Biology:Valine dehydrogenase (NADP+)
From HandWiki
| valine dehydrogenase (NADP) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.4.1.8 | ||||||||
| CAS number | 37255-39-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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+ [math]\displaystyle{ \rightleftharpoons }[/math] 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 (nicotinamide adenine dinucleotide phosphate), and valine dehydrogenase (NADP+).
References
- "Biosynthesis of valine by reductive amination of its keto analogue in plants". Enzymologia 30 (6): 343–66. 1966. PMID 6005410.
- "[Soluble valine dehydrogenase from roots of plant seedings]". Biokhimiia 33 (1): 89–96. 1968. PMID 4385962.
- "[Purification and properties of valine dehydrogenase]". Biokhimiia 34 (1): 59–65. 1969. PMID 4389825.
- Behal V; Vancura, A; Volc, J; Neuzil, J; Flieger, M; Basarová, G; Bĕhal, V (1988). "Isolation and characterization of valine dehydrogenase from Streptomyces aureofaciens". J. Bacteriol. 170 (11): 5192–6. doi:10.1128/jb.170.11.5192-5196.1988. PMID 3182727.
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