Isocitrate lyase

From Wikipedia, the free encyclopedia

In enzymology, an isocitrate lyase (EC 4.1.3.1) is an enzyme that catalyzes the chemical reaction

isocitrate $\rightleftharpoons$ succinate + glyoxylate

Hence, this enzyme has one substrate, isocitrate, and two products, succinate and glyoxylate.

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is isocitrate glyoxylate-lyase (succinate-forming). Other names in common use include isocitrase, isocitritase, isocitratase, threo-Ds-isocitrate glyoxylate-lyase, and isocitrate glyoxylate-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

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

[edit] Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1DQU, 1F61, 1F8I, 1F8M, and 1IGW.

[edit] References

IUBMB entry for 4.1.3.1
BRENDA references for 4.1.3.1 (Recommended.)
PubMed references for 4.1.3.1
PubMed Central references for 4.1.3.1
Google Scholar references for 4.1.3.1
McFadden BA and Howes WV (1963). "Crystallisation and some properties of isocitrate lyase from Pseudomonas indigofera". J. Biol. Chem. 238: 1737–1742.
Shiio I, Shiio T and McFadden BA (1965). "Isocitrate lyase from Pseudomonas indigofera. I. Preparation, amino acid composition and molecular weight". Biochim. Biophys. Acta 96: 114–122.
VICKERY HB (1962). "A suggested new nomenclature for the isomers of isocitric acid". J. Biol. Chem. 237: 1739–41. PMID 13925783.