The Enzyme Database

Displaying entries 51-66 of 66.

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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]
 
 


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