| diaminopimelate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.16 | ||||||||
| CAS no. | 60894-21-5 | ||||||||
| 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 diaminopimelate dehydrogenase ( EC 1.4.1.16) is an enzyme that catalyzes the chemical reaction
- meso-2,6-diaminoheptanedioate + H2O + NADP+ L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+
The 3 substrates of this enzyme are meso-2,6-diaminoheptanedioate, H2O, and NADP+, whereas its 4 products are L-2-amino-6-oxoheptanedioate, 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 meso-2,6-diaminoheptanedioate:NADP+ oxidoreductase (deaminating). Other names in common use include meso-alpha,epsilon-diaminopimelate dehydrogenase, and meso-diaminopimelate dehydrogenase. This enzyme participates in lysine biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1DAP, 1F06, 2DAP, and 3DAP.
References
- Misono H, Togawa H, Yamamoto T, Soda K (1976). "Occurrence of meso-alpha, epsilon-diaminopimelate dehydrogenase in Bacillus sphaericus". Biochem. Biophys. Res. Commun. 72 (1): 89–93. doi: 10.1016/0006-291X(76)90964-5. PMID 10904.
- Misono H, Togawa H, Yamamoto T, Soda K (1979). "Meso-alpha,epsilon-diaminopimelate D-dehydrogenase: distribution and the reaction product". J. Bacteriol. 137 (1): 22–7. doi: 10.1128/JB.137.1.22-27.1979. PMC 218413. PMID 762012.
