(R)-2-hydroxyacid dehydrogenase

From Wikipedia, the free encyclopedia

(R)-2-hydroxyacid dehydrogenase

Identifiers

Databases

PDB structures

Search
PMC	articles
PubMed	articles
NCBI	proteins

In enzymology, a (R)-2-hydroxyacid dehydrogenase (EC 1.1.1.272) is an enzyme that catalyzes the chemical reaction

(2R)-3-sulfolactate + NAD(P)⁺

\rightleftharpoons

3-sulfopyruvate + NAD(P)H + H⁺

The 3 substrates of this enzyme are (2R)-3-sulfolactic acid, NAD⁺, and NADP⁺, whereas its 4 products are 3-sulfopyruvic acid, NADH, NADPH, and H⁺. This enzyme is important in the metabolism of archaea, particularly their biosynthesis of coenzymes such as coenzyme M, tetrahydromethanopterin and methanofuran.^[1]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is (R)-2-hydroxyacid:NAD(P)⁺ oxidoreductase. Other names in common use include (R)-sulfolactate:NAD(P)⁺ oxidoreductase, L-sulfolactate dehydrogenase, ComC, and (R)-sulfolactate dehydrogenase.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1RFM.

References

^ Graupner M, Xu H, White RH (2000). "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea". J. Bacteriol. 182 (13): 3688–92. doi:10.1128/JB.182.13.3688-3692.2000. PMC 94539. PMID 10850983.

Graupner M, White RH (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 (1): 169–73. doi:10.1016/S0167-4838(01)00220-5. PMID 11451450.
Graham DE, White RH (2002). "Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics". Nat. Prod. Rep. 19 (2): 133–47. doi:10.1039/b103714p. PMID 12013276.

v t e 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: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
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 Alcohol 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

This EC 1.1.1 enzyme-related article is a stub. You can help Wikipedia by expanding it.

Categories:

Hidden categories: