Dihydrodipicolinate synthase

From Wikipedia, the free encyclopedia

In enzymology, a dihydrodipicolinate synthase (EC 4.2.1.52) is an enzyme that catalyzes the chemical reaction

L-aspartate 4-semialdehyde + pyruvate $\rightleftharpoons$ (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H₂O

Thus, the two substrates of this enzyme are L-aspartate 4-semialdehyde and pyruvate, whereas its two products are (S)-2,3-dihydropyridine-2,6-dicarboxylate and H₂O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and cyclizing; (S)-2,3-dihydropyridine-2,6-dicarboxylate-forming]. Other names in common use include dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and, and cyclizing). 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, 16 structures have been solved for this class of enzymes, with PDB accession codes 1DHP, 1O5K, 1S5T, 1S5V, 1S5W, 1XKY, 1XL9, 1XXX, 1YXC, 1YXD, 2A6L, 2A6N, 2ATS, 2D5K, 2EHH, and 2PCQ.

[edit] References

IUBMB entry for 4.2.1.52
BRENDA references for 4.2.1.52 (Recommended.)
PubMed references for 4.2.1.52
PubMed Central references for 4.2.1.52
Google Scholar references for 4.2.1.52
Shedlarski JG, Gilvarg C (1970). "The pyruvate-aspartic semialdehyde condensing enzyme of Escherichia coli". J. Biol. Chem. 245: 1362–73. PMID 4910051.
Yugari Y, Gilvarg C (1965). "The condensation step in diaminopimelate synthesis". J. Biol. Chem. 240: 4710–6. PMID 5321309.