EC |
5.1.3.19 |
Accepted name: |
chondroitin-glucuronate 5-epimerase |
Reaction: |
chondroitin D-glucuronate = dermatan L-iduronate |
|
For diagram of the later stages of chondroitin biosynthesis, click here |
Other name(s): |
polyglucuronate 5-epimerase; dermatan-sulfate 5-epimerase; urunosyl C-5 epimerase; chondroitin D-glucuronosyl 5-epimerase |
Systematic name: |
chondroitin-D-glucuronate 5-epimerase |
Comments: |
Not identical with EC 5.1.3.17 heparosan-N-sulfate-glucuronate 5-epimerase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 70766-66-4 |
References: |
1. |
Malmström, A. and Åberg, L. Biosynthesis of dermatan sulphate. Assay and properties of the uronosyl C-5 epimerase. Biochem. J. 201 (1982) 489–493. [PMID: 7092807] |
|
[EC 5.1.3.19 created 1986] |
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|
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EC |
5.1.3.20 |
Accepted name: |
ADP-glyceromanno-heptose 6-epimerase |
Reaction: |
ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose |
Systematic name: |
ADP-L-glycero-D-manno-heptose 6-epimerase |
Comments: |
Requires NAD+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 85030-75-7 |
References: |
1. |
Ding, L., Seto, B.L., Ahmed, S.A., Coleman, W.G., Jr. Purification and properties of the Escherichia coli K-12 NAD-dependent nucleotide diphosphosugar epimerase, ADP-L-glycero-D-manno-heptose 6-epimerase. J. Biol. Chem. 269 (1994) 24384–24390. [PMID: 7929099] |
2. |
Raetz, C.R.H. Biochemistry of endotoxins. Annu. Rev. Biochem. 58 (1990) 129–170. [DOI] [PMID: 1695830] |
|
[EC 5.1.3.20 created 1999] |
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|
|
|
EC |
5.1.3.21 |
Accepted name: |
maltose epimerase |
Reaction: |
α-maltose = β-maltose |
Systematic name: |
maltose 1-epimerase |
Comments: |
The enzyme catalyses the interconversion of α and β anomers of maltose more effectively than those of disaccharides such as lactose and cellobiose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 166799-98-0 |
References: |
1. |
Shirokane, Y. and Suzuki, M. A novel enzyme, maltose 1-epimerase from Lactobacillus brevis IFO 3345. FEBS Lett. 367 (1995) 177–179. [DOI] [PMID: 7796915] |
|
[EC 5.1.3.21 created 2002] |
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|
|
|
EC |
5.1.3.22 |
Accepted name: |
L-ribulose-5-phosphate 3-epimerase |
Reaction: |
L-ribulose 5-phosphate = L-xylulose 5-phosphate |
|
For diagram of the bacterial pathway of ascorbic-acid catabolism, click here |
Other name(s): |
L-xylulose 5-phosphate 3-epimerase; UlaE; SgaU |
Systematic name: |
L-ribulose-5-phosphate 3-epimerase |
Comments: |
Along with EC 4.1.1.85, 3-dehydro-L-gulonate-6-phosphate decarboxylase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 1114425-98-7 |
References: |
1. |
Yew, W.S. and Gerlt, J.A. Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol. 184 (2002) 302–306. [DOI] [PMID: 11741871] |
|
[EC 5.1.3.22 created 2005] |
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|
EC |
5.1.3.23 |
Accepted name: |
UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase |
Reaction: |
UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate = UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronate |
|
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here |
Glossary: |
UDP-α-D-GlcNAc3NAcA = UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid
UDP-α-D-ManNAc3NAcA = UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid |
Other name(s): |
UDP-GlcNAc3NAcA 2-epimerase; UDP-α-D-GlcNAc3NAcA 2-epimerase; 2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerase; WbpI; WlbD |
Systematic name: |
2,3-diacetamido-2,3-dideoxy-α-D-glucuronate 2-epimerase |
Comments: |
This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of the B-band lipopolysaccharide of Pseudomonas aeroginosa serotype O5 and of the band-A trisaccharide of Bordetella pertussis, both important respiratory pathogens [1]. The enzyme is highly specific as UDP-α-D-GlcNAc, UDP-α-D-GlcNAcA (UDP-2-acetamido-2-deoxy-α-D-glucuronic acid) and UDP-α-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucose) cannot act as substrates [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Westman, E.L., McNally, D.J., Rejzek, M., Miller, W.L., Kannathasan, V.S., Preston, A., Maskell, D.J., Field, R.A., Brisson, J.R. and Lam, J.S. Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 123–130. [DOI] [PMID: 17346239] |
2. |
Westman, E.L., McNally, D.J., Rejzek, M., Miller, W.L., Kannathasan, V.S., Preston, A., Maskell, D.J., Field, R.A., Brisson, J.R. and Lam, J.S. Erratum report: Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 625. |
3. |
Sri Kannathasan, V., Staines, A.G., Dong, C.J., Field, R.A., Preston, A.G., Maskell, D.J. and Naismith, J.H. Overexpression, purification, crystallization and data collection on the Bordetella pertussis wlbD gene product, a putative UDP-GlcNAc 2′-epimerase. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1310–1312. [PMID: 11526328] |
|
[EC 5.1.3.23 created 2007] |
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|
|
|
EC |
5.1.3.24 |
Accepted name: |
N-acetylneuraminate epimerase |
Reaction: |
N-acetyl-α-neuraminate = N-acetyl-β-neuraminate (oveall reaction) (1a) N-acetyl-α-neuraminate = aceneuramate (1b) aceneuramate = N-acetyl-β-neuraminate |
Glossary: |
aceneuramate = (4S,5R,6R,7S,8R)-5-acetamido-4,6,7,8,9-pentahydroxy-2-oxononanoate |
Other name(s): |
sialic acid epimerase; N-acetylneuraminate mutarotase; NanM; NanQ |
Systematic name: |
N-acetyl-α-neuraminate 2-epimerase |
Comments: |
Sialoglycoconjugates present in vertebrates are linked exclusively by α-linkages and are released in α form during degradation. This enzyme accelerates maturotation to the β form via the open form (which also occurs as a slow spontaneous reaction). The open form is necessary for further metabolism by the bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Severi, E., Müller, A., Potts, J.R., Leech, A., Williamson, D., Wilson, K.S. and Thomas, G.H. Sialic acid mutarotation is catalyzed by the Escherichia coli β-propeller protein YjhT. J. Biol. Chem. 283 (2008) 4841–4849. [DOI] [PMID: 18063573] |
2. |
Kentache, T., Thabault, L., Deumer, G., Haufroid, V., Frederick, R., Linster, C.L., Peracchi, A., Veiga-da-Cunha, M., Bommer, G.T. and Van Schaftingen, E. The metalloprotein YhcH is an anomerase providing N-acetylneuraminate aldolase with the open form of its substrate. J. Biol. Chem. :100699 (2021). [DOI] [PMID: 33895133] |
|
[EC 5.1.3.24 created 2011, modified 2021] |
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|
EC |
5.1.3.25 |
Accepted name: |
dTDP-L-rhamnose 4-epimerase |
Reaction: |
dTDP-6-deoxy-β-L-talose = dTDP-β-L-rhamnose |
Glossary: |
dTDP-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
|
Other name(s): |
dTDP-4-L-rhamnose 4-epimerase; wbiB (gene name) |
Systematic name: |
dTDP-6-deoxy-β-L-talose 4-epimerase |
Comments: |
The equilibrium is strongly towards dTDP-β-L-rhamnose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yoo, H.G., Kwon, S.Y., Karki, S. and Kwon, H.J. A new route to dTDP-6-deoxy-L-talose and dTDP-L-rhamnose: dTDP-L-rhamnose 4-epimerase in Burkholderia thailandensis. Bioorg. Med. Chem. Lett. 21 (2011) 3914–3917. [DOI] [PMID: 21640586] |
|
[EC 5.1.3.25 created 2012] |
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|
EC |
5.1.3.26 |
Accepted name: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase |
Reaction: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol |
Other name(s): |
GlcNAc-P-P-Und epimerase; GlcNAc-P-P-Und 4-epimerase; gne (gene name) |
Systematic name: |
N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase |
Comments: |
The enzyme is involved in biosynthesis of the repeating tetrasaccharide unit of the O-antigen produced by some Gram-negative bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rush, J.S., Alaimo, C., Robbiani, R., Wacker, M. and Waechter, C.J. A novel epimerase that converts GlcNAc-P-P-undecaprenol to GalNAc-P-P-undecaprenol in Escherichia coli O157. J. Biol. Chem. 285 (2010) 1671–1680. [DOI] [PMID: 19923219] |
|
[EC 5.1.3.26 created 2013] |
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EC |
5.1.3.27 |
Accepted name: |
dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase |
Reaction: |
dTDP-4-dehydro-6-deoxy-α-D-glucose = dTDP-4-dehydro-6-deoxy-α-D-gulose |
|
For diagram of dTDP-6-deoxy-α-D-allose biosynthesis, click here and for diagram of dTDP-6-deoxyhexose biosynthesis, click here |
Glossary: |
dTDP-4-dehydro-6-deoxy-α-D-gulose = dTDP-4-dehydro-6-deoxy-α-D-allose |
Other name(s): |
dTDP-deoxyglucose 3-epimerase; dTDP-4-keto-6-deoxy-D-glucose 3-epimerase; dTDP-4-keto-6-deoxyglucose 3-epimerase; gerF (gene name); tylJ (gene name); chmJ (gene name); mydH (gene name) |
Systematic name: |
dTDP-4-dehydro-6-deoxy-α-D-glucose 3-epimerase |
Comments: |
The enzyme is involved in the biosynthetic pathway of dTDP-6-deoxy-α-D-allose, which is converted to mycinose after attachment to the aglycones of several macrolide antibiotics, including tylosin, chalcomycin, dihydrochalcomycin, and mycinamicin II. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Sohng, J.K., Kim, H.J., Nam, D.H., Lim, D.O., Han, J.M., Lee, H.J. and Yoo, J.C. Cloning, expression, and biological function of a dTDP-deoxyglucose epimerase (gerF) gene from Streptomyces sp. GERI-155. Biotechnol. Lett. 26 (2004) 185–191. [PMID: 15049360] |
2. |
Thuy, T.T., Liou, K., Oh, T.J., Kim, D.H., Nam, D.H., Yoo, J.C. and Sohng, J.K. Biosynthesis of dTDP-6-deoxy-β-D-allose, biochemical characterization of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC 0041BP. Glycobiology 17 (2007) 119–126. [DOI] [PMID: 17053005] |
3. |
Kubiak, R.L., Phillips, R.K., Zmudka, M.W., Ahn, M.R., Maka, E.M., Pyeatt, G.L., Roggensack, S.J. and Holden, H.M. Structural and functional studies on a 3′-epimerase involved in the biosynthesis of dTDP-6-deoxy-D-allose. Biochemistry 51 (2012) 9375–9383. [DOI] [PMID: 23116432] |
|
[EC 5.1.3.27 created 2013] |
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|
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EC |
5.1.3.28 |
Accepted name: |
UDP-N-acetyl-L-fucosamine synthase |
Reaction: |
UDP-2-acetamido-2,6-dideoxy-β-L-talose = UDP-N-acetyl-β-L-fucosamine
|
|
For diagram of UDP-N-acetyl-β-L-fucosamine biosynthesis, click here |
Glossary: |
UDP-2-acetamido-2,6-dideoxy-β-L-talose = UDP-N-acetyl-β-L-pneumosamine |
Other name(s): |
WbjD; Cap5G |
Systematic name: |
UDP-2-acetamido-2,6-dideoxy-β-L-talose 2-epimerase |
Comments: |
Isolated from the bacteria Pseudomonas aeruginosa and Staphylococcus aureus. Involved in bacterial polysaccharide biosynthesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kneidinger, B., O'Riordan, K., Li, J., Brisson, J.R., Lee, J.C. and Lam, J.S. Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications for the UDP-N-acetyl-L-fucosamine biosynthetic pathway. J. Biol. Chem. 278 (2003) 3615–3627. [DOI] [PMID: 12464616] |
2. |
Mulrooney, E.F., Poon, K.K., McNally, D.J., Brisson, J.R. and Lam, J.S. Biosynthesis of UDP-N-acetyl-L-fucosamine, a precursor to the biosynthesis of lipopolysaccharide in Pseudomonas aeruginosa serotype O11. J. Biol. Chem. 280 (2005) 19535–19542. [DOI] [PMID: 15778500] |
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[EC 5.1.3.28 created 2014] |
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EC |
5.1.3.29 |
Accepted name: |
L-fucose mutarotase |
Reaction: |
α-L-fucopyranose = β-L-fucopyranose |
|
For diagram of L-fucose catabolism, click here |
Other name(s): |
FucU; fucose mutarotase; FucM |
Systematic name: |
L-fucose 1-epimerase |
Comments: |
This enzyme shows no 1-epimerase activity with D-glucose, L-rhamnose and D-fucose (cf. EC 5.1.3.3, aldose 1-epimerase) [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
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] |
2. |
Park, D., Ryu, K.S., Choi, D., Kwak, J. and Park, C. Characterization and role of fucose mutarotase in mammalian cells. Glycobiology 17 (2007) 955–962. [DOI] [PMID: 17602138] |
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[EC 5.1.3.29 created 2014] |
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EC |
5.1.3.30 |
Accepted name: |
D-psicose 3-epimerase |
Reaction: |
D-psicose = D-fructose
|
Glossary: |
D-psicose = D-ribo-hex-2-ulose = D-allulose |
Other name(s): |
D-allulose 3-epimerase; DPEase (ambiguous) |
Systematic name: |
D-psicose 3-epimerase |
Comments: |
The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose (cf. EC 5.1.3.31, D-tagatose 3-epimerase). The enzyme from the bacterium Clostridium scindens requires Mn2+ [1], whereas the enzymes from the bacteria Clostridium cellulolyticum [2,5], Clostridium sp. BNL1100 [3], and Clostridium bolteae [4] require Co2+ as optimum cofactor. The enzyme from Ruminococcus sp. [6] is not dependent on the presence of metal ions, but its activity is enhanced by Mn2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Mu, W., Chu, F., Xing, Q., Yu, S., Zhou, L. and Jiang, B. Cloning, expression, and characterization of a D-psicose 3-epimerase from Clostridium cellulolyticum H10. J. Agric. Food Chem. 59 (2011) 7785–7792. [DOI] [PMID: 21663329] |
2. |
Chan, H.C., Zhu, Y., Hu, Y., Ko, T.P., Huang, C.H., Ren, F., Chen, C.C., Ma, Y., Guo, R.T. and Sun, Y. Crystal structures of D-psicose 3-epimerase from Clostridium cellulolyticum H10 and its complex with ketohexose sugars. Protein Cell 3 (2012) 123–131. [DOI] [PMID: 22426981] |
3. |
Zhu, Y., Men, Y., Bai, W., Li, X., Zhang, L., Sun, Y. and Ma, Y. Overexpression of D-psicose 3-epimerase from Ruminococcus sp. in Escherichia coli and its potential application in D-psicose production. Biotechnol. Lett. 34 (2012) 1901–1906. [DOI] [PMID: 22760176] |
4. |
Zhang, W., Fang, D., Xing, Q., Zhou, L., Jiang, B. and Mu, W. Characterization of a novel metal-dependent D-psicose 3-epimerase from Clostridium scindens 35704. PLoS One 8:e62987 (2013). [DOI] [PMID: 23646168] |
5. |
Mu, W., Zhang, W., Fang, D., Zhou, L., Jiang, B. and Zhang, T. Characterization of a D-psicose-producing enzyme, D-psicose 3-epimerase, from Clostridium sp. Biotechnol. Lett. 35 (2013) 1481–1486. [DOI] [PMID: 23660703] |
6. |
Jia, M., Mu, W., Chu, F., Zhang, X., Jiang, B., Zhou, L.L. and Zhang, T. A D-psicose 3-epimerase with neutral pH optimum from Clostridium bolteae for D-psicose production: cloning, expression, purification, and characterization. Appl. Microbiol. Biotechnol. 98 (2014) 717–725. [DOI] [PMID: 23644747] |
|
[EC 5.1.3.30 created 2014] |
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|
EC |
5.1.3.31 |
Accepted name: |
D-tagatose 3-epimerase |
Reaction: |
(1) D-tagatose = D-sorbose (2) D-psicose = D-fructose |
|
For diagram of tagatose metabolism, click here |
Glossary: |
D-psicose = D-ribo-hex-2-ulose |
Other name(s): |
L-ribulose 3-epimerase; ketose 3-epimerase |
Systematic name: |
D-tagatose 3-epimerase |
Comments: |
The enzymes isolated from the bacteria Pseudomonas cichorii [2], Pseudomonas sp. ST-24 [1], Rhodobacter sphaeroides [3] and Mesorhizobium loti [4] catalyse the epimerization of various ketoses at the C-3 position, interconverting D-fructose and D-psicose, D-tagatose and D-sorbose, D-ribulose and D-xylulose, and L-ribulose and L-xylulose. The specificity depends on the species. The enzymes from Pseudomonas cichorii and Rhodobacter sphaeroides require Mn2+ [2,3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Itoh, H., Okaya, H., Khan, A. R., Tajima, S., Hayakawa, S., Izumori, K. Purification and characterization of D-tagatose 3-epimerase from Pseudomonas sp. ST-24. Biosci. Biotechnol. Biochem. 58 (1994) 2168–2171. |
2. |
Yoshida, H., Yamada, M., Nishitani, T., Takada, G., Izumori, K. and Kamitori, S. Crystal structures of D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and D-fructose. J. Mol. Biol. 374 (2007) 443–453. [DOI] [PMID: 17936787] |
3. |
Zhang, L., Mu, W., Jiang, B. and Zhang, T. Characterization of D-tagatose-3-epimerase from Rhodobacter sphaeroides that converts D-fructose into D-psicose. Biotechnol. Lett. 31 (2009) 857–862. [DOI] [PMID: 19205890] |
4. |
Uechi, K., Takata, G., Fukai, Y., Yoshihara, A. and Morimoto, K. Gene cloning and characterization of L-ribulose 3-epimerase from Mesorhizobium loti and its application to rare sugar production. Biosci. Biotechnol. Biochem. 77 (2013) 511–515. [DOI] [PMID: 23470755] |
|
[EC 5.1.3.31 created 2014] |
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|
EC |
5.1.3.32 |
Accepted name: |
L-rhamnose mutarotase |
Reaction: |
α-L-rhamnopyranose = β-L-rhamnopyranose |
Other name(s): |
rhamnose 1-epimerase; type-3 mutarotase; YiiL |
Systematic name: |
L-rhamnopyranose 1-epimerase |
Comments: |
The enzyme is specific for L-rhamnopyranose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
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] |
2. |
Ryu, K.S., Kim, J.I., Cho, S.J., Park, D., Park, C., Cheong, H.K., Lee, J.O. and Choi, B.S. Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase. J. Mol. Biol. 349 (2005) 153–162. [DOI] [PMID: 15876375] |
|
[EC 5.1.3.32 created 2014] |
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|
EC |
5.1.3.33 |
Accepted name: |
2-epi-5-epi-valiolone epimerase |
Reaction: |
2-epi-5-epi-valiolone = 5-epi-valiolone |
|
For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone= (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexanone
5-epi-valiolone = (2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexanone |
Other name(s): |
CetB; EVE |
Systematic name: |
2-epi-5-epi-valiolone 2-epimerase |
Comments: |
The enzyme, characterized from the bacterium Actinomyces sp. Lu 9419, is involved in the biosynthesis of the antitumor agent cetoniacytone A. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wu, X., Flatt, P.M., Xu, H. and Mahmud, T. Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419. ChemBioChem 10 (2009) 304–314. [DOI] [PMID: 19101977] |
|
[EC 5.1.3.33 created 2015] |
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|
|
|
EC |
5.1.3.34 |
Accepted name: |
monoglucosyldiacylglycerol epimerase |
Reaction: |
a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = a 1,2-diacyl-3-O-(β-D-galactopyranosyl)-sn-glycerol |
Glossary: |
a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = β-monoglucosyldiacylglycerol = GlcDG
a 1,2-diacyl-3-O-(β-D-galactopyranosyl)-sn-glycerol = β-monogalactosyldiacylglycerol = MGDG |
Other name(s): |
glucolipid epimerase; mgdE (gene name) |
Systematic name: |
1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol 4-epimerase |
Comments: |
The enzyme, characterized from cyanobacteria, is involves in the biosynthesis of galactolipids found in their photosynthetic membranes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sato, N. and Murata, N. Lipid biosynthesis in the blue-green alga, Anabaena variabilis II. Fatty acids and lipid molecular species. Biochim. Biophys. Acta 710 (1982) 279–289. |
2. |
Awai, K., Ohta, H. and Sato, N. Oxygenic photosynthesis without galactolipids. Proc. Natl. Acad. Sci. USA 111 (2014) 13571–13575. [DOI] [PMID: 25197079] |
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[EC 5.1.3.34 created 2015] |
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EC |
5.1.3.35 |
Accepted name: |
2-epi-5-epi-valiolone 7-phosphate 2-epimerase |
Reaction: |
2-epi-5-epi-valiolone 7-phosphate = 5-epi-valiolone 7-phosphate |
|
For diagram of valiolone biosynthesis, click here |
Glossary: |
2-epi-5-epi-valiolone 7-phosphate = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(phosphonooxymethyl)cyclohexanone
5-epi-valiolone 7-phosphate = (2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(phosphonooxymethyl)cyclohexanone
|
Other name(s): |
AcbO |
Systematic name: |
2-epi-5-epi-valiolone-7-phosphate 2-epimerase |
Comments: |
The enzyme, isolated from the bacterium Actinoplanes sp. SE 50/110, is involved in the biosynthesis of the α-glucosidase inhibitor acarbose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Zhang, C.S., Podeschwa, M., Altenbach, H.J., Piepersberg, W. and Wehmeier, U.F. The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a 2-epi-5-epi-valiolone-7-phosphate 2-epimerase. FEBS Lett. 540 (2003) 47–52. [DOI] [PMID: 12681481] |
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[EC 5.1.3.35 created 2015] |
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|
EC |
5.1.3.36 |
Accepted name: |
heparosan-glucuronate 5-epimerase |
Reaction: |
[heparosan]-D-glucuronate = [acharan]-L-iduronate |
Glossary: |
acharan = [GlcNAc-α-(1→4)-IdoA-α-(1→4)]n
heparosan = [GlcNAc-α-(1→4)-GlcA-β-(1→4)]n |
Other name(s): |
HG-5epi |
Systematic name: |
[heparosan]-D-glucuronate 5-epimerase |
Comments: |
The enzyme, characterized from the giant African snail Achatina fulica, participates in the biosynthetic pathway of acharan sulfate. Unlike EC 5.1.3.17, heparosan-N-sulfate-glucuronate 5-epimerase, it shows no activity with D-glucuronate residues in heparosan-N-sulfate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mochizuki, H., Yamagishi, K., Suzuki, K., Kim, Y.S. and Kimata, K. Heparosan-glucuronate 5-epimerase: Molecular cloning and characterization of a novel enzyme. Glycobiology 25 (2015) 735–744. [DOI] [PMID: 25677302] |
|
[EC 5.1.3.36 created 2015] |
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EC |
5.1.3.37 |
Accepted name: |
mannuronan 5-epimerase |
Reaction: |
[mannuronan]-β-D-mannuronate = [alginate]-α-L-guluronate |
Glossary: |
mannuronan = a linear polymer of β-D-mannuronate residues linked by (1-4) linkages
alginate = a linear polymer of β-D-mannuronate residues linked by (1-4) linkages, with variable amounts of its C-5 epimer α-L-guluronate. |
Other name(s): |
algG (gene name); alginate epimerase; C5-mannuronan epimerase; mannuronan C-5-epimerase |
Systematic name: |
[mannuronan]-β-D-mannuronate 5-epimerase |
Comments: |
The enzyme epimerizes the C-5 bond in some β-D-mannuronate residues in mannuronan, converting them to α-L-guluronate residues, and thus modifying the mannuronan into alginate. It is found in brown algae and alginate-producing bacterial species from the Pseudomonas and Azotobacter genera. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Franklin, M.J., Chitnis, C.E., Gacesa, P., Sonesson, A., White, D.C. and Ohman, D.E. Pseudomonas aeruginosa AlgG is a polymer level alginate C5-mannuronan epimerase. J. Bacteriol. 176 (1994) 1821–1830. [DOI] [PMID: 8144447] |
2. |
Morea, A., Mathee, K., Franklin, M.J., Giacomini, A., O'Regan, M. and Ohman, D.E. Characterization of algG encoding C5-epimerase in the alginate biosynthetic gene cluster of Pseudomonas fluorescens. Gene 278 (2001) 107–114. [DOI] [PMID: 11707327] |
3. |
Nyvall, P., Corre, E., Boisset, C., Barbeyron, T., Rousvoal, S., Scornet, D., Kloareg, B. and Boyen, C. Characterization of mannuronan C-5-epimerase genes from the brown alga Laminaria digitata. Plant Physiol. 133 (2003) 726–735. [DOI] [PMID: 14526115] |
4. |
Jain, S., Franklin, M.J., Ertesvag, H., Valla, S. and Ohman, D.E. The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa. Mol. Microbiol. 47 (2003) 1123–1133. [DOI] [PMID: 12581364] |
5. |
Douthit, S.A., Dlakic, M., Ohman, D.E. and Franklin, M.J. Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed β-helix. J. Bacteriol. 187 (2005) 4573–4583. [DOI] [PMID: 15968068] |
6. |
Wolfram, F., Kitova, E.N., Robinson, H., Walvoort, M.T., Codee, J.D., Klassen, J.S. and Howell, P.L. Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG. J. Biol. Chem. 289 (2014) 6006–6019. [DOI] [PMID: 24398681] |
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[EC 5.1.3.37 created 2015] |
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EC |
5.1.3.38 |
Accepted name: |
D-erythrulose 1-phosphate 3-epimerase |
Reaction: |
D-erythrulose 1-phosphate = L-erythrulose 1-phosphate |
Other name(s): |
eryC (gene name) |
Systematic name: |
D-erythrulose-1-phosphate 3-epimerase |
Comments: |
The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Barbier, T., Collard, F., Zuniga-Ripa, A., Moriyon, I., Godard, T., Becker, J., Wittmann, C., Van Schaftingen, E. and Letesson, J.J. Erythritol feeds the pentose phosphate pathway via three new isomerases leading to D-erythrose-4-phosphate in Brucella. Proc. Natl. Acad. Sci. USA 111 (2014) 17815–17820. [DOI] [PMID: 25453104] |
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[EC 5.1.3.38 created 2016] |
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EC
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5.1.3.39
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Deleted entry: | L-erythrulose 4-phosphate epimerase. The activity has been shown not to take place. |
[EC 5.1.3.39 created 2016, deleted 2018] |
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EC |
5.1.3.40 |
Accepted name: |
D-tagatose 6-phosphate 4-epimerase |
Reaction: |
D-tagatose 6-phosphate = D-fructose 6-phosphate |
|
For diagram of tagatose metabolism, click here |
Systematic name: |
D-tagatose 6-phosphate 4-epimerase |
Comments: |
The enzyme from Agrobacterium fabrum C58 is part of D-altritol and galactitol degradation pathways. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wichelecki, D.J., Vetting, M.W., Chou, L., Al-Obaidi, N., Bouvier, J.T., Almo, S.C. and Gerlt, J.A. ATP-binding cassette (ABC) transport system solute-binding protein-guided identification of novel D-altritol and galactitol catabolic pathways in Agrobacterium tumefaciens C58. J. Biol. Chem. 290 (2015) 28963–28976. [DOI] [PMID: 26472925] |
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[EC 5.1.3.40 created 2017] |
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EC |
5.1.3.41 |
Accepted name: |
fructoselysine 3-epimerase |
Reaction: |
N6-(D-fructosyl)-L-lysine = N6-(D-psicosyl)-L-lysine |
Other name(s): |
frlC (gene name) |
Systematic name: |
D-fructosyl-L-lysine 3-epimerase |
Comments: |
The enzyme, characterized from the bacterium Escherichia coli, is involved in the catabolism of fructoseamines, amino acid sugar complexes that are formed non-enzymically. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wiame, E. and Van Schaftingen, E. Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli. Biochem. J. 378 (2004) 1047–1052. [DOI] [PMID: 14641112] |
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[EC 5.1.3.41 created 2017] |
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EC |
5.1.3.42 |
Accepted name: |
D-glucosamine-6-phosphate 4-epimerase |
Reaction: |
D-glucosamine 6-phosphate = D-galactosamine 6-phosphate |
|
For diagram of UDP-N-acetylglucosamine biosynthesis, click here |
Other name(s): |
ST2245 (locus name) |
Systematic name: |
D-glucosamine 6-phosphate 4-epimerase |
Comments: |
The enzyme, characterized from the archaeon Sulfolobus tokodaii, participates in a pathway for the biosynthesis of UDP-N-acetyl-α-D-galactosamine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091] |
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[EC 5.1.3.42 created 2018] |
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EC |
5.1.3.43 |
Accepted name: |
sulfoquinovose mutarotase |
Reaction: |
6-sulfo-α-D-quinovose = 6-sulfo-β-D-quinovose |
Systematic name: |
6-sulfo-D-quinovose 1-epimerase |
Comments: |
The enzyme is found in bacteria that possess sulfoglycolytic pathways. The enzyme can also act on other aldohexoses such as D-galactose, D-glucose, D-glucose-6-phosphate, and D-glucuronate, but with lower efficiency. Does not act on D-mannose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Abayakoon, P., Lingford, J.P., Jin, Y., Bengt, C., Davies, G.J., Yao, S., Goddard-Borger, E.D. and Williams, S.J. Discovery and characterization of a sulfoquinovose mutarotase using kinetic analysis at equilibrium by exchange spectroscopy. Biochem. J. 475 (2018) 1371–1383. [PMID: 29535276] |
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[EC 5.1.3.43 created 2019] |
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EC |
5.1.3.44 |
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] |
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[EC 5.1.3.44 created 2020] |
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EC |
5.1.99.1 |
Accepted name: |
methylmalonyl-CoA epimerase |
Reaction: |
(R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA |
|
For diagram of the 3-hydroxypropanoate cycle, click here |
Other name(s): |
methylmalonyl-CoA racemase; methylmalonyl coenzyme A racemase; DL-methylmalonyl-CoA racemase; 2-methyl-3-oxopropanoyl-CoA 2-epimerase [incorrect] |
Systematic name: |
methylmalonyl-CoA 2-epimerase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-03-7 |
References: |
1. |
Mazumder, R., Sasakawa, T., Kaziro, Y. and Ochoa, S. Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase. J. Biol. Chem. 237 (1962) 3065–3068. [PMID: 13934211] |
2. |
Overath, P., Kellerman, G.M., Lynen, F., Fritz, H.P. and Keller, H.J. Zum Mechanismus der Umlagerung von Methylmalonyl-CoA in Succinyl-CoA. II. Versuche zur Wirkungsweise von Methylmalonyl-CoA-Isomerase and Methylmalonyl-CoA-Racemase. Biochem. Z. 335 (1962) 500–518. [PMID: 14482843] |
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[EC 5.1.99.1 created 1965, modified 1981] |
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EC |
5.1.99.2 |
Accepted name: |
16-hydroxysteroid epimerase |
Reaction: |
16α-hydroxysteroid = 16β-hydroxysteroid |
Systematic name: |
16-hydroxysteroid 16-epimerase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37318-40-4 |
References: |
1. |
Dahm, K., Lindlau, M. and Breuer, H. Steroid epimerase-a new enzyme of estrogen metabolism. Biochim. Biophys. Acta 159 (1968) 377–389. [DOI] [PMID: 5657462] |
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[EC 5.1.99.2 created 1972] |
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EC |
5.1.99.3 |
Accepted name: |
allantoin racemase |
Reaction: |
(S)(+)-allantoin = (R)(-)-allantoin |
|
For diagram of AMP catabolism, click here |
Systematic name: |
allantoin racemase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56214-40-5 |
References: |
1. |
van der Drift, L., Vogels, G.D. and van der Drift, C. Allantoin racemase: a new enzyme from Pseudomonas species. Biochim. Biophys. Acta 391 (1975) 240–248. [DOI] [PMID: 237557] |
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[EC 5.1.99.3 created 1976] |
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EC |
5.1.99.4 |
Accepted name: |
α-methylacyl-CoA racemase |
Reaction: |
(2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA |
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For diagram of cholic acid biosynthesis (sidechain), click here |
Systematic name: |
2-methylacyl-CoA 2-epimerase |
Comments: |
α-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates. Also active towards some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Not active towards free acids |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 156681-44-6 |
References: |
1. |
Schmitz, W., Fingerhut, R., Conzelmann, E. Purification and properties of an α-methylacyl-CoA racemase from rat liver. Eur. J. Biochem. 222 (1994) 313–323. [DOI] [PMID: 8020470] |
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[EC 5.1.99.4 created 1999] |
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EC |
5.1.99.5 |
Accepted name: |
hydantoin racemase |
Reaction: |
D-5-monosubstituted hydantoin = L-5-monosubstituted hydantoin |
Glossary: |
hydantoin = imidazolidine-2,4-dione |
Other name(s): |
5′-monosubstituted-hydantoin racemase; HyuA; HyuE |
Systematic name: |
D-5-monosubstituted-hydantoin racemase |
Comments: |
This enzyme, along with N-carbamoylase (EC 3.5.1.77 and EC 3.5.1.87) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [7]. The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-[2-(methylsulfanyl)ethyl]hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position [2]. In the enzyme from Sinorhizobium meliloti, Cys76 is responsible for recognition and proton retrieval of D-isomers, while Cys181 is responsible for L-isomer recognition and racemization [6]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Watabe, K., Ishikawa, T., Mukohara, Y. and Nakamura, H. Purification and characterization of the hydantoin racemase of Pseudomonas sp. strain NS671 expressed in Escherichia coli. J. Bacteriol. 174 (1992) 7989–7995. [DOI] [PMID: 1459947] |
2. |
Wiese, A., Pietzsch, M., Syldatk, C., Mattes, R. and Altenbuchner, J. Hydantoin racemase from Arthrobacter aurescens DSM 3747: heterologous expression, purification and characterization. J. Biotechnol. 80 (2000) 217–230. [DOI] [PMID: 10949312] |
3. |
Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Mingorance-Cazorla, L., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. Molecular cloning, purification, and biochemical characterization of hydantoin racemase from the legume symbiont Sinorhizobium meliloti CECT 4114. Appl. Environ. Microbiol. 70 (2004) 625–630. [DOI] [PMID: 14711700] |
4. |
Martínez-Rodríguez, S., Las Heras-Vázquez, F.J., Clemente-Jiménez, J.M. and Rodríguez-Vico, F. Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58. Biochimie 86 (2004) 77–81. [DOI] [PMID: 15016445] |
5. |
Suzuki, S., Onishi, N. and Yokozeki, K. Purification and characterization of hydantoin racemase from Microbacterium liquefaciens AJ 3912. Biosci. Biotechnol. Biochem. 69 (2005) 530–536. [DOI] [PMID: 15784981] |
6. |
Martínez-Rodríguez, S., Andújar-Sánchez, M., Neira, J.L., Clemente-Jiménez, J.M., Jara-Pérez, V., Rodríguez-Vico, F. and Las Heras-Vázquez, F.J. Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti. Protein Sci. 15 (2006) 2729–2738. [DOI] [PMID: 17132860] |
7. |
Altenbuchner, J., Siemann-Herzberg, M. and Syldatk, C. Hydantoinases and related enzymes as biocatalysts for the synthesis of unnatural chiral amino acids. Curr. Opin. Biotechnol. 12 (2001) 559–563. [DOI] [PMID: 11849938] |
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[EC 5.1.99.5 created 2008] |
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EC |
5.1.99.6 |
Accepted name: |
NAD(P)H-hydrate epimerase |
Reaction: |
(1) (6R)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide (2) (6R)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate |
Glossary: |
6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = NADHX = NADH-hydrate
6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = NADPHX = NADPH-hydrate |
Other name(s): |
NAD(P)HX epimerase |
Systematic name: |
(6R)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide 6-epimerase |
Comments: |
The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate. Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93, ATP-dependent NAD(P)H-hydrate dehydratase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Marbaix, A.Y., Noel, G., Detroux, A.M., Vertommen, D., Van Schaftingen, E. and Linster, C.L. Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair. J. Biol. Chem. 286 (2011) 41246–41252. [DOI] [PMID: 21994945] |
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[EC 5.1.99.6 created 2012] |
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EC |
5.1.99.7 |
Accepted name: |
dihydroneopterin triphosphate 2′-epimerase |
Reaction: |
7,8-dihydroneopterin 3′-triphosphate = 7,8-dihydromonapterin 3′-triphosphate |
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For diagram of monapterin biosynthesis, click here |
Glossary: |
7,8-dihydroneopterin 3′-triphosphate = (2R,3S)-3-(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)-2,3-dihydroxypropyl triphosphate
7,8-dihydromonapterin 3′-triphosphate = (2S,3S)-3-(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)-2,3-dihydroxypropyl triphosphate |
Other name(s): |
D-erythro-7,8-dihydroneopterin triphosphate epimerase; folX (gene name) |
Systematic name: |
7,8-dihydroneopterin 3′-triphosphate 2′-epimerase |
Comments: |
The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ahn, C., Byun, J. and Yim, J. Purification, cloning, and functional expression of dihydroneopterin triphosphate 2′-epimerase from Escherichia coli. J. Biol. Chem. 272 (1997) 15323–15328. [DOI] [PMID: 9182560] |
2. |
Haussmann, C., Rohdich, F., Schmidt, E., Bacher, A. and Richter, G. Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. J. Biol. Chem. 273 (1998) 17418–17424. [DOI] [PMID: 9651328] |
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[EC 5.1.99.7 created 2015] |
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EC |
5.1.99.8 |
Accepted name: |
7,8-dihydroneopterin epimerase |
Reaction: |
7,8-dihydroneopterin = 7,8-dihydromonapterin |
Glossary: |
7,8-dihydroneopterin = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one
7,8-dihydromonapterin = 2-amino-6-[(1S,2S)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one |
Systematic name: |
7,8-dihydroneopterin 2′-epimerase |
Comments: |
The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81, 7,8-dihydroneopterin oxygenase) [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Haussmann, C., Rohdich, F., Schmidt, E., Bacher, A. and Richter, G. Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. J. Biol. Chem. 273 (1998) 17418–17424. [DOI] [PMID: 9651328] |
2. |
Goyer, A., Illarionova, V., Roje, S., Fischer, M., Bacher, A. and Hanson, A.D. Folate biosynthesis in higher plants. cDNA cloning, heterologous expression, and characterization of dihydroneopterin aldolases. Plant Physiol. 135 (2004) 103–111. [DOI] [PMID: 15107504] |
3. |
Czekster, C.M. and Blanchard, J.S. One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 134 (2012) 19758–19771. [DOI] [PMID: 23150985] |
4. |
Blaszczyk, J., Lu, Z., Li, Y., Yan, H. and Ji, X. Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase. Cell Biosci 4:52 (2014). [DOI] [PMID: 25264482] |
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[EC 5.1.99.8 created 2015] |
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EC |
5.2.1.1 |
Accepted name: |
maleate isomerase |
Reaction: |
maleate = fumarate |
Systematic name: |
maleate cis-trans-isomerase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-74-9 |
References: |
1. |
Behrman, E.J. and Stanier, R.Y. The bacterial oxidation of nicotinic acid. J. Biol. Chem. 228 (1957) 923–945. [PMID: 13475371] |
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[EC 5.2.1.1 created 1961] |
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EC |
5.2.1.2 |
Accepted name: |
maleylacetoacetate isomerase |
Reaction: |
4-maleylacetoacetate = 4-fumarylacetoacetate |
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For diagram of tyrosine catabolism, click here |
Other name(s): |
maleylacetoacetic isomerase; maleylacetone isomerase; maleylacetone cis-trans-isomerase |
Systematic name: |
4-maleylacetoacetate cis-trans-isomerase |
Comments: |
Also acts on maleylpyruvate. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-75-0 |
References: |
1. |
Edwards, S.W. and Knox, W.E. Homogentisate metabolism: the isomerization of maleylacetoacetate by an enzyme which requires glutathione. J. Biol. Chem. 220 (1956) 79–91. [PMID: 13319328] |
2. |
Lack, L. Enzymic cis-trans isomerization of maleylpyruvic acid. J. Biol. Chem. 236 (1961) 2835–2840. [PMID: 14461395] |
3. |
Seltzer, S. Purification and properties of maleylacetone cis-trans isomerase from Vibrio 01. J. Biol. Chem. 248 (1973) 215–222. [PMID: 4692831] |
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[EC 5.2.1.2 created 1961] |
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EC
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5.2.1.3
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Deleted entry: | retinal isomerase. Now known to be catalysed by a pathway involving EC 1.1.1.300, NADP-retinol dehydrogenase; EC 2.3.1.135, phosphatidylcholine—retinol O-acyltransferase; EC 3.1.1.64, retinoid isomerohydrolase; and EC 1.1.1.315, 11-cis-retinol dehydrogenase. |
[EC 5.2.1.3 created 1961, modified 1976, deleted 2011] |
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EC |
5.2.1.4 |
Accepted name: |
maleylpyruvate isomerase |
Reaction: |
3-maleylpyruvate = 3-fumarylpyruvate |
Systematic name: |
3-maleylpyruvate cis-trans-isomerase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-77-2 |
References: |
1. |
Lack, L. Enzymic cis-trans isomerization of maleylpyruvic acid. J. Biol. Chem. 236 (1961) 2835–2840. [PMID: 14461395] |
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[EC 5.2.1.4 created 1965] |
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EC |
5.2.1.5 |
Accepted name: |
linoleate isomerase |
Reaction: |
9-cis,12-cis-octadecadienoate = 9-cis,11-trans-octadecadienoate |
Other name(s): |
linoleic acid isomerase |
Systematic name: |
linoleate Δ12-cis-Δ11-trans-isomerase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37318-41-5 |
References: |
1. |
Kepler, C.R. and Tove, S.B. Biohydrogenation of unsaturated fatty acids. III. Purification and properties of linoleate Δ12-cis, Δ11-trans-isomerase from Butyrivibrio fibrosolvens. J. Biol. Chem. 242 (1967) 5686–5692. [PMID: 5633396] |
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[EC 5.2.1.5 created 1972] |
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EC |
5.2.1.6 |
Accepted name: |
furylfuramide isomerase |
Reaction: |
(E)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide = (Z)-2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide |
Systematic name: |
2-(2-furyl)-3-(5-nitro-2-furyl)acrylamide cis-trans-isomerase |
Comments: |
Requires NADH. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72561-07-0 |
References: |
1. |
Tomoeda, M. and Kitamura, R. A cis-trans isomerising activity of Escherichia coli. Isomerization from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide) to its trans isomer. Biochim. Biophys. Acta 480 (1977) 315–325. [DOI] [PMID: 12827] |
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[EC 5.2.1.6 created 1978] |
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EC
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5.2.1.7
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Transferred entry: | retinol isomerase. Transferred to EC 3.1.1.64, retinoid isomerohydrolase.
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[EC 5.2.1.7 created 1989, deleted 2011] |
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EC |
5.2.1.8 |
Accepted name: |
peptidylprolyl isomerase |
Reaction: |
peptidylproline (ω=180) = peptidylproline (ω=0) |
Glossary: |
For definition of ω, click here |
Other name(s): |
PPIase; cyclophilin [misleading, see comments]; peptide bond isomerase; peptidyl-prolyl cis-trans isomerase |
Systematic name: |
peptidylproline cis-trans-isomerase |
Comments: |
The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95076-93-0 |
References: |
1. |
Fischer, G. and Bang, H. The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase. Biochim. Biophys. Acta 828 (1985) 39–42. [DOI] [PMID: 3882150] |
2. |
Fischer, G., Bang, H. and Mech, C. [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides] Biomed. Biochim. Acta 43 (1984) 1101–1111. [PMID: 6395866] |
3. |
Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. and Schmid, F.X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337 (1989) 476–478. [DOI] [PMID: 2492638] |
4. |
Takahashi, N., Hayano, T. and Suzuki, M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337 (1989) 473–475. [DOI] [PMID: 2644542] |
5. |
Hennig, L., Christner, C., Kipping, M., Schelbert, B., Rucknagel, K.P., Grabley, S., Kullertz, G. and Fischer, G. Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. Biochemistry 37 (1998) 5953–5960. [DOI] [PMID: 9558330] |
6. |
Fischer, G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33 (1994) 1415–1436. |
7. |
Harrison, R.K. and Stein, R.L. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry 29 (1990) 3813–3816. [PMID: 1693856] |
8. |
Eisenmesser, E.Z., Bosco, D.A., Akke, M. and Kern, D. Enzyme dynamics during catalysis. Science 295 (2002) 1520–1523. [DOI] [PMID: 11859194] |
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[EC 5.2.1.8 created 1989, modified 2002] |
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EC |
5.2.1.9 |
Accepted name: |
farnesol 2-isomerase |
Reaction: |
(2E,6E)-farnesol = (2Z,6E)-farnesol |
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For diagram of the biosynthesis of bisabolene-derived sesquiterpenoid, click here |
Other name(s): |
farnesol isomerase |
Systematic name: |
(2E,6E)-farnesol 2-cis-trans-isomerase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-16-2 |
References: |
1. |
Anastasis, P., Freer, I., Gilmore, C., Mackie, H., Overton, K., Picken, D. and Swanson, S. Biosynthesis of γ-bisabolene in tissue-cultures of Andrographis paniculata. Can. J. Chem. 62 (1984) 2079–2088. |
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[EC 5.2.1.9 created 1989] |
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EC |
5.2.1.10 |
Accepted name: |
2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase |
Reaction: |
cis-2-chloro-4-carboxymethylenebut-2-en-1,4-olide = trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide |
Other name(s): |
2-chlorocarboxymethylenebutenolide isomerase; chlorodienelactone isomerase |
Systematic name: |
2-chloro-4-carboxymethylenebut-2-en-1,4-olide cis-trans-isomerase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 115629-29-3 |
References: |
1. |
Schwien, U., Schmidt, E., Knackmuss, H.-J. and Reinecke, W. Degradation of chlorosubstituted aromatic-compounds by Pseudomonas sp. strain-B13 - fate of 3,5-dichlorocatechol. Arch. Microbiol. 150 (1988) 78–84. |
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[EC 5.2.1.10 created 1992] |
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EC
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5.2.1.11
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Deleted entry: | 4-hydroxyphenylacetaldehyde-oxime isomerase. The existence of this enzyme has been called into question by one of the authors of the reference cited |
[EC 5.2.1.11 created 1992, deleted 2005] |
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EC |
5.2.1.12 |
Accepted name: |
ζ-carotene isomerase |
Reaction: |
9,15,9′-tricis-ζ-carotene = 9,9′-dicis-ζ-carotene |
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For diagram of plant and cyanobacteria carotenoid biosynthesis, click here |
Other name(s): |
Z-ISO; 15-cis-ζ-carotene isomerase |
Systematic name: |
9,15,9′-tricis-ζ-carotene cis-trans-isomerase |
Comments: |
The enzyme catalyses the cis-trans isomerization of the 15-15′ carbon-carbon double bond in 9,15,9′-tricis-ζ-carotene, which is required for biosynthesis of all plant carotenoids. Requires heme b. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chen, Y., Li, F. and Wurtzel, E.T. Isolation and characterization of the Z-ISO gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiol. 153 (2010) 66–79. [DOI] [PMID: 20335404] |
2. |
Li, F., Murillo, C. and Wurtzel, E.T. Maize Y9 encodes a product essential for 15-cis-ζ-carotene isomerization. Plant Physiol. 144 (2007) 1181–1189. [DOI] [PMID: 17434985] |
3. |
Beltran, J., Kloss, B., Hosler, J.P., Geng, J., Liu, A., Modi, A., Dawson, J.H., Sono, M., Shumskaya, M., Ampomah-Dwamena, C., Love, J.D. and Wurtzel, E.T. Control of carotenoid biosynthesis through a heme-based cis-trans isomerase. Nat. Chem. Biol. 11 (2015) 598–605. [DOI] [PMID: 26075523] |
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[EC 5.2.1.12 created 2011] |
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EC |
5.2.1.13 |
Accepted name: |
prolycopene isomerase |
Reaction: |
7,9,7′,9′-tetracis-lycopene = all-trans-lycopene |
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For diagram of plant and cyanobacteria carotenoid biosynthesis, click here |
Glossary: |
prolycopene = 7,9,7′,9′-tetracis-lycopene |
Other name(s): |
CRTISO; carotene cis-trans isomerase; ZEBRA2 (gene name); carotene isomerase; carotenoid isomerase |
Systematic name: |
7,9,7′,9′-tetracis-lycopene cis-trans-isomerase |
Comments: |
Requires FADH2 [1]. The enzyme is involved in carotenoid biosynthesis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yu, Q., Ghisla, S., Hirschberg, J., Mann, V. and Beyer, P. Plant carotene cis-trans isomerase CRTISO: a new member of the FADred-dependent flavoproteins catalyzing non-redox reactions. J. Biol. Chem. 286 (2011) 8666–8676. [DOI] [PMID: 21209101] |
2. |
Li, Q., Farre, G., Naqvi, S., Breitenbach, J., Sanahuja, G., Bai, C., Sandmann, G., Capell, T., Christou, P. and Zhu, C. Cloning and functional characterization of the maize carotenoid isomerase and β-carotene hydroxylase genes and their regulation during endosperm maturation. Transgenic Res. 19 (2010) 1053–1068. [DOI] [PMID: 20221689] |
3. |
Isaacson, T., Ronen, G., Zamir, D. and Hirschberg, J. Cloning of tangerine from tomato reveals a carotenoid isomerase essential for the production of β-carotene and xanthophylls in plants. Plant Cell 14 (2002) 333–342. [DOI] [PMID: 11884678] |
4. |
Chai, C., Fang, J., Liu, Y., Tong, H., Gong, Y., Wang, Y., Liu, M., Wang, Y., Qian, Q., Cheng, Z. and Chu, C. ZEBRA2, encoding a carotenoid isomerase, is involved in photoprotection in rice. Plant Mol. Biol. 75 (2011) 211–221. [DOI] [PMID: 21161331] |
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[EC 5.2.1.13 created 2011] |
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EC |
5.2.1.14 |
Accepted name: |
β-carotene isomerase |
Reaction: |
all-trans-β-carotene = 9-cis-β-carotene |
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For diagram of strigol biosynthesis, click here |
Other name(s): |
DWARF27 (gene name) |
Systematic name: |
β-carotene 9-cis-all-trans isomerase |
Comments: |
The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Lin, H., Wang, R., Qian, Q., Yan, M., Meng, X., Fu, Z., Yan, C., Jiang, B., Su, Z., Li, J. and Wang, Y. DWARF27, an iron-containing protein required for the biosynthesis of strigolactones, regulates rice tiller bud outgrowth. Plant Cell 21 (2009) 1512–1525. [DOI] [PMID: 19470589] |
2. |
Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348–1351. [DOI] [PMID: 22422982] |
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[EC 5.2.1.14 created 2012] |
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EC |
5.3.1.1 |
Accepted name: |
triose-phosphate isomerase |
Reaction: |
D-glyceraldehyde 3-phosphate = glycerone phosphate |
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Glossary: |
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate |
Other name(s): |
phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase |
Systematic name: |
D-glyceraldehyde-3-phosphate aldose-ketose-isomerase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-78-3 |
References: |
1. |
Meyer-Arendt, E., Beisenherz, G. and Bücher, T. Triosephosphate isomerase. Naturwissenschaften 40 (1953) 59. |
2. |
Meyerhof, O. and Beck, L.V. Triosephosphate isomerase. J. Biol. Chem. 156 (1944) 109–120. |
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[EC 5.3.1.1 created 1961] |
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EC
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5.3.1.2
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Deleted entry: | erythrose isomerase |
[EC 5.3.1.2 created 1961, deleted 1976] |
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