Valine dehydrogenase (NADP+)

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In enzymology, a valine dehydrogenase (NADP+) (EC 1.4.1.8) is an enzyme that catalyzes the chemical reaction

L-valine + H₂O + NADP⁺ $\rightleftharpoons$ 3-methyl-2-oxobutanoate + NH₃ + NADPH + H⁺

The 3 substrates of this enzyme are L-valine, H₂O, and NADP⁺, whereas its 4 products are 3-methyl-2-oxobutanoate, NH₃, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-valine:NADP+ oxidoreductase (deaminating). Other names in common use include valine dehydrogenase (nicotinanide adenine dinucleotide phosphate), and valine dehydrogenase (NADP+).

[edit] References

IUBMB entry for 1.4.1.8
BRENDA references for 1.4.1.8 (Recommended.)
PubMed references for 1.4.1.8
PubMed Central references for 1.4.1.8
Google Scholar references for 1.4.1.8
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Kagan ZS, Poliakov VA, Kretovich VL (1968). "[Soluble valine dehydrogenase from roots of plant seedings]". Biokhimiia. 33: 89–96. PMID 4385962.
Kagan ZS, Poliakov VA, Kretovich VL (1969). "[Purification and properties of valine dehydrogenase]". Biokhimiia. 34: 59–65. PMID 4389825.
Behal V (1988). "Isolation and characterization of valine dehydrogenase from Streptomyces aureofaciens". J. Bacteriol. 170: 5192–6. PMID 3182727.