Diaminopimelate dehydrogenase

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

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

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.

This page was last edited on 26 August 2023, at 13:49