Leucine dehydrogenase

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leucine dehydrogenase
leucine dehydrogenase oktamer, Sporosarcina psychrophila
EC no.
CAS no.9082-71-7
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a leucine dehydrogenase (EC is an enzyme that catalyzes the chemical reaction

L-leucine + H2O + NAD+ 4-methyl-2-oxopentanoate + NH3 + NADH + H+

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.

Structural studies[edit]

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


  • Sanwal BD, Zink MW (1961). "L-Leucine dehydrogenase of Bacillus cereus". Arch. Biochem. Biophys. 94 (3): 430–435. doi:10.1016/0003-9861(61)90070-4. PMID 13746411.
  • Zink MW, Sanwal BD (1962). "The distribution and substrate specificity of L-leucine dehydrogenase". Arch. Biochem. Biophys. 99: 72–77. doi:10.1016/0003-9861(62)90245-X.