From Wikipedia, the free encyclopedia
valine dehydrogenase (NADP)
Identifiers
EC no. 1.4.1.8
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

L-valine + H2O + NADP+ 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

  • Kagan ZS, Kretovich WL, Polyakov WA (1966). "Biosynthesis of valine by reductive amination of its keto analogue in plants". Enzymologia. 30 (6): 343–66. PMID  6005410.
  • Kagan ZS, Poliakov VA, Kretovich VL (1968). "[Soluble valine dehydrogenase from roots of plant seedings]". Biokhimiia. 33 (1): 89–96. PMID  4385962.
  • Kagan ZS, Poliakov VA, Kretovich VL (1969). "[Purification and properties of valine dehydrogenase]". Biokhimiia. 34 (1): 59–65. 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. PMC  211589. PMID  3182727.


From Wikipedia, the free encyclopedia
valine dehydrogenase (NADP)
Identifiers
EC no. 1.4.1.8
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

L-valine + H2O + NADP+ 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

  • Kagan ZS, Kretovich WL, Polyakov WA (1966). "Biosynthesis of valine by reductive amination of its keto analogue in plants". Enzymologia. 30 (6): 343–66. PMID  6005410.
  • Kagan ZS, Poliakov VA, Kretovich VL (1968). "[Soluble valine dehydrogenase from roots of plant seedings]". Biokhimiia. 33 (1): 89–96. PMID  4385962.
  • Kagan ZS, Poliakov VA, Kretovich VL (1969). "[Purification and properties of valine dehydrogenase]". Biokhimiia. 34 (1): 59–65. 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. PMC  211589. PMID  3182727.



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