Leucine dehydrogenase
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In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction
- L-leucine + H2O + NAD+ 4-methyl-2-oxopentanoate + NH3 + NADH + H+
Quick Facts Identifiers, EC no. ...
leucine dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.4.1.9 | ||||||||
CAS no. | 9082-71-7 | ||||||||
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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The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, 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-leucine:NAD+ oxidoreductase (deaminating). Other names in common use include L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, and LeuDH. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis.