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)
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 created 1972]
Accepted name: dimethylmalate dehydrogenase
Reaction: (R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH
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.
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]
[EC created 1972]
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.
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. [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. [PMID: 236454]
[EC created 2014]
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, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate.
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. [PMID: 26774271]
[EC created 2017]
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
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.
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. [PMID: 16952935]
[EC created 2014]
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)
1.  Britten, J.S., Morell, H. and Taggart, J.V. Anion activation of maleate hydratase. Biochim. Biophys. Acta 185 (1969) 220–227. [PMID: 5796106]
2.  Sacks, W. and Jensen, C.O. Malease, a hydrase from corn kernals. J. Biol. Chem. 192 (1951) 231–236. [PMID: 14917669]
[EC created 1972]