Leucine dehydrogenase
| leucine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 leucine dehydrogenase oktamer, Sporosarcina psychrophila | |||||||||
| 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 | ||||||||
| |||||||||
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+
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.
References
[edit]- 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.
