The Enzyme Database

Displaying entries 51-67 of 67.

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EC 5.4.99.51     
Accepted name: baccharis oxide synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = baccharis oxide
For diagram of baccharis oxide, baruol and shionone biosynthesis, click here
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baccharis-oxide-forming)
Comments: The enzyme from Stevia rebaudiana also gives traces of other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Sagara, A., Saitoh, A., Kushiro, T. and Ebizuka, Y. Biosynthesis of baccharis oxide, a triterpene with a 3,10-oxide bridge in the A-ring. Org. Lett. 10 (2008) 5071–5074. [DOI] [PMID: 18850716]
[EC 5.4.99.51 created 2011]
 
 
EC 5.4.99.52     
Accepted name: α-seco-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = α-seco-amyrin
For diagram of α-amyrin, α-seco-amyrin and germanicol biosynthesis, click here
Glossary: α-seco-amyrin = 8,14-secoursa-7,13-diene-3β-ol
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, α-seco-amyrin-forming)
Comments: The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of α- and β-seco-amyrin. See EC 5.4.99.54, β-seco-amyrin synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Xiang, T., Katsube, Y., Otsuka, M., Zhang, H. and Ebizuka, Y. Origin of structural diversity in natural triterpenes: direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase. J. Am. Chem. Soc. 129 (2007) 1450–1455. [DOI] [PMID: 17263431]
[EC 5.4.99.52 created 2011]
 
 
EC 5.4.99.53     
Accepted name: marneral synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = marneral
For diagram of arabidiol, camellidiol and thalianol biosynthesis, click here
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, marneral-forming)
Comments: Marneral is a triterpenoid formed by Grob fragmentation of the A ring of 2,3-epoxy-2,3-dihydrosqualene during cyclization.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xiong, Q., Wilson, W.K. and Matsuda, S.P.T. An Arabidopsis oxidosqualene cyclase catalyzes iridal skeleton formation by Grob fragmentation. Angew. Chem. Int. Ed. Engl. 45 (2006) 1285–1288. [DOI] [PMID: 16425307]
[EC 5.4.99.53 created 2011]
 
 
EC 5.4.99.54     
Accepted name: β-seco-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = β-seco-amyrin
For diagram of beta-amyrin and soysapogenol biosynthesis, click here
Glossary: β-seco-amyrin = 8,14-secooleana-7,13-diene-3β-ol
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, β-seco-amyrin-forming)
Comments: The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of α- and β-seco-amyrin. See EC 5.4.99.52, α-seco-amyrin synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shibuya, M., Xiang, T., Katsube, Y., Otsuka, M., Zhang, H. and Ebizuka, Y. Origin of structural diversity in natural triterpenes: direct synthesis of seco-triterpene skeletons by oxidosqualene cyclase. J. Am. Chem. Soc. 129 (2007) 1450–1455. [DOI] [PMID: 17263431]
[EC 5.4.99.54 created 2011]
 
 
EC 5.4.99.55     
Accepted name: δ-amyrin synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = δ-amyrin
For diagram of α-amyrin, α-seco-amyrin and germanicol biosynthesis, click here
Other name(s): SlTTS2 (gene name)
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, δ-amyrin-forming)
Comments: The enzyme from tomato (Solanum lycopersicum) gives 48% δ-amyrin, 18% α-amyrin, 13% β-amyrin and traces of three or four other triterpenoid alcohols [1]. See also EC 5.4.99.40, α-amyrin synthase and EC 5.4.99.39, β-amyrin synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Z., Guhling, O., Yao, R., Li, F., Yeats, T.H., Rose, J.K. and Jetter, R. Two oxidosqualene cyclases responsible for biosynthesis of tomato fruit cuticular triterpenoids. Plant Physiol. 155 (2011) 540–552. [DOI] [PMID: 21059824]
[EC 5.4.99.55 created 2011]
 
 
EC 5.4.99.56     
Accepted name: tirucalladienol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = tirucalla-7,24-dien-3β-ol
For diagram of dammarenediol II and tirucalla-7,24-dien-3β-ol biosynthesis, click here
Other name(s): PEN3
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, tirucalla-7,24-dien-3β-ol-forming)
Comments: The product from Arabidopsis thaliana is 85% tirucalla-7,24-dien-3β-ol with trace amounts of other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morlacchi, P., Wilson, W.K., Xiong, Q., Bhaduri, A., Sttivend, D., Kolesnikova, M.D. and Matsuda, S.P. Product profile of PEN3: the last unexamined oxidosqualene cyclase in Arabidopsis thaliana. Org. Lett. 11 (2009) 2627–2630. [DOI] [PMID: 19445469]
[EC 5.4.99.56 created 2011]
 
 
EC 5.4.99.57     
Accepted name: baruol synthase
Reaction: (3S)-2,3-epoxy-2,3-dihydrosqualene = baruol
For diagram of baccharis oxide, baruol and shionone biosynthesis, click here
Other name(s): BARS1
Systematic name: (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baruol-forming)
Comments: The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lodeiro, S., Xiong, Q., Wilson, W.K., Kolesnikova, M.D., Onak, C.S. and Matsuda, S.P. An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis. J. Am. Chem. Soc. 129 (2007) 11213–11222. [DOI] [PMID: 17705488]
[EC 5.4.99.57 created 2012]
 
 
EC 5.4.99.58     
Accepted name: methylornithine synthase
Reaction: L-lysine = (3R)-3-methyl-D-ornithine
Glossary: (3R)-3-methyl-D-ornithine = (2R,3R)-2,5-diamino-3-methylpentanoate
Other name(s): PylB
Systematic name: L-lysine carboxy-aminomethylmutase
Comments: The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182]
2.  Quitterer, F., List, A., Eisenreich, W., Bacher, A. and Groll, M. Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis. Angew. Chem. Int. Ed. Engl. 51 (2012) 1339–1342. [DOI] [PMID: 22095926]
[EC 5.4.99.58 created 2012]
 
 
EC 5.4.99.59     
Accepted name: dTDP-fucopyranose mutase
Reaction: dTDP-α-D-fucopyranose = dTDP-α-D-fucofuranose
For diagram of dTDP-6-deoxyhexose biosynthesis, click here
Other name(s): Fcf2
Systematic name: dTDP-α-D-fucopyranose furanomutase
Comments: The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Q., Ding, P., Perepelov, A.V., Xu, Y., Wang, Y., Knirel, Y.A., Wang, L. and Feng, L. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70 (2008) 1358–1367. [DOI] [PMID: 19019146]
[EC 5.4.99.59 created 2013]
 
 
EC 5.4.99.60     
Accepted name: cobalt-precorrin-8 methylmutase
Reaction: cobalt-precorrin-8 = cobyrinate
For diagram of anaerobic corrin biosynthesis (part 2), click here
Other name(s): cbiC (gene name)
Systematic name: precorrin-8 11,12-methylmutase
Comments: The enzyme catalyses the the conversion of cobalt-precorrin-8 to cobyrinate by methyl rearrangement, a step in the anaerobic (early cobalt insertion) pathway of adenosylcobalamin biosynthesis. The equivalent enzyme in the aerobic pathway is EC 5.4.99.61, precorrin-8X methylmutase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Roessner, C.A., Warren, M.J., Santander, P.J., Atshaves, B.P., Ozaki, S., Stolowich, N.J., Iida, K., Scott, A.I. Expression of Salmonella typhimurium enzymes for cobinamide synthesis. Identification of the 11-methyl and 20-methyl transferases of corrin biosynthesis. FEBS Lett. 301 (1992) 73–78. [DOI] [PMID: 1451790]
2.  Roth, J.R., Lawrence, J.G., Rubenfield, M., Kieffer-Higgins, S., Church, G.M. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. J. Bacteriol. 175 (1993) 3303–3316. [DOI] [PMID: 8501034]
3.  Xue, Y., Wei, Z., Li, X. and Gong, W. The crystal structure of putative precorrin isomerase CbiC in cobalamin biosynthesis. J. Struct. Biol. 153 (2006) 307–311. [DOI] [PMID: 16427313]
4.  Moore, S.J., Lawrence, A.D., Biedendieck, R., Deery, E., Frank, S., Howard, M.J., Rigby, S.E. and Warren, M.J. Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12). Proc. Natl. Acad. Sci. USA 110 (2013) 14906–14911. [DOI] [PMID: 23922391]
[EC 5.4.99.60 created 2014]
 
 
EC 5.4.99.61     
Accepted name: precorrin-8X methylmutase
Reaction: precorrin-8X = hydrogenobyrinate
For diagram of corrin biosynthesis (part 4), click here
Other name(s): precorrin isomerase; hydrogenobyrinic acid-binding protein; cobH (gene name)
Systematic name: precorrin-8X 11,12-methylmutase
Comments: The enzyme catalyses the the conversion of precorrin-8X to hydrogenobyrinate by methyl rearrangement, a step in the aerobic (late cobalt insertion) pathway of adenosylcobalamin biosynthesis. The equivalent enzyme in the anaerobic pathway is EC 5.4.99.60, precorrin-8 methylmutase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 138238-71-8
References:
1.  Thibaut, D., Couder, M., Famechon, A., Debussche, L., Cameron, B., Crouzet, J., Blanche, F. The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8X as the substrate. J. Bacteriol. 174 (1992) 1043–1049. [DOI] [PMID: 1732194]
2.  Crouzet, J., Cameron, B., Cauchois, L., Rigault, S., Rouyez, M.C., Blanche, F. , Thibaut D., Debussche, L. Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid. J. Bacteriol. 172 (1990) 5980–5990. [DOI] [PMID: 2211521]
3.  Shipman, L.W., Li, D., Roessner, C.A., Scott, A.I. and Sacchettini, J.C. Crystal structure of precorrin-8x methyl mutase. Structure 9 (2001) 587–596. [DOI] [PMID: 11470433]
[EC 5.4.99.61 created 1999 as EC 5.4.1.2, transferred 2014 to EC 5.4.99.61]
 
 
EC 5.4.99.62     
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
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 5.4.99.63     
Accepted name: ethylmalonyl-CoA mutase
Reaction: (2R)-ethylmalonyl-CoA = (2S)-methylsuccinyl-CoA
Other name(s): Ecm
Systematic name: (2R)-ethylmalonyl-CoA CoA-carbonylmutase
Comments: The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. Requires coenzyme B12 for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Erb, T.J., Retey, J., Fuchs, G. and Alber, B.E. Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new subclade of coenzyme B12-dependent acyl-CoA mutases. J. Biol. Chem. 283 (2008) 32283–32293. [DOI] [PMID: 18819910]
[EC 5.4.99.63 created 2015]
 
 
EC 5.4.99.64     
Accepted name: 2-hydroxyisobutanoyl-CoA mutase
Reaction: 2-hydroxy-2-methylpropanoyl-CoA = (S)-3-hydroxybutanoyl-CoA
Glossary: 2-hydroxy-2-methylpropanoyl-CoA = 2-hydroxyisobutanoyl-CoA
Other name(s): hcmAB (gene names)
Systematic name: 2-hydroxy-2-methylpropanoyl-CoA mutase
Comments: The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. It consists of two subunits, the smaller one containing a cobalamin cofactor. It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yaneva, N., Schuster, J., Schafer, F., Lede, V., Przybylski, D., Paproth, T., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial acyl-CoA mutase specifically catalyzes coenzyme B12-dependent isomerization of 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA. J. Biol. Chem. 287 (2012) 15502–15511. [DOI] [PMID: 22433853]
2.  Kurteva-Yaneva, N., Zahn, M., Weichler, M.T., Starke, R., Harms, H., Muller, R.H., Strater, N. and Rohwerder, T. Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase. J. Biol. Chem. 290 (2015) 9727–9737. [DOI] [PMID: 25720495]
[EC 5.4.99.64 created 2016 as EC 5.3.3.20, transferred 2017 to EC 5.4.99.64]
 
 
EC 5.4.99.65     
Accepted name: pre-α-onocerin synthase
Reaction: (3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene = pre-α-onocerin
For diagram of α-onocerin biosynthesis, click here
Glossary: pre-α-onocerin = (21S)-21,22-epoxypolypoda-8(26)-13,17-trien-3β-ol
Other name(s): LCC
Systematic name: (3S,22S)-2,3:22,23-diepoxy-2,3,22,23-tetrahydrosqualene mutase (cyclizing, pre-α-onocerin-forming)
Comments: Isolated from the plant Lycopodium clavatum. The enzyme does not act on (3S)-2,3-epoxy-2,3-dihydrosqualene and does not form any α-onocerin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Araki, T., Saga, Y., Marugami, M., Otaka, J., Araya, H., Saito, K., Yamazaki, M., Suzuki, H. and Kushiro, T. Onocerin biosynthesis requires two highly dedicated triterpene cyclases in a fern Lycopodium clavatum. ChemBioChem 17 (2016) 288–290. [DOI] [PMID: 26663356]
[EC 5.4.99.65 created 2017]
 
 
EC 5.4.99.66     
Accepted name: α-onocerin synthase
Reaction: pre-α-onocerin = α-onocerin
For diagram of α-onocerin biosynthesis, click here
Glossary: α-onocerin = 8,14-secogammacera-8(26),14(27)-diene-3β,21α-diol
pre-α-onocerin = (21S)-21,22-epoxypolypoda-8(26)-13,17-trien-3β-ol
Other name(s): LCD
Systematic name: pre-α-onocerin mutase (cyclizing, α-onocerin-forming)
Comments: Isolated from the plant Lycopodium clavatum.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Araki, T., Saga, Y., Marugami, M., Otaka, J., Araya, H., Saito, K., Yamazaki, M., Suzuki, H. and Kushiro, T. Onocerin biosynthesis requires two highly dedicated triterpene cyclases in a fern Lycopodium clavatum. ChemBioChem 17 (2016) 288–290. [DOI] [PMID: 26663356]
[EC 5.4.99.66 created 2017]
 
 
EC 5.4.99.67     
Accepted name: 4-amino-4-deoxychorismate mutase
Reaction: 4-amino-4-deoxychorismate = 4-amino-4-deoxyprephenate
Other name(s): cmlD (gene name); papB (gene name)
Systematic name: 4-amino-4-deoxychorismate pyruvatemutase
Comments: The enzyme, characterized from the bacteria Streptomyces venezuelae and Streptomyces pristinaespiralis, participates in the biosynthesis of the antibiotics chloramphenicol and pristinamycin IA, respectively. cf. EC 5.4.99.5, chorismate mutase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Blanc, V., Gil, P., Bamas-Jacques, N., Lorenzon, S., Zagorec, M., Schleuniger, J., Bisch, D., Blanche, F., Debussche, L., Crouzet, J. and Thibaut, D. Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I. Mol. Microbiol. 23 (1997) 191–202. [PMID: 9044253]
2.  He, J., Magarvey, N., Piraee, M. and Vining, L.C. The gene cluster for chloramphenicol biosynthesis in Streptomyces venezuelae ISP5230 includes novel shikimate pathway homologues and a monomodular non-ribosomal peptide synthetase gene. Microbiology 147 (2001) 2817–2829. [PMID: 11577160]
[EC 5.4.99.67 created 2019]
 
 


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