IPR006254
Isocitrate lyase
InterPro entry
Short name | Isocitrate_lyase |
Overlapping homologous superfamilies |
Description
Isocitrate lyase (
4.1.3.1)
[1, 2] is an enzyme that catalyzes the conversion of isocitrate to succinate and glyoxylate. This is the first step in the glyoxylate bypass, an alternative to the tricarboxylic acid cycle (also known as the TCA cycle) in bacteria, fungi and plants. A cysteine, a histidine and a glutamate or aspartate have been found to be important for the enzyme's catalytic activity. Only one cysteine residue is conserved between the sequences of the fungal, plant and bacterial enzymes; it is located in the middle of a conserved hexapeptide.
Mitochondrial 2-methylisocitrate lyase ICL2 from the yeast Saccharomyces cerevisiae does not act on isocitrate but on 2-methylisocitrate. It catalyses the formation of pyruvate and succinate during the metabolism of endogenous propionyl-CoA
[3]. Methylisocitrate lyase, mitochondrial from the filamentous fungus Aspergillus nidulans is responsible for the same reaction
[4].
References
1.High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis. Beeching JR. Protein Seq. Data Anal. 2, 463-6, (1989). PMID: 2696959
2.Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization. Atomi H, Ueda M, Hikida M, Hishida T, Teranishi Y, Tanaka A. J. Biochem. 107, 262-6, (1990). View articlePMID: 2361956
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties
Contributing Member Database Entries
- PIRSF:PIRSF001362
- NCBIfam:TIGR01346
- PANTHER:PTHR21631
- Pfam:PF00463
Representative structure
3lg3: 1.4A Crystal Structure of Isocitrate Lyase from Yersinia pestis CO92