| EC |
1.1.1.83 |
| Accepted name: |
D-malate dehydrogenase (decarboxylating) |
| Reaction: |
(R)-malate + NAD+ = pyruvate + CO2 + NADH |
| Other name(s): |
D-malate dehydrogenase; D-malic enzyme; bifunctional L(+)-tartrate dehydrogenase-D(+)-malate (decarboxylating) |
| Systematic name: |
(R)-malate:NAD+ oxidoreductase (decarboxylating) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-20-7 |
| References: |
| 1. |
Stern, J.R. and O'Brien, R.W. Oxidation D-malic and β-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes. J. Bacteriol. 98 (1969) 147–151. [PMID: 4889267] |
|
| [EC 1.1.1.83 created 1972] |
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| EC |
1.1.1.84 |
| Accepted name: |
dimethylmalate dehydrogenase |
| Reaction: |
(R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH |
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For diagram of pantothenate catabolism, click here |
| Other name(s): |
β,β-dimethylmalate dehydrogenase |
| Systematic name: |
(R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating) |
| Comments: |
Requires K+ or NH4+ and Mn2+ or Co2+; also acts on (R)-malate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-21-8 |
| References: |
| 1. |
Magee, P.T. and Snell, E.E. The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to α-ketoisovalerate. Biochemistry 5 (1966) 409–416. [PMID: 4287371] |
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| [EC 1.1.1.84 created 1972] |
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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] |
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| [EC 1.1.5.10 created 2014] |
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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 |
2.8.3.20 |
| Accepted name: |
succinyl-CoA—D-citramalate CoA-transferase |
| Reaction: |
(1) succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
(2) succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
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| Glossary: |
(R)-citramalate = (2R)-2-hydroxy-2-methylbutanedioate
(R)-malate = (2R)-2-hydroxybutanedioate
(R)-malyl-CoA = (3R)-3-carboxy-3-hydroxypropanoyl-CoA |
| Other name(s): |
Sct |
| Systematic name: |
succinyl-CoA:(R)-citramalate CoA-transferase |
| Comments: |
The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Friedmann, S., Alber, B.E. and Fuchs, G. Properties of succinyl-coenzyme A:D-citramalate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188 (2006) 6460–6468. [DOI] [PMID: 16952935] |
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| [EC 2.8.3.20 created 2014] |
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| EC |
4.2.1.31 |
| Accepted name: |
maleate hydratase |
| Reaction: |
(R)-malate = maleate + H2O |
| Other name(s): |
D-malate hydro-lyase; malease; (R)-malate hydro-lyase |
| Systematic name: |
(R)-malate hydro-lyase (maleate-forming) |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37290-71-4 |
| References: |
| 1. |
Britten, J.S., Morell, H. and Taggart, J.V. Anion activation of maleate hydratase. Biochim. Biophys. Acta 185 (1969) 220–227. [DOI] [PMID: 5796106] |
| 2. |
Sacks, W. and Jensen, C.O. Malease, a hydrase from corn kernals. J. Biol. Chem. 192 (1951) 231–236. [PMID: 14917669] |
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| [EC 4.2.1.31 created 1972] |
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