L-2-hydroxycarboxylate dehydrogenase (NAD+)

L-2-hydroxycarboxylate dehydrogenase (NAD⁺) (EC 1.1.1.337, (R)-sulfolactate:NAD⁺ oxidoreductase, L-sulfolactate dehydrogenase, (R)-sulfolactate dehydrogenase, L-2-hydroxyacid dehydrogenase (NAD⁺), ComC) is an enzyme with systematic name (2S)-2-hydroxycarboxylate:NAD+ oxidoreductase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

(2S)-2-hydroxycarboxylate + NAD⁺

\rightleftharpoons

2-oxocarboxylate + NADH + H⁺

The enzyme from the archaeon Methanocaldococcus jannaschii uses as a substrate multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate.

References

↑ Graupner, M.; Xu, H.; White, R. H. (2000). "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea". J. Bacteriol. 182: 3688–3692. doi:10.1128/JB.182.13.3688-3692.2000. PMC 94539. PMID 10850983.
↑ Graupner, M.; White, R. H. (2001). "The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea". Biochim. Biophys. Acta. 1548: 169–173. doi:10.1016/S0167-4838(01)00220-5. PMID 11451450.
↑ Graham, D. E.; White, R. H. (2002). "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Nat. Prod. Rep. 19: 133–147. doi:10.1039/b103714p. PMID 12013276.
↑ Rein, U.; Gueta, R.; Denger, K.; Ruff, J.; Hollemeyer, K.; Cook, A. M. (2005). "Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA". Microbiology. 151 (Pt 3): 737–747. doi:10.1099/mic.0.27548-0. PMID 15758220.

External links

L-2-hydroxycarboxylate dehydrogenase (NAD ) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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