Methylisocitrate lyase

From Wikipedia, the free encyclopedia

In enzymology, a methylisocitrate lyase (EC 4.1.3.30) is an enzyme that catalyzes the chemical reaction

(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate $\rightleftharpoons$ succinate + pyruvate

Hence, this enzyme has one substrate, (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate, and two products, succinate and pyruvate.

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 (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase (succinate-forming). Other names in common use include 2-methylisocitrate lyase, MICL, and (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase. This enzyme participates in propanoate metabolism.

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

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1MUM, 1O5Q, 1OQF, 1UJQ, 1XG3, and 1XG4.

[edit] References

IUBMB entry for 4.1.3.30
BRENDA references for 4.1.3.30 (Recommended.)
PubMed references for 4.1.3.30
PubMed Central references for 4.1.3.30
Google Scholar references for 4.1.3.30
Tabuchi T and Satoh T (1976). "Distinction between isocitrate lyase and methylisocitrate lyase in Candida lipolytica". Agric. Biol. Chem. 40: 1863–1869.
Tabuchi T and Satoh T (1977). "Purification and properties of methylisocitrate lyase, a key enzyme in propionate metabolism, from Candida lipolytica". Agric. Biol. Chem. 41: 169–174.