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⁺ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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

[edit] References

IUBMB entry for 1.4.1.9
BRENDA references for 1.4.1.9 (Recommended.)
PubMed references for 1.4.1.9
PubMed Central references for 1.4.1.9
Google Scholar references for 1.4.1.9
Sanwal BD and Zink MW (1961). "L-Leucine dehydrogenase of Bacillus cereus". Arch. Biochem. Biophys. 94: 430–435.
Zink MW and 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.