EC |
1.1.1.28 |
Accepted name: |
D-lactate dehydrogenase |
Reaction: |
(R)-lactate + NAD+ = pyruvate + NADH + H+ |
Other name(s): |
lactic acid dehydrogenase; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase |
Systematic name: |
(R)-lactate:NAD+ oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-36-8 |
References: |
1. |
Dennis, D. and Kaplan, N.O. D and L-lactic acid dehydrogenase in Lactobacillus plantarum. J. Biol. Chem. 235 (1960) 810–818. [PMID: 13815938] |
|
[EC 1.1.1.28 created 1961] |
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|
|
EC
|
1.1.1.222
|
Transferred entry: | (R)-4-hydroxyphenyllactate dehydrogenase. Now included with EC 1.1.1.110, aromatic 2-oxoacid reductase
|
[EC 1.1.1.222 created 1989, deleted 2018] |
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|
|
|
EC |
1.1.2.4 |
Accepted name: |
D-lactate dehydrogenase (cytochrome) |
Reaction: |
(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+ |
Other name(s): |
lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase |
Systematic name: |
(R)-lactate:cytochrome-c 2-oxidoreductase |
Comments: |
A flavoprotein (FAD). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-79-6 |
References: |
1. |
Gregolin, C. and Singer, T.P. The lactate dehydrogenase of yeast. III. D-(-)-Lactate cytochrome c reductase, a zinc-flavoprotein from aerobic yeast. Biochim. Biophys. Acta 67 (1963) 201–218. [PMID: 13950255] |
2. |
Gregolin, C., Singer, T.P., Kearney, E.B. and Boeri, E. The formation and enzymatic properties of the various lactic dehydrogenases of yeast. Ann. N.Y. Acad. Sci. 94 (1961) 780–797. [DOI] [PMID: 13901630] |
3. |
Nygaard, A.P. D-(-)-Lactate cytochrome c reductase, a flavoprotein from yeast. J. Biol. Chem. 236 (1961) 920–925. [PMID: 13729965] |
4. |
Nygaard, A.P. Lactate dehydrogenases of yeast. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 557–565. |
|
[EC 1.1.2.4 created 1961] |
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|
EC |
1.1.2.5 |
Accepted name: |
D-lactate dehydrogenase (cytochrome c-553) |
Reaction: |
(R)-lactate + 2 ferricytochrome c-553 = pyruvate + 2 ferrocytochrome c-553 + 2 H+ |
Systematic name: |
(R)-lactate:cytochrome-c-553 2-oxidoreductase |
Comments: |
The enzyme from the sulfate-reducing bacterium Desulfovibrio vulgaris can also act on (R)-2-hydroxybutanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-79-6 |
References: |
1. |
Ogata, M., Arihara, K. and Yagi, T. D-Lactate dehydrogenase of Desulfovibrio vulgaris. J. Biochem. (Tokyo) 89 (1981) 1423–1431. [PMID: 7275946] |
|
[EC 1.1.2.5 created 1989] |
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|
|
|
EC |
1.1.5.10 |
Accepted name: |
D-2-hydroxyacid dehydrogenase (quinone) |
Reaction: |
(R)-2-hydroxyacid + a quinone = 2-oxoacid + a quinol |
Other name(s): |
(R)-2-hydroxy acid dehydrogenase; (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase; D-lactate dehydrogenase (ambiguous) |
Systematic name: |
(R)-2-hydroxyacid:quinone oxidoreductase |
Comments: |
The enzyme from mammalian kidney contains one mole of FAD per mole of enzyme.(R)-lactate, (R)-malate and meso-tartrate are good substrates. Ubiquinone-1 and the dye 2,6-dichloroindophenol can act as acceptors; NAD+ and NADP+ are not acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Tubbs, P.K. and Greville, G.D. Dehydrogenation of D-lactate by a soluble enzyme from kidney mitochondria. Biochim. Biophys. Acta 34 (1959) 290–291. [DOI] [PMID: 13839714] |
2. |
Tubbs, P.K. and Greville, G.D. The oxidation of D-α-hydroxy acids in animal tissues. Biochem. J. 81 (1961) 104–114. [PMID: 13922962] |
3. |
Cammack, R. Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase. Biochem. J. 115 (1969) 55–64. [PMID: 5359443] |
4. |
Cammack, R. D-2-hydroxy acid dehydrogenase from animal tissue. Methods Enzymol. 41 (1975) 323–329. [DOI] [PMID: 236454] |
|
[EC 1.1.5.10 created 2014] |
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|
|
|
EC |
1.1.5.12 |
Accepted name: |
D-lactate dehydrogenase (quinone) |
Reaction: |
(R)-lactate + a quinone = pyruvate + a quinol |
Other name(s): |
dld (gene name) |
Systematic name: |
(R)-lactate:quinone 2-oxidoreductase |
Comments: |
The enzyme is an FAD-dependent peripheral membrane dehydrogenase that participates in respiration. Electrons derived from D-lactate oxidation are transferred to the membrane soluble quinone pool. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kohn, L.D. and Kaback, H.R. Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from Escherichia coli. J. Biol. Chem. 248 (1973) 7012–7017. [PMID: 4582730] |
2. |
Futai, M. Membrane D-lactate dehydrogenase from Escherichia coli. Purification and properties. Biochemistry 12 (1973) 2468–2474. [PMID: 4575624] |
3. |
Matsushita, K. and Kaback, H.R. D-Lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase. Biochemistry 25 (1986) 2321–2327. [PMID: 3013300] |
4. |
Peersen, O.B., Pratt, E.A., Truong, H.T., Ho, C. and Rule, G.S. Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study. Biochemistry 29 (1990) 3256–3262. [PMID: 2185834] |
5. |
Dym, O., Pratt, E.A., Ho, C. and Eisenberg, D. The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc. Natl. Acad. Sci. USA 97 (2000) 9413–9418. [DOI] [PMID: 10944213] |
|
[EC 1.1.5.12 created 2017] |
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|
EC |
1.1.99.6 |
Accepted name: |
D-lactate dehydrogenase (acceptor) |
Reaction: |
(R)-lactate + acceptor = pyruvate + reduced acceptor |
Other name(s): |
D-2-hydroxy acid dehydrogenase; D-2-hydroxy-acid dehydrogenase; (R)-2-hydroxy-acid:acceptor 2-oxidoreductase |
Systematic name: |
(R)-lactate:acceptor 2-oxidoreductase |
Comments: |
The zinc flavoprotein (FAD) from the archaeon Archaeoglobus fulgidus cannot utilize NAD+, cytochrome c, methylene blue or dimethylnaphthoquinone as acceptors. In vitro it is active with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-83-5 |
References: |
1. |
Reed, D.W. and Hartzell, P.L. The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn2+ flavoprotein. J. Bacteriol. 181 (1999) 7580–7587. [PMID: 10601217] |
|
[EC 1.1.99.6 created 1965, modified 2013] |
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EC |
1.1.99.14 |
Accepted name: |
glycolate dehydrogenase |
Reaction: |
glycolate + acceptor = glyoxylate + reduced acceptor |
Other name(s): |
glycolate oxidoreductase; glycolic acid dehydrogenase; glycolate:(acceptor) 2-oxidoreductase |
Systematic name: |
glycolate:acceptor 2-oxidoreductase |
Comments: |
Also acts on (R)-lactate. 2,6-Dichloroindophenol and phenazine methosulfate can act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37368-32-4 |
References: |
1. |
Lord, J.M. Glycolate oxidoreductase in Escherichia coli. Biochim. Biophys. Acta 267 (1972) 227–237. [DOI] [PMID: 4557653] |
|
[EC 1.1.99.14 created 1978] |
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|
EC |
1.1.99.39 |
Accepted name: |
D-2-hydroxyglutarate dehydrogenase |
Reaction: |
(R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor |
Other name(s): |
D2HGDH (gene name) |
Systematic name: |
(R)-2-hydroxyglutarate:acceptor 2-oxidoreductase |
Comments: |
Contains FAD. The enzyme has no activity with NAD+ or NADP+, and was assayed in vitro using artificial electron acceptors. It has lower activity with (R)-lactate, (R)-2-hydroxybutyrate and meso-tartrate, and no activity with the (S) isomers. The mammalian enzyme is stimulated by Zn2+, Co2+ and Mn2+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Engqvist, M., Drincovich, M.F., Flugge, U.I. and Maurino, V.G. Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and β-oxidation pathways. J. Biol. Chem. 284 (2009) 25026–25037. [DOI] [PMID: 19586914] |
2. |
Achouri, Y., Noel, G., Vertommen, D., Rider, M.H., Veiga-Da-Cunha, M. and Van Schaftingen, E. Identification of a dehydrogenase acting on D-2-hydroxyglutarate. Biochem. J. 381 (2004) 35–42. [DOI] [PMID: 15070399] |
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[EC 1.1.99.39 created 2013] |
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EC |
1.1.99.40 |
Accepted name: |
(R)-2-hydroxyglutarate—pyruvate transhydrogenase |
Reaction: |
(R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate |
Other name(s): |
DLD3 (gene name) |
Systematic name: |
(R)-2-hydroxyglutarate:pyruvate oxidoreductase [(R)-lactate-forming] |
Comments: |
The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Becker-Kettern, J., Paczia, N., Conrotte, J.F., Kay, D.P., Guignard, C., Jung, P.P. and Linster, C.L. Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its degradation to D-lactate formation via a cytosolic transhydrogenase. J. Biol. Chem. 291 (2016) 6036–6058. [DOI] [PMID: 26774271] |
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[EC 1.1.99.40 created 2017] |
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|
EC |
3.1.6.17 |
Accepted name: |
D-lactate-2-sulfatase |
Reaction: |
(R)-2-O-sulfolactate + H2O = (R)-lactate + sulfate |
Other name(s): |
(S)-2-O-sulfolactate 2-sulfohydrolase (incorrect stereochemistry) |
Systematic name: |
(R)-2-O-sulfolactate 2-sulfohydrolase |
Comments: |
Highly specific. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93586-05-1 |
References: |
1. |
Crescenzi, A.M.V., Dodgson, K.S. and White, G.F. Purification and some properties of the D-lactate-2-sulphatase of Pseudomonas syringae GG. Biochem. J. 223 (1984) 487–494. [PMID: 6497859] |
|
[EC 3.1.6.17 created 1989] |
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EC |
3.4.13.22 |
Accepted name: |
D-Ala-D-Ala dipeptidase |
Reaction: |
D-Ala-D-Ala + H2O = 2 D-Ala |
Other name(s): |
D-alanyl-D-alanine dipeptidase; vanX D-Ala-D-Ala dipeptidase; VanX |
Comments: |
A Zn2+-dependent enzyme [4]. The enzyme protects Enterococcus faecium from the antibiotic vancomycin, which can bind to the -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan pentapeptide (see diagram). This enzyme reduces the availability of the free dipeptide D-Ala-D-Ala, which is the precursor for this pentapeptide sequence, allowing D-Ala-(R)-lactate (for which vancomycin has much less affinity) to be added to the cell wall instead [2,3]. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates [2]. Belongs in peptidase family M15. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Reynolds, P.E., Depardieu, F., Dutka-Malen, S., Arthur, M. and Courvalin, P. Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine. Mol. Microbiol. 13 (1994) 1065–1070. [DOI] [PMID: 7854121] |
2. |
Wu, Z., Wright, G.D. and Walsh, C.T. Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 34 (1995) 2455–2463. [PMID: 7873524] |
3. |
McCafferty, D.G., Lessard, I.A. and Walsh, C.T. Mutational analysis of potential zinc-binding residues in the active site
of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry 36 (1997) 10498–10505. [DOI] [PMID: 9265630] |
4. |
Bussiere, D.E., Pratt, S.D., Katz, L., Severin, J.M., Holzman, T. and Park, C.H. The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. Mol. Cell. 2 (1998) 75–84. [DOI] [PMID: 9702193] |
5. |
Tan, A.L., Loke, P. and Sim, T.S. Molecular cloning and functional characterisation of VanX, a D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2). Res. Microbiol. 153 (2002) 27–32. [DOI] [PMID: 11881895] |
6. |
Matthews, M.L., Periyannan, G., Hajdin, C., Sidgel, T.K., Bennett, B. and Crowder, M.W. Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid-freeze quench EPR studies on the Co(II)-substituted enzyme. J. Am. Chem. Soc. 128 (2006) 13050–13051. [DOI] [PMID: 17017774] |
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[EC 3.4.13.22 created 2006] |
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EC |
3.5.1.124 |
Accepted name: |
protein deglycase |
Reaction: |
(1) an Nω-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + lactate (2) an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate (3) an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + lactate |
Glossary: |
2-oxopropanal = methylglyoxal |
Other name(s): |
PARK7 (gene name); DJ-1 protein; yhbO (gene name); yajL (gene name); glyoxylase III (incorrect) |
Systematic name: |
a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming] |
Comments: |
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Misra, K., Banerjee, A.B., Ray, S. and Ray, M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem. J. 305 (1995) 999–1003. [PMID: 7848303] |
2. |
Subedi, K.P., Choi, D., Kim, I., Min, B. and Park, C. Hsp31 of Escherichia coli K-12 is glyoxalase III. Mol. Microbiol. 81 (2011) 926–936. [DOI] [PMID: 21696459] |
3. |
Richarme, G., Mihoub, M., Dairou, J., Bui, L.C., Leger, T. and Lamouri, A. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290 (2015) 1885–1897. [DOI] [PMID: 25416785] |
4. |
Mihoub, M., Abdallah, J., Gontero, B., Dairou, J. and Richarme, G. The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 463 (2015) 1305–1310. [DOI] [PMID: 26102038] |
5. |
Abdallah, J., Mihoub, M., Gautier, V. and Richarme, G. The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 470 (2016) 282–286. [DOI] [PMID: 26774339] |
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[EC 3.5.1.124 created 2016] |
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EC |
4.2.1.54 |
Accepted name: |
lactoyl-CoA dehydratase |
Reaction: |
(R)-lactoyl-CoA = acryloyl-CoA + H2O |
Other name(s): |
lactoyl coenzyme A dehydratase; lactyl-coenzyme A dehydrase; lactyl CoA dehydratase; acrylyl coenzyme A hydratase; lactoyl-CoA hydro-lyase |
Systematic name: |
(R)-lactoyl-CoA hydro-lyase (acryloyl-CoA-forming) |
Comments: |
A bacterial enzyme that is involved in propanoate fermentation (also known as the acrylate pathway). |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 9031-12-3 |
References: |
1. |
Baldwin, R.L., Wood, W.A. and Emery, R.S. Lactate metabolism by Peptostreptococcus elsdenii: evidence for lactyl coenzyme a dehydrase. Biochim. Biophys. Acta 97 (1965) 202–213. [DOI] [PMID: 14292829] |
2. |
Schweiger, G. and Buckel, W. On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum. FEBS Lett. 171 (1984) 79–84. [DOI] [PMID: 6586495] |
3. |
Kuchta, R.D. and Abeles, R.H. Lactate reduction in Clostridium propionicum. Purification and properties of lactyl-CoA dehydratase. J. Biol. Chem. 260 (1985) 13181–13189. [PMID: 4055736] |
4. |
Kuchta, R.D., Hanson, G.R., Holmquist, B. and Abeles, R.H. Fe-S centers in lactyl-CoA dehydratase. Biochemistry 25 (1986) 7301–7307. [PMID: 3026450] |
5. |
Hofmeister, A.E. and Buckel, W. (R)-Lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA. Eur. J. Biochem. 206 (1992) 547–552. [DOI] [PMID: 1597194] |
|
[EC 4.2.1.54 created 1972, modified 2012] |
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|
EC |
4.2.1.126 |
Accepted name: |
N-acetylmuramic acid 6-phosphate etherase |
Reaction: |
(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O |
Other name(s): |
MurNAc-6-P etherase; MurQ |
Systematic name: |
(R)-lactate hydro-lyase (adding N-acetyl-D-glucosamine 6-phosphate; N-acetylmuramate 6-phosphate-forming) |
Comments: |
This enzyme, along with EC 2.7.1.170, anhydro-N-acetylmuramic acid kinase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium’s own cell wall murein during cell wall recycling. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Jaeger, T., Arsic, M. and Mayer, C. Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase". J. Biol. Chem. 280 (2005) 30100–30106. [DOI] [PMID: 15983044] |
2. |
Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M. and Park, J.T. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187 (2005) 3643–3649. [DOI] [PMID: 15901686] |
3. |
Uehara, T., Suefuji, K., Jaeger, T., Mayer, C. and Park, J.T. MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall. J. Bacteriol. 188 (2006) 1660–1662. [DOI] [PMID: 16452451] |
4. |
Hadi, T., Dahl, U., Mayer, C. and Tanner, M.E. Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling. Biochemistry 47 (2008) 11547–11558. [DOI] [PMID: 18837509] |
5. |
Jaeger, T. and Mayer, C. N-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism. Cell. Mol. Life Sci. 65 (2008) 928–939. [DOI] [PMID: 18049859] |
|
[EC 4.2.1.126 created 2011] |
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|
|
|
EC |
4.2.1.130 |
Accepted name: |
D-lactate dehydratase |
Reaction: |
(R)-lactate = 2-oxopropanal + H2O |
Glossary: |
methylglyoxal = 2-oxopropanal
(R)-lactate = D-lactate
|
Other name(s): |
glyoxylase III; GLO3 |
Systematic name: |
(R)-lactate hydro-lyase |
Comments: |
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hasim, S., Hussin, N.A., Alomar, F., Bidasee, K.R., Nickerson, K.W. and Wilson, M.A. A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans. J. Biol. Chem. 289 (2014) 1662–1674. [DOI] [PMID: 24302734] |
2. |
Zhao, Q., Su, Y., Wang, Z., Chen, C., Wu, T. and Huang, Y. Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe. BMC Evol Biol 14:86 (2014). [DOI] [PMID: 24758716] |
|
[EC 4.2.1.130 created 2011] |
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|
|
EC |
5.1.2.1 |
Accepted name: |
lactate racemase |
Reaction: |
(S)-lactate = (R)-lactate |
Other name(s): |
lacticoracemase; hydroxyacid racemase; lactic acid racemase; larA (gene name) |
Systematic name: |
lactate racemase |
Comments: |
The enzyme has been characterized from the bacterium Lactobacillus plantarum and appears to be restricted to lactic acid bacteria. It contains a unique nickel-containing cofactor, pyridinium-3-thioamide-5-thiocarboxylate mononucleotide Ni pincer complex. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-05-9 |
References: |
1. |
Huennekens, F.M., Mahler, H.R. and Nordmann, J. Studies on the cyclophorase system. XVII. The occurrence and properties of an α-hydroxy acid racemase. Arch. Biochem. 30 (1951) 77–89. [PMID: 14800428] |
2. |
Kitahara, K., Obayashi, A. and Fukui, S. Racemase I cell-free racemase. Enzymologia 15 (1953) 259–266. |
3. |
Goffin, P., Deghorain, M., Mainardi, J.L., Tytgat, I., Champomier-Verges, M.C., Kleerebezem, M. and Hols, P. Lactate racemization as a rescue pathway for supplying D-lactate to the cell wall biosynthesis machinery in Lactobacillus plantarum. J. Bacteriol. 187 (2005) 6750–6761. [DOI] [PMID: 16166538] |
4. |
Desguin, B., Goffin, P., Viaene, E., Kleerebezem, M., Martin-Diaconescu, V., Maroney, M.J., Declercq, J.P., Soumillion, P. and Hols, P. Lactate racemase is a nickel-dependent enzyme activated by a widespread maturation system. Nat. Commun. 5:3615 (2014). [DOI] [PMID: 24710389] |
5. |
Desguin, B., Zhang, T., Soumillion, P., Hols, P., Hu, J. and Hausinger, R.P. A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase. Science 349 (2015) 66–69. [DOI] [PMID: 26138974] |
6. |
Yu, M.J. and Chen, S.L. From NAD+ to nickel pincer complex: a significant cofactor evolution presented by lactate racemase. Chemistry 23 (2017) 7545–7557. [DOI] [PMID: 28374531] |
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[EC 5.1.2.1 created 1961] |
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EC |
6.1.2.1 |
Accepted name: |
D-alanine—(R)-lactate ligase |
Reaction: |
D-alanine + (R)-lactate + ATP = D-alanyl-(R)-lactate + ADP + phosphate |
Glossary: |
(R)-lactate = D-lactate
D-alanyl-(R)-lactate = D-alanyl-D-lactate = (2R)-2-(D-alanyloxy)propanoic acid = (R)-2-((R)-2-aminopropanoyloxy)propanoic acid |
Other name(s): |
VanA; VanB; VanD |
Systematic name: |
D-alanine:(R)-lactate ligase (ADP-forming) |
Comments: |
The product of this enzyme, the depsipeptide D-alanyl-(R)-lactate, can be incorporated into the peptidoglycan pentapeptide instead of the usual D-alanyl-D-alanine dipeptide, which is formed by EC 6.3.2.4, D-alanine—D-alanine ligase. The resulting peptidoglycan does not bind the glycopeptide antibiotics vancomycin and teicoplanin, conferring resistance on the bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Bugg, T.D., Wright, G.D., Dutka-Malen, S., Arthur, M., Courvalin, P. and Walsh, C.T. Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry 30 (1991) 10408–10415. [PMID: 1931965] |
2. |
Meziane-Cherif, D., Badet-Denisot, M.A., Evers, S., Courvalin, P. and Badet, B. Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583. FEBS Lett. 354 (1994) 140–142. [DOI] [PMID: 7957913] |
3. |
Perichon, B., Reynolds, P. and Courvalin, P. VanD-type glycopeptide-resistant Enterococcus faecium BM4339. Antimicrob. Agents Chemother. 41 (1997) 2016–2018. [PMID: 9303405] |
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[EC 6.1.2.1 created 2010] |
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