Dihydrodipicolinate reductase

From Wikipedia, the free encyclopedia

In enzymology, a dihydrodipicolinate reductase (EC 1.3.1.26) is an enzyme that catalyzes the chemical reaction

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ $\rightleftharpoons$ 2,3-dihydrodipicolinate + NAD(P)H + H⁺

The 3 substrates of this enzyme are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, NAD⁺, and NADP⁺, whereas its 4 products are 2,3-dihydrodipicolinate, NADH, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)+ oxidoreductase. Other names in common use include dihydrodipicolinic acid reductase, and 2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase. 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, 11 structures have been solved for this class of enzymes, with PDB accession codes 1ARZ, 1C3V, 1DIH, 1DRU, 1DRV, 1DRW, 1P9L, 1VM6, 1YL5, 1YL6, and 1YL7.

[edit] References

IUBMB entry for 1.3.1.26
BRENDA references for 1.3.1.26 (Recommended.)
PubMed references for 1.3.1.26
PubMed Central references for 1.3.1.26
Google Scholar references for 1.3.1.26
Farkas W, Gilvarg C (1965). "The reduction step in diaminopimelic acid biosynthesis". J. Biol. Chem. 240: 4717–22. PMID 4378965.
Tamir H (1971). "Dihydrodipicolinic acid reductase (Escherichia coli)". Methods Enzymol. 17B: 134–139.