + H+
Systematic name: N-(D-1-carboxyethyl)-β-alanine:NAD+ oxidoreductase (β-alanine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 113573-64-1
References:
1.  Sato, M., Takahara, M., Kanno, N., Sato, Y. and Ellington, W.R. Isolation of a new opine, β-alanopine, from the extracts of the muscle of the marine bivalve mollusc Scapharca broughtonii. Comp. Biochem. Physiol. 88B (1987) 803–806.
[EC 1.5.1.26 created 1990]
 
 
EC 3.2.1.31     Relevance: 97.8%
Accepted name: β-glucuronidase
Reaction: a β-D-glucuronoside + H2O = D-glucuronate + an alcohol
Other name(s): β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase
Systematic name: β-D-glucuronoside glucuronosohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-45-0
References:
1.  Diez, T. and Cabezas, J.A. Properties of two molecular forms of β-glucuronidase from the mollusc Littorina littorea L. Eur. J. Biochem. 93 (1978) 301–311.
2.  Doyle, M.L., Katzman, P.A. and Doisy, E.A. Production and properties of bacterial β-glucuronidase. J. Biol. Chem. 217 (1955) 921–930. [PMID: 13271452]
3.  Fishman, W.H. Beta-glucuronidase. Adv. Enzymol. Relat. Subj. Biochem. 16 (1955) 361–409. [PMID: 14376216]
4.  Levvy, G.A. and Marsh, C.A. β-Glucuronidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 397–407.
5.  Wakabayashi, M. and Fishman, W.H. The comparative ability of β-glucuronidase preparations (liver, Escherichia coli, Helix pomatia, and Patella vulgata) to hydrolyze certain steroid glucosiduronic acids. J. Biol. Chem. 236 (1961) 996–1001. [PMID: 13782588]
[EC 3.2.1.31 created 1961]
 
 
EC 2.4.99.1      
Transferred entry: β-galactoside α-(2,6)-sialyltransferase. Now EC 2.4.3.1, β-galactoside α-(2,6)-sialyltransferase
[EC 2.4.99.1 created 1972, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2017), deleted 2022]
 
 
EC 2.4.3.1     Relevance: 97.8%
Accepted name: β-galactoside α-(2,6)-sialyltransferase
Reaction: CMP-N-acetyl-β-neuraminate + β-D-galactosyl-R = CMP + N-acetyl-α-neuraminyl-(2→6)-β-D-galactosyl-R
Other name(s): ST6Gal-I; CMP-N-acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase; lactosylceramide α-2,6-N-sialyltransferase; CMP-N-acetylneuraminate:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosamine α-(2→6)-N-acetylneuraminyltransferase; β-galactoside α-2,6-sialyltransferase
Systematic name: CMP-N-acetyl-β-neuraminate:β-D-galactoside α-(2→6)-N-acetylneuraminyltransferase (configuration-inverting)
Comments: The enzyme acts on the terminal non-reducing β-D-galactosyl residue of the oligosaccharide moiety of glycoproteins and glycolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-81-4
References:
1.  Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase. J. Biol. Chem. 243 (1968) 6520–6528. [PMID: 5726897]
2.  Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin. J. Biol. Chem. 245 (1970) 759–766. [PMID: 4313609]
3.  Bartholomew, B.A., Jourdian, G.W. and Roseman, S. The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum. J. Biol. Chem. 248 (1973) 5751–5762. [PMID: 4723915]
4.  Paulson, J.C., Beranek, W.E. and Hill, R.L. Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose. J. Biol. Chem. 252 (1977) 2356–2362. [PMID: 849932]
5.  Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98–134. [PMID: 6366476]
6.  Albarracin, I., Lassaga, F.E. and Caputto, R. Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide α2,6-N-acetylneuraminyltransferase (EC 2.4.99.-). Biochem. J. 254 (1988) 559–565. [PMID: 2460092]
[EC 2.4.3.1 created 1972 as EC 2.4.99.1, modified 1976, modified 1986, modified 2017 (EC 2.4.99.11 created 1992, incorporated 2016), modified 2017, transferred 2021 to EC 2.4.3.1]
 
 
EC 1.14.99.63     Relevance: 97.7%
Accepted name: β-carotene 4-ketolase
Reaction: (1) β-carotene + 2 reduced acceptor + 2 O2 = echinenone + 2 acceptor + 3 H2O
(2) echinenone + 2 reduced acceptor + 2 O2 = canthaxanthin + 2 acceptor + 3 H2O
For diagram of canthaxanthin biosynthesis, click here
Glossary: echinenone = β,β-caroten-4-one
canthaxanthin = β,β-carotene-4,4′-dione
zeaxanthin = β,β-carotene-3,3′-diol
astaxanthin = 3,3′-dihydroxy-β,β-carotene-4,4′-dione
Other name(s): BKT (ambiguous); β-C-4 oxygenase; β-carotene ketolase; crtS (gene name); crtW (gene name)
Systematic name: β-carotene,donor:oxygen oxidoreductase (echinenone-forming)
Comments: The enzyme, studied from algae, plants, fungi, and bacteria, adds an oxo group at position 4 of a carotenoid β ring. It is involved in the biosynthesis of carotenoids such as astaxanthin and flexixanthin. The enzyme does not act on β rings that are hydroxylated at position 3, such as in zeaxanthin (cf. EC 1.14.99.64, zeaxanthin 4-ketolase). The enzyme from the yeast Xanthophyllomyces dendrorhous is bifuntional and also catalyses the activity of EC 1.14.15.24, β-carotene 3-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lotan, T. and Hirschberg, J. Cloning and expression in Escherichia coli of the gene encoding β-C-4-oxygenase, that converts β-carotene to the ketocarotenoid canthaxanthin in Haematococcus pluvialis. FEBS Lett. 364 (1995) 125–128. [PMID: 7750556]
2.  Breitenbach, J., Misawa, N., Kajiwara, S. and Sandmann, G. Expression in Escherichia coli and properties of the carotene ketolase from Haematococcus pluvialis. FEMS Microbiol. Lett. 140 (1996) 241–246. [PMID: 8764486]
3.  Steiger, S. and Sandmann, G. Cloning of two carotenoid ketolase genes from Nostoc punctiforme for the heterologous production of canthaxanthin and astaxanthin. Biotechnol. Lett. 26 (2004) 813–817. [PMID: 15269553]
4.  Ojima, K., Breitenbach, J., Visser, H., Setoguchi, Y., Tabata, K., Hoshino, T., van den Berg, J. and Sandmann, G. Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a β-carotene 3-hydroxylase/4-ketolase. Mol. Genet. Genomics 275 (2006) 148–158. [PMID: 16416328]
5.  Tao, L., Yao, H., Kasai, H., Misawa, N. and Cheng, Q. A carotenoid synthesis gene cluster from Algoriphagus sp. KK10202C with a novel fusion-type lycopene β-cyclase gene. Mol. Genet. Genomics 276 (2006) 79–86. [PMID: 16625353]
6.  Kathiresan, S., Chandrashekar, A., Ravishankar, G.A. and Sarada, R. Regulation of astaxanthin and its intermediates through cloning and genetic transformation of β-carotene ketolase in Haematococcus pluvialis. J. Biotechnol. 196-197 (2015) 33–41. [PMID: 25612872]
[EC 1.14.99.63 created 2018]
 
 
EC 5.5.1.17     Relevance: 97.6%
Accepted name: (S)-β-macrocarpene synthase
Reaction: (S)-β-bisabolene = (S)-β-macrocarpene
For diagram of biosynthesis of bicyclic sesquiterpenoids derived from bisabolyl cation, click here and for diagram of bisabolene and macrocarpene biosynthesis, click here
Other name(s): TPS6; TPS11; (S)-β-macrocarpene lyase (decyclizing)
Systematic name: (S)-β-macrocarpene lyase (ring-opening)
Comments: The synthesis of (S)-β-macrocarpene from (2E,6E)-farnesyl diphosphate proceeds in two steps. The first step is the cyclization to (S)-β-bisabolene (cf. EC 4.2.3.55, (S)-β-bisabolene synthase). The second step is the isomerization to (S)-β-macrocarpene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kollner, T.G., Schnee, C., Li, S., Svatos, A., Schneider, B., Gershenzon, J. and Degenhardt, J. Protonation of a neutral (S)-β-bisabolene intermediate is involved in (S)-β-macrocarpene formation by the maize sesquiterpene synthases TPS6 and TPS11. J. Biol. Chem. 283 (2008) 20779–20788. [DOI] [PMID: 18524777]
[EC 5.5.1.17 created 2011]
 
 
EC 2.4.1.134     Relevance: 97.4%
Accepted name: galactosylxylosylprotein 3-β-galactosyltransferase
Reaction: UDP-α-D-galactose + [protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine = UDP + [protein]-3-O-(β-D-galactosyl-(1→3)-β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine
For diagram of heparan and chondroitin biosynthesis (early stages), click here
Other name(s): galactosyltransferase II; uridine diphosphogalactose-galactosylxylose galactosyltransferase; UDP-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase; UDP-α-D-galactose:4-β-D-galactosyl-O-β-D-xylosylprotein 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:[protein]-3-O-(β-D-galactosyl-(1→4)-β-D-xylosyl)-L-serine (configuration-inverting)
Comments: Involved in the biosynthesis of the linkage region of glycosaminoglycan chains as part of proteoglycan biosynthesis (chondroitin, dermatan and heparan sulfates). Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56626-21-2, 56626-19-8
References:
1.  Robinson, J.A. and Robinson, H.C. Initiation of chondroitin sulphate synthesis by β-D-galactosides. Substrates for galactosyltransferase II. Biochem. J. 227 (1985) 805–814. [PMID: 3924029]
2.  Schwartz, N.B. and Roden, L. Biosynthesis of chondroitin sulfate. Solubilization of chondroitin sulfate glycosyltransferases and partial purification of uridine diphosphate-D-galactose:D-xylose galactosyltransferase. J. Biol. Chem. 250 (1975) 5200–5207. [PMID: 1150655]
3.  Bai, X., Zhou, D., Brown, J.R., Crawford, B.E., Hennet, T. and Esko, J.D. Biosynthesis of the linkage region of glycosaminoglycans: cloning and activity of galactosyltransferase II, the sixth member of the β1,3-galactosyltransferase family (β3GalT6). J. Biol. Chem. 276 (2001) 48189–48195. [DOI] [PMID: 11551958]
[EC 2.4.1.134 created 1984, modified 2002]
 
 
EC 2.4.2.25     Relevance: 97.1%
Accepted name: flavone apiosyltransferase
Reaction: UDP-α-D-apiose + apigenin 7-O-β-D-glucoside = UDP + apigenin 7-O-[β-D-apiosyl-(1→2)-β-D-glucoside]
For diagram of apigenin derivatives biosynthesis, click here
Glossary: apigenin = 4′,5,7-trihydroxyflavone
β-D-apiose = (2R,3R,4R)-4-(hydroxymethyl)tetrahydrofuran-2,3,4-triol
Other name(s): uridine diphosphoapiose-flavone apiosyltransferase; UDP-apiose:7-O-(β-D-glucosyl)-flavone apiosyltransferase
Systematic name: UDP-apiose:5,4′-dihydroxyflavone 7-O-β-D-glucoside 2′′-O-β-D-apiofuranosyltransferase
Comments: 7-O-β-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37332-49-3
References:
1.  Ortmann, R., Sutter, A. and Grisebach, H. Purification and properties of UDPapiose: 7-O-(β-D-glucosyl)-flavone apiosyltransferase from cell suspension cultures of parsley. Biochim. Biophys. Acta 289 (1972) 293–302. [DOI] [PMID: 4650134]
[EC 2.4.2.25 created 1976]
 
 
EC 5.4.99.62     Relevance: 97.1%
Accepted name: D-ribose pyranase
Reaction: β-D-ribopyranose = β-D-ribofuranose
Other name(s): RbsD
Systematic name: D-ribopyranose furanomutase
Comments: The enzyme also catalyses the conversion between β-allopyranose and β-allofuranose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kim, M.S., Shin, J., Lee, W., Lee, H.S. and Oh, B.H. Crystal structures of RbsD leading to the identification of cytoplasmic sugar-binding proteins with a novel folding architecture. J. Biol. Chem. 278 (2003) 28173–28180. [DOI] [PMID: 12738765]
2.  Ryu, K.S., Kim, C., Kim, I., Yoo, S., Choi, B.S. and Park, C. NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration. J. Biol. Chem. 279 (2004) 25544–25548. [DOI] [PMID: 15060078]
[EC 5.4.99.62 created 2014]
 
 
EC 2.3.1.173     Relevance: 96.6%
Accepted name: flavonol-3-O-triglucoside O-coumaroyltransferase
Reaction: 4-coumaroyl-CoA + a flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] = CoA + a flavonol 3-O-[6-(4-coumaroyl)-β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside]
For diagram of kaempferol-glycoside biosynthesis, click here
Other name(s): 4-coumaroyl-CoA:flavonol-3-O-[β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase (incorrect)
Systematic name: 4-coumaroyl-CoA:flavonol 3-O-[β-D-glucosyl-(1→2)-β-D-glucosyl-(1→2)-β-D-glucoside] 6′′′-O-4-coumaroyltransferase
Comments: Acylates kaempferol 3-O-triglucoside on the terminal glucosyl unit, almost certainly at C-6.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64972-79-8
References:
1.  Saylor, M.H. and Mansell, R.L. Hydroxycinnamoyl:coenzyme A transferase involved in the biosynthesis of kaempferol-3-(p-coumaroyl triglucoside) in Pisum sativum. Z. Naturforsch. 32 (1977) 765–768. [PMID: 145116]
[EC 2.3.1.173 created 2004]
 
 
EC 2.4.1.392     Relevance: 96.5%
Accepted name: 3-O-β-D-glucopyranosyl-β-D-glucuronide phosphorylase
Reaction: a 3-O-β-D-glucosyl-β-D-glucuronoside + phosphate = a β-D-glucuronoside + α-D-glucopyranose 1-phosphate
Other name(s): PBOR_13355 (locus name)
Systematic name: 3-O-β-D-glucopyranosyl-β-D-glucuronide:phosphate α-D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Paenibacillus borealis, catalyses a reversible reaction, transferring a glucosyl residue attached by a β(1,3) linkage to a D-glucuronate residue (either free or as a part of a β-D-glucuronide) to a free phosphate, generating α-D-glucopyranose 1-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Isono, N., Mizutani, E., Hayashida, H., Katsuzaki, H. and Saburi, W. Functional characterization of a novel GH94 glycoside phosphorylase, 3-O-β-D-glucopyranosyl β-D-glucuronide phosphorylase, and implication of the metabolic pathway of acidic carbohydrates in Paenibacillus borealis. Biochem. Biophys. Res. Commun. 625 (2022) 60–65. [DOI] [PMID: 35947916]
[EC 2.4.1.392 created 2022]
 
 
EC 3.2.1.164     Relevance: 96.2%
Accepted name: galactan endo-1,6-β-galactosidase
Reaction: Endohydrolysis of (1→6)-β-D-galactosidic linkages in arabinogalactan proteins and (1→3):(1→6)-β-galactans to yield galactose and (1→6)-β-galactobiose as the final products
Other name(s): endo-1,6-β-galactanase
Systematic name: endo-β-(1→6)-galactanase
Comments: The enzyme specifically hydrolyses 1,6-β-D-galactooligosaccharides with a degree of polymerization (DP) higher than 3, and their acidic derivatives with 4-O-methylglucosyluronate or glucosyluronate groups at the non-reducing terminals [2]. 1,3-β-D- and 1,4-β-D-galactosyl residues cannot act as substrates. The enzyme can also hydrolyse α-L-arabinofuranosidase-treated arabinogalactan protein (AGP) extracted from radish roots [2,3]. AGPs are thought to be involved in many physiological events, such as cell division, cell expansion and cell death [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brillouet, J.-M., Williams, P. and Moutounet, M. Purification and some properties of a novel endo-β-(1→6)-D-galactanase from Aspergillus niger. Agric. Biol. Chem. 55 (1991) 1565–1571.
2.  Okemoto, K., Uekita, T., Tsumuraya, Y., Hashimoto, Y. and Kasama, T. Purification and characterization of an endo-β-(1→6)-galactanase from Trichoderma viride. Carbohydr. Res. 338 (2003) 219–230. [DOI] [PMID: 12543554]
3.  Kotake, T., Kaneko, S., Kubomoto, A., Haque, M.A., Kobayashi, H. and Tsumuraya, Y. Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-β-(1→6)-galactanase gene. Biochem. J. 377 (2004) 749–755. [DOI] [PMID: 14565843]
[EC 3.2.1.164 created 2007]
 
 
EC 2.4.1.274     Relevance: 96.2%
Accepted name: glucosylceramide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of glycolipid biosynthesis, click here
Other name(s): lactosylceramide synthase; uridine diphosphate-galactose:glucosyl ceramide β 1-4 galactosyltransferase; UDP-Gal:glucosylceramide β1→4galactosyltransferase; GalT-2 (misleading); UDP-galactose:β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase
Systematic name: UDP-α-D-galactose:β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase
Comments: Involved in the synthesis of several different major classes of glycosphingolipids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chatterjee, S. and Castiglione, E. UDPgalactose:glucosylceramide β1→4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. Biochim. Biophys. Acta 923 (1987) 136–142. [DOI] [PMID: 3099851]
2.  Trinchera, M., Fiorilli, A. and Ghidoni, R. Localization in the Golgi apparatus of rat liver UDP-Gal:glucosylceramide β1→4galactosyltransferase. Biochemistry 30 (1991) 2719–2724. [PMID: 1900430]
3.  Chatterjee, S., Ghosh, N. and Khurana, S. Purification of uridine diphosphate-galactose:glucosyl ceramide, β 1-4 galactosyltransferase from human kidney. J. Biol. Chem. 267 (1992) 7148–7153. [PMID: 1551920]
4.  Nomura, T., Takizawa, M., Aoki, J., Arai, H., Inoue, K., Wakisaka, E., Yoshizuka, N., Imokawa, G., Dohmae, N., Takio, K., Hattori, M. and Matsuo, N. Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide β-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273 (1998) 13570–13577. [DOI] [PMID: 9593693]
5.  Takizawa, M., Nomura, T., Wakisaka, E., Yoshizuka, N., Aoki, J., Arai, H., Inoue, K., Hattori, M. and Matsuo, N. cDNA cloning and expression of human lactosylceramide synthase. Biochim. Biophys. Acta 1438 (1999) 301–304. [DOI] [PMID: 10320813]
[EC 2.4.1.274 created 2011]
 
 
EC 3.4.24.32     Relevance: 95.9%
Accepted name: β-lytic metalloendopeptidase
Reaction: Cleavage of N-acetylmuramoyl┼Ala, and of the insulin B chain at Gly23┼Phe > Val18┼Cya
Other name(s): Myxobacter β-lytic proteinase; achromopeptidase component; β-lytic metalloproteinase; β-lytic protease; Myxobacterium sorangium β-lytic proteinase; Myxobacter495 β-lytic proteinase
Comments: From Achromobacter lyticus and Lysobacter enzymogenes. Digests bacterial cell walls. Type example of peptidase family M23.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 37288-92-9
References:
1.  Whitaker, D.R., Roy, C., Tsai, C.S. and Juraöek, L. Lytic enzymes of Sorangium sp. A comparison of the proteolytic properties of the α- and β-lytic proteases. Can. J. Biochem. 43 (1965) 1961–1970. [PMID: 5880182]
2.  Whitaker, D.R. and Roy, C. Concerning the nature of the α- and β-lytic proteases of Sorangium sp. Can. J. Biochem. 45 (1967) 911. [PMID: 6034704]
3.  Li, S. L., Norioka, S. and Sakiyama, F. Molecular cloning and nucleotide sequence of the β-lytic protease gene from Achromobacter lyticus. J. Bacteriol. 172 (1990) 6506–6511. [DOI] [PMID: 2228973]
[EC 3.4.24.32 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.32]
 
 
EC 5.1.3.44     Relevance: 95.7%
Accepted name: mannose 2-epimerase
Reaction: β-D-mannopyranose = β-D-glucopyranose
Systematic name: β-D-mannopyranose 2-epimerase
Comments: The enzyme, characterized from multiple bacterial species, catalyses the interconversion between β-D-glucopyranose and β-D-mannopyranose through proton abstraction-addition at the C2 position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Saburi, W., Sato, S., Hashiguchi, S., Muto, H., Iizuka, T. and Mori, H. Enzymatic characteristics of D-mannose 2-epimerase, a new member of the acylglucosamine 2-epimerase superfamily. Appl. Microbiol. Biotechnol. 103 (2019) 6559–6570. [DOI] [PMID: 31201453]
[EC 5.1.3.44 created 2020]
 
 
EC 1.14.13.134      
Transferred entry: β-amyrin 11-oxidase. Now EC 1.14.14.152, β-amyrin 11-oxidase
[EC 1.14.13.134 created 2011, deleted 2018]
 
 
EC 3.2.1.91     Relevance: 95.7%
Accepted name: cellulose 1,4-β-cellobiosidase (non-reducing end)
Reaction: Hydrolysis of (1→4)-β-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
Other name(s): exo-cellobiohydrolase; β-1,4-glucan cellobiohydrolase; β-1,4-glucan cellobiosylhydrolase; 1,4-β-glucan cellobiosidase; exoglucanase; avicelase; CBH 1; C1 cellulase; cellobiohydrolase I; cellobiohydrolase; exo-β-1,4-glucan cellobiohydrolase; 1,4-β-D-glucan cellobiohydrolase; cellobiosidase
Systematic name: 4-β-D-glucan cellobiohydrolase (non-reducing end)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37329-65-0
References:
1.  Berghem, L.E.R. and Pettersson, L.G. The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from Trichoderma viride active on highly ordered cellulose. Eur. J. Biochem. 37 (1973) 21–30. [DOI] [PMID: 4738092]
2.  Eriksson, K.E. and Pettersson, B. Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cellulose. 3. Purification and physico-chemical characterization of an exo-1,4-β-glucanase. Eur. J. Biochem. 51 (1975) 213–218. [DOI] [PMID: 235428]
3.  Halliwell, G., Griffin, M. and Vincent, R. The role of component C1 in cellulolytic systems. Biochem. J. 127 (1972) 43P. [PMID: 5076675]
[EC 3.2.1.91 created 1976, modified 2011]
 
 
EC 2.4.1.12     Relevance: 95.6%
Accepted name: cellulose synthase (UDP-forming)
Reaction: UDP-α-D-glucose + [(1→4)-β-D-glucosyl]n = UDP + [(1→4)-β-D-glucosyl]n+1
Other name(s): UDP-glucose—β-glucan glucosyltransferase; UDP-glucose-cellulose glucosyltransferase; GS-I; β-1,4-glucosyltransferase; uridine diphosphoglucose-1,4-β-glucan glucosyltransferase; β-1,4-glucan synthase; β-1,4-glucan synthetase; β-glucan synthase; 1,4-β-D-glucan synthase; 1,4-β-glucan synthase; glucan synthase; UDP-glucose-1,4-β-glucan glucosyltransferase; uridine diphosphoglucose-cellulose glucosyltransferase; UDP-glucose:1,4-β-D-glucan 4-β-D-glucosyltransferase; UDP-glucose:(1→4)-β-D-glucan 4-β-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:(1→4)-β-D-glucan 4-β-D-glucosyltransferase (configuration-inverting)
Comments: Involved in the synthesis of cellulose. A similar enzyme utilizes GDP-glucose [EC 2.4.1.29 cellulose synthase (GDP-forming)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-19-4
References:
1.  Glaser, L. The synthesis of cellulose in cell-free extracts of Acetobacter xylinum. J. Biol. Chem. 232 (1958) 627–636. [PMID: 13549448]
[EC 2.4.1.12 created 1961]
 
 
EC 3.2.1.85     Relevance: 95.4%
Accepted name: 6-phospho-β-galactosidase
Reaction: a 6-phospho-β-D-galactoside + H2O = 6-phospho-D-galactose + an alcohol
Other name(s): phospho-β-galactosidase; β-D-phosphogalactoside galactohydrolase; phospho-β-D-galactosidase; 6-phospho-β-D-galactosidase
Systematic name: 6-phospho-β-D-galactoside 6-phosphogalactohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-42-6
References:
1.  Hengstenberg, W., Penberthy, W.K. and Morse, M.L. Purification of the staphylococcal 6-phospho-β-D-galactosidase. Eur. J. Biochem. 14 (1970) 27–32. [DOI] [PMID: 5447434]
[EC 3.2.1.85 created 1976]
 
 
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 2.4.3.10     Relevance: 95.4%
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 2.4.1.391     Relevance: 95.2%
Accepted name: β-1,2-glucosyltransferase
Reaction: [(1→2)-β-D-glucosyl]n + a D-glucoside = [(1→2)-β-D-glucosyl]n-1 + a β-D-glucosyl-(1→2)-D-glucoside
Systematic name: 1,2-β-D-glucan:D-glucoside 2-β-D-glucosyltransferase (configuration-retaining)
Comments: The enzyme, characterized from the bacterium Ignavibacterium album, transfers a glucosyl residue from the non-reducing end of a 1,2-β-D-glucan to a glucose residue of an acceptor molecule, forming a β(1,2) linkage. The donor molecule can be as small as sophorose (which contains two glucosyl residues). The enzyme has a very broad specificity for the acceptor, and can act on various aryl- and alkyl-glucosides. In addition, the accepting glucose unit can be in either α or β configuration.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kobayashi, K., Shimizu, H., Tanaka, N., Kuramochi, K., Nakai, H., Nakajima, M. and Taguchi, H. Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages. J. Biol. Chem. 298:101606 (2022). [DOI] [PMID: 35065074]
[EC 2.4.1.391 created 2022]
 
 
EC 3.2.1.8     Relevance: 95.2%
Accepted name: endo-1,4-β-xylanase
Reaction: Endohydrolysis of (1→4)-β-D-xylosidic linkages in xylans
Other name(s): endo-(1→4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase
Systematic name: 4-β-D-xylan xylanohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-57-4
References:
1.  Howard, B.H., Jones, G. and Purdom, M.R. The pentosanases of some rumen bacteria. Biochem. J. 74 (1960) 173–180. [PMID: 14403433]
2.  Whistler, R.L. and Masek, E. Enzymatic hydolysis of xylan. J. Am. Chem. Soc. 77 (1955) 1241–1243.
[EC 3.2.1.8 created 1961]
 
 
EC 2.4.1.330     Relevance: 95.1%
Accepted name: β-D-glucosyl crocetin β-1,6-glucosyltransferase
Reaction: (1) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + β-D-gentiobiosyl crocetin
(2) UDP-α-D-glucose + bis(β-D-glucosyl) crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl β-D-glucosyl crocetin = UDP + crocin
For diagram of crocin biosynthesis, click here
Glossary: crocin = bis(β-D-gentiobiosyl) crocetin
crocetin = (2E,4E,6E,8E,10E,12E,14E)-2,6,11,15-tetramethylhexadeca-2,4,6,8,10,12,14-heptaenedioate
Other name(s): UGT94E5; UDP-glucose:crocetin glucosyl ester glucosyltransferasee
Systematic name: UDP-α-D-glucose:β-D-glucosyl crocetin β-1,6-glucosyltransferase
Comments: The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271, crocetin glucosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett. 586 (2012) 1055–1061. [DOI] [PMID: 22569263]
[EC 2.4.1.330 created 2014]
 
 
EC 1.14.17.1     Relevance: 95%
Accepted name: dopamine β-monooxygenase
Reaction: dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
For diagram of dopa biosynthesis, click here
Glossary: dopamine = 4-(2-aminoethyl)benzene-1,2-diol
Other name(s): dopamine β-hydroxylase; MDBH (membrane-associated dopamine β-monooxygenase); SDBH (soluble dopamine β-monooxygenase); dopamine-B-hydroxylase; 3,4-dihydroxyphenethylamine β-oxidase; 4-(2-aminoethyl)pyrocatechol β-oxidase; dopa β-hydroxylase; dopamine β-oxidase; dopamine hydroxylase; phenylamine β-hydroxylase; (3,4-dihydroxyphenethylamine)β-mono-oxygenase; DβM (gene name)
Systematic name: dopamine,ascorbate:oxygen oxidoreductase (β-hydroxylating)
Comments: A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-38-1
References:
1.  Levin, E.Y., Levenberg, B. and Kaufman, S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J. Biol. Chem. 235 (1960) 2080–2086. [PMID: 14416204]
2.  Friedman, S. and Kaufman, S. 3,4-Dihydroxyphenylethylamine β-hydroxylase. Physical properties, copper content, and role of copper in the catalytic activity. J. Biol. Chem. 240 (1965) 4763–4773. [PMID: 5846992]
3.  Skotland, T. and Ljones, T. Direct spectrophotometric detection of ascorbate free radical formed by dopamine β-monooxygenase and by ascorbate oxidase. Biochim. Biophys. Acta 630 (1980) 30–35. [PMID: 7388045]
4.  Evans, J.P., Ahn, K. and Klinman, J.P. Evidence that dioxygen and substrate activation are tightly coupled in dopamine β-monooxygenase. Implications for the reactive oxygen species. J. Biol. Chem. 278 (2003) 49691–49698. [PMID: 12966104]
[EC 1.14.17.1 created 1965 as EC 1.14.2.1, transferred 1972 to EC 1.14.17.1, modified 2020]
 
 
EC 2.4.1.165     Relevance: 94.9%
Accepted name: N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Other name(s): uridine diphosphoacetylgalactosamine-acetylneuraminyl(α2→3)galactosyl(β1→4)glucosyl β1→4-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-2,3-α-D-galactosyl-1,4-β-D-glucosylceramide β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2→3)-α-D-galactosyl-(1→4)-β-D-glucosyl(1↔1)ceramide 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2→3)-α-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-N-acetylgalactosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-galactosamine:α-N-acetylneuraminyl-(2→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-N-acetylgalactosaminyltransferase
Comments: Requires Mn2+. Only substances containing sialic acid residues can act as acceptors; bovine fetuin is the best acceptor tested.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109136-50-7
References:
1.  Chien, J.-L., Williams, T. and Basu, S. Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain. J. Biol. Chem. 248 (1973) 1778–1785. [PMID: 4632917]
2.  Piller, F., Blanchard, D., Huet, M. and Cartron, J.-P. Identification of a α-NeuAc-(2-3)-β-D-galactopyranosyl N-acetyl-β-D-galactosaminyltransferase in human kidney. Carbohydr. Res. 149 (1986) 171–184. [DOI] [PMID: 2425965]
3.  Takeya, A., Hosomi, O. and Kogure, T. Identification and characterization of UDP-GalNAc: NeuAc α2-3Gal β1-4Glc(NAc) β1-4(GalNAc to Gal)N-acetylgalactosaminyltransferase in human blood plasma. J. Biochem. (Tokyo) 101 (1987) 251–259. [PMID: 3106337]
[EC 2.4.1.165 created 1989]
 
 
EC 2.4.1.10     Relevance: 94.8%
Accepted name: levansucrase
Reaction: sucrose + [6)-β-D-fructofuranosyl-(2→]n α-D-glucopyranoside = D-glucose + [6)-β-D-fructofuranosyl-(2→]n+1 α-D-glucopyranoside
For diagram of reaction, click here
Other name(s): sucrose 6-fructosyltransferase; β-2,6-fructosyltransferase; β-2,6-fructan:D-glucose 1-fructosyltransferase; sucrose:2,6-β-D-fructan 6-β-D-fructosyltransferase; sucrose:(2→6)-β-D-fructan 6-β-D-fructosyltransferase
Systematic name: sucrose:[6)-β-D-fructofuranosyl-(2→]n α-D-glucopyranoside 6-β-D-fructosyltransferase
Comments: Some other sugars can act as D-fructosyl acceptors.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-17-5
References:
1.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337. [PMID: 24540594]
2.  Hestrin, S., Feingold, D.S. and Avigad, G. The mechanism of polysaccharide production from sucrose. 3. Donor-acceptor specificity of levansucrase from Aerobacter levanicum. Biochem. J. 64 (1956) 340–351. [PMID: 13363847]
3.  Reese, E.T. and Avigad, G. Purification of levansucrase by precipitation with levan. Biochim. Biophys. Acta 113 (1966) 79–83. [PMID: 5940635]
4.  Meng, G. and Futterer, K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat. Struct. Biol. 10 (2003) 935–941. [DOI] [PMID: 14517548]
[EC 2.4.1.10 created 1961, modified 2011]
 
 
EC 3.2.1.126     Relevance: 94.6%
Accepted name: coniferin β-glucosidase
Reaction: coniferin + H2O = D-glucose + coniferol
Other name(s): coniferin-hydrolyzing β-glucosidase
Systematic name: coniferin β-D-glucosidase
Comments: Also hydrolyses syringin, 4-cinnamyl alcohol β-glucoside and, more slowly, some other aryl β-glycosides. A plant cell-wall enzyme involved in the biosynthesis of lignin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 83869-30-1
References:
1.  Hösel, W., Surholt, E. and Borgmann, E. Characterization of β-glucosidase isoenzymes possibly involved in lignification from chick pea (Cicer arietinum L.) cell suspension cultures. Eur. J. Biochem. 84 (1978) 487–492. [DOI] [PMID: 25181]
2.  Marcinowski, S. and Grisebach, H. Enzymology of lignification. Cell-wall bound β-glucosidase for coniferin from spruce (Picea abies) seedlings. Eur. J. Biochem. 87 (1978) 37–44. [DOI] [PMID: 27355]
[EC 3.2.1.126 created 1989]
 
 
EC 3.2.1.80     Relevance: 94.5%
Accepted name: fructan β-fructosidase
Reaction: Hydrolysis of terminal, non-reducing (2→1)- and (2→6)-linked β-D-fructofuranose residues in fructans
For diagram of hydrolysis of the 2,6-bond, click here and the 2,1-bond, click here
Other name(s): exo-β-D-fructosidase; exo-β-fructosidase; polysaccharide β-fructofuranosidase; fructan exohydrolase
Systematic name: β-D-fructan fructohydrolase
Comments: Hydrolyses inulin and levan, and also sucrose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-56-5
References:
1.  DaCosta, T. and Gibbons, R.J. Hydrolysis of levan by human plaque streptococci. Arch. Oral Biol. 13 (1968) 609–617. [PMID: 5244285]
2.  Jacques, N.J., Morrey-Jones, J.G. and Walker, G.J. Inducible and constitutive formation of fructanase in batch and continuous cultures of Streptococcus mutans. J. Gen. Microbiol. 131 (1985) 1625–1633. [DOI] [PMID: 4045423]
[EC 3.2.1.80 created 1972]
 
 
EC 4.2.3.106     Relevance: 94%
Accepted name: (E)-β-ocimene synthase
Reaction: geranyl diphosphate = (E)-β-ocimene + diphosphate
Glossary: (E)-β-ocimene = (3E)-3,7-dimethylocta-1,3,6-triene
Other name(s): β-ocimene synthase; AtTPS03; ama0a23; LjEβOS; MtEBOS
Systematic name: geranyl-diphosphate diphosphate-lyase [(E)-β-ocimene-forming]
Comments: Widely distributed in plants, which release β-ocimene when attacked by herbivorous insects.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Faldt, J., Arimura, G., Gershenzon, J., Takabayashi, J. and Bohlmann, J. Functional identification of AtTPS03 as (E)-β-ocimene synthase: a monoterpene synthase catalyzing jasmonate- and wound-induced volatile formation in Arabidopsis thaliana. Planta 216 (2003) 745–751. [DOI] [PMID: 12624761]
2.  Dudareva, N., Martin, D., Kish, C.M., Kolosova, N., Gorenstein, N., Faldt, J., Miller, B. and Bohlmann, J. (E)-β-ocimene and myrcene synthase genes of floral scent biosynthesis in snapdragon: function and expression of three terpene synthase genes of a new terpene synthase subfamily. Plant Cell 15 (2003) 1227–1241. [DOI] [PMID: 12724546]
3.  Arimura, G., Ozawa, R., Kugimiya, S., Takabayashi, J. and Bohlmann, J. Herbivore-induced defense response in a model legume. Two-spotted spider mites induce emission of (E)-β-ocimene and transcript accumulation of (E)-β-ocimene synthase in Lotus japonicus. Plant Physiol. 135 (2004) 1976–1983. [DOI] [PMID: 15310830]
4.  Navia-Gine, W.G., Yuan, J.S., Mauromoustakos, A., Murphy, J.B., Chen, F. and Korth, K.L. Medicago truncatula (E)-β-ocimene synthase is induced by insect herbivory with corresponding increases in emission of volatile ocimene. Plant Physiol. Biochem. 47 (2009) 416–425. [DOI] [PMID: 19249223]
[EC 4.2.3.106 created 2012]
 
 
EC 1.2.1.82     Relevance: 94%
Accepted name: β-apo-4′-carotenal dehydrogenase
Reaction: 4′-apo-β,ψ-caroten-4′-al + NAD+ + H2O = neurosporaxanthin + NADH + 2 H+
For diagram of reaction, click here
Glossary: neurosporaxanthin = 4′-apo-β,ψ-caroten-4′-oic acid
Other name(s): β-apo-4′-carotenal oxygenase; YLO-1; carD (gene name)
Systematic name: 4′-apo-β,ψ-carotenal:NAD+ oxidoreductase
Comments: Neurosporaxanthin is responsible for the orange color of of Neurospora.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Estrada, A.F., Youssar, L., Scherzinger, D., Al-Babili, S. and Avalos, J. The ylo-1 gene encodes an aldehyde dehydrogenase responsible for the last reaction in the Neurospora carotenoid pathway. Mol. Microbiol. 69 (2008) 1207–1220. [DOI] [PMID: 18627463]
2.  Diaz-Sanchez, V., Estrada, A.F., Trautmann, D., Al-Babili, S. and Avalos, J. The gene carD encodes the aldehyde dehydrogenase responsible for neurosporaxanthin biosynthesis in Fusarium fujikuroi. FEBS J. 278 (2011) 3164–3176. [DOI] [PMID: 21749649]
[EC 1.2.1.82 created 2011, modified 2023]
 
 
EC 3.2.1.88     Relevance: 93.9%
Accepted name: non-reducing end β-L-arabinopyranosidase
Reaction: Removal of a terminal β-L-arabinopyranose residue from the non-reducing end of its substrate.
Other name(s): vicianosidase; β-L-arabinosidase (ambiguous); β-L-arabinoside arabinohydrolase (ambiguous)
Systematic name: β-L-arabinopyranoside non-reducing end β-L-arabinopyranosidase
Comments: The enzyme, which was characterized from dormant seeds of the plant Cajanus cajan (pigeon pea), has been shown to remove the terminal non-reducing β-L-arabinopyranoside residue from the artificial substrate p-nitrophenyl-β-L-arabinopyranose [1]. In the presence of methanol the enzyme demonstrates transglycosylase activity, transferring the arabinose moiety to methanol while retaining the anomeric configuration, generating 1-O-methyl-β-L-arabinopyranose [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39361-63-2
References:
1.  Dey, P.M. β-L-Arabinosidase from Cajanus indicus: a new enzyme. Biochim. Biophys. Acta 302 (1973) 393–398. [DOI] [PMID: 4699248]
2.  Dey, P. M. Further characterization of β-L-arabinosidase from Cajanus indicus. Biochim.Biophys. Acta 746 (1983) 8–13.
[EC 3.2.1.88 created 1976, modified 2013]
 
 
EC 3.2.1.175     Relevance: 93.6%
Accepted name: β-D-glucopyranosyl abscisate β-glucosidase
Reaction: D-glucopyranosyl abscisate + H2O = D-glucose + abscisate
For diagram of abscisic-acid biosynthesis, click here
Other name(s): AtBG1; ABA-β-D-glucosidase; ABA-specific β-glucosidase; ABA-GE hydrolase; β-D-glucopyranosyl abscisate hydrolase
Systematic name: β-D-glucopyranosyl abscisate glucohydrolase
Comments: The enzyme hydrolzes the biologically inactive β-D-glucopyranosyl ester of abscisic acid to produce active abscisate. Abscisate is a phytohormone critical for plant growth, development and adaption to various stress conditions. The enzyme does not hydrolyse β-D-glucopyranosyl zeatin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, K.H., Piao, H.L., Kim, H.Y., Choi, S.M., Jiang, F., Hartung, W., Hwang, I., Kwak, J.M., Lee, I.J. and Hwang, I. Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid. Cell 126 (2006) 1109–1120. [DOI] [PMID: 16990135]
2.  Kato-Noguchi, H. and Tanaka, Y. Effect of ABA-β-D-glucopyranosyl ester and activity of ABA-β-D-glucosidase in Arabidopsis thaliana. J. Plant Physiol. 165 (2008) 788–790. [DOI] [PMID: 17923167]
3.  Dietz, K.J., Sauter, A., Wichert, K., Messdaghi, D. and Hartung, W. Extracellular β-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves. J. Exp. Bot. 51 (2000) 937–944. [DOI] [PMID: 10948220]
[EC 3.2.1.175 created 2011]
 
 
EC 5.4.99.39     Relevance: 93.5%
Accepted name: β-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = β-amyrin
For diagram of beta-amyrin and soysapogenol biosynthesis, click here
Other name(s): 2,3-oxidosqualene β-amyrin cyclase; AsbAS1; BPY; EtAS; GgbAS1; LjAMY1; MtAMY1; PNY; BgbAS
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, β-amyrin-forming)
Comments: Some organism possess a monofunctional β-amyrin synthase [3,4,6-11], other have a multifunctional enzyme that also catalyses the synthesis of α-amyrin (EC 5.4.99.40) [5] or lupeol (EC 5.4.99.41) [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Abe, I, Ebizuka, Y., Seo, S. and Sankawa, U. Purification of squalene-2,3-epoxide cyclases from cell suspension cultures of Rabdosia japonica Hara. FEBS Lett. 249 (1989) 100–104.
2.  Abe, I., Sankawa, U. and Ebizuka, Y. Purification of 2,3-oxdosqualene:β-amyrin cyclase from pea seedlings. Chem. Pharm. Bull. 37 (1989) 536.
3.  Kushiro, T., Shibuya, M. and Ebizuka, Y. β-Amyrin synthase-cloning of oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants. Eur. J. Biochem. 256 (1998) 238–244. [DOI] [PMID: 9746369]
4.  Hayashi, H., Huang, P., Kirakosyan, A., Inoue, K., Hiraoka, N., Ikeshiro, Y., Kushiro, T., Shibuya, M. and Ebizuka, Y. Cloning and characterization of a cDNA encoding β-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice. Biol. Pharm. Bull. 24 (2001) 912–916. [PMID: 11510484]
5.  Husselstein-Muller, T., Schaller, H. and Benveniste, P. Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana. Plant Mol. Biol. 45 (2001) 75–92. [PMID: 11247608]
6.  Iturbe-Ormaetxe, I., Haralampidis, K., Papadopoulou, K. and Osbourn, A.E. Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus. Plant Mol. Biol. 51 (2003) 731–743. [PMID: 12683345]
7.  Zhang, H., Shibuya, M., Yokota, S. and Ebizuka, Y. Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. japonica: molecular evolution of oxidosqualene cyclases in higher plants. Biol. Pharm. Bull. 26 (2003) 642–650. [PMID: 12736505]
8.  Hayashi, H., Huang, P., Takada, S., Obinata, M., Inoue, K., Shibuya, M. and Ebizuka, Y. Differential expression of three oxidosqualene cyclase mRNAs in Glycyrrhiza glabra. Biol. Pharm. Bull. 27 (2004) 1086–1092. [PMID: 15256745]
9.  Kajikawa, M., Yamato, K.T., Fukuzawa, H., Sakai, Y., Uchida, H. and Ohyama, K. Cloning and characterization of a cDNA encoding β-amyrin synthase from petroleum plant Euphorbia tirucalli L. Phytochemistry 66 (2005) 1759–1766. [DOI] [PMID: 16005035]
10.  Basyuni, M., Oku, H., Tsujimoto, E., Kinjo, K., Baba, S. and Takara, K. Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae. FEBS J. 274 (2007) 5028–5042. [DOI] [PMID: 17803686]
11.  Liu, Y., Cai, Y., Zhao, Z., Wang, J., Li, J., Xin, W., Xia, G. and Xiang, F. Cloning and functional analysis of a β-amyrin synthase gene associated with oleanolic acid biosynthesis in Gentiana straminea MAXIM. Biol. Pharm. Bull. 32 (2009) 818–824. [PMID: 19420748]
[EC 5.4.99.39 created 2011]
 
 
EC 1.14.13.129      
Transferred entry: β-carotene 3-hydroxylase. Now EC 1.14.15.24, β-carotene 3-hydroxylase.
[EC 1.14.13.129 created 2011, deleted 2017]
 
 
EC 2.4.1.34     Relevance: 93.4%
Accepted name: 1,3-β-glucan synthase
Reaction: UDP-glucose + [(1→3)-β-D-glucosyl]n = UDP + [(1→3)-β-D-glucosyl]n+1
Other name(s): 1,3-β-D-glucan—UDP glucosyltransferase; UDP-glucose—1,3-β-D-glucan glucosyltransferase; callose synthetase; 1,3-β-D-glucan-UDP glucosyltransferase; UDP-glucose-1,3-β-D-glucan glucosyltransferase; paramylon synthetase; UDP-glucose-β-glucan glucosyltransferase; GS-II; (1,3)-β-glucan (callose) synthase; β-1,3-glucan synthase; β-1,3-glucan synthetase; 1,3-β-D-glucan synthetase; 1,3-β-D-glucan synthase; 1,3-β-glucan-uridine diphosphoglucosyltransferase; callose synthase; UDP-glucose-1,3-β-glucan glucosyltransferase; UDP-glucose:(1,3)β-glucan synthase; uridine diphosphoglucose-1,3-β-glucan glucosyltransferase; UDP-glucose:1,3-β-D-glucan 3-β-D-glucosyltransferase
Systematic name: UDP-glucose:(1→3)-β-D-glucan 3-β-D-glucosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-30-3
References:
1.  Maréchal, L.R. and Goldemberg, S.H. Uridine diphosphate glucose-β-1,3-glucan β-3-glucosyltransferase from Euglena gracilis. J. Biol. Chem. 239 (1964) 3163–3167. [PMID: 14245356]
[EC 2.4.1.34 created 1972]
 
 
EC 1.13.11.71     Relevance: 93.3%
Accepted name: carotenoid-9′,10′-cleaving dioxygenase
Reaction: all-trans-β-carotene + O2 = all-trans-10′-apo-β-carotenal + β-ionone
For diagram of 10′-apo-β-carotenal biosynthesis, click here
Other name(s): BCO2 (gene name); β-carotene 9′,10′-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9′,10′-cleaving)
Systematic name: all-trans-β-carotene:oxygen oxidoreductase (9′,10′-cleaving)
Comments: Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E. and von Lintig, J. Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J. Biol. Chem. 276 (2001) 14110–14116. [DOI] [PMID: 11278918]
2.  Lindqvist, A., He, Y.G. and Andersson, S. Cell type-specific expression of β-carotene 9′,10′-monooxygenase in human tissues. J. Histochem. Cytochem. 53 (2005) 1403–1412. [DOI] [PMID: 15983114]
[EC 1.13.11.71 created 2012]
 
 


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