Diaminopimelate dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a diaminopimelate dehydrogenase (EC 1.4.1.16) is an enzyme that catalyzes the chemical reaction

meso-2,6-diaminoheptanedioate + H₂O + NADP⁺ $\rightleftharpoons$ 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.

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

[edit] 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.

[edit] References

IUBMB entry for 1.4.1.16
BRENDA references for 1.4.1.16 (Recommended.)
PubMed references for 1.4.1.16
PubMed Central references for 1.4.1.16
Google Scholar references for 1.4.1.16
Misono H, Togawa H, Yamamoto T, Soda K (1976). "Occurrence of meso-alpha, epsilon-diaminopimelate dehydrogenase in Bacillus sphaericus". Biochem. Biophys. Res. Commun. 72: 89–93. 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: 22–7. PMID 762012.