PROSITE documentation PDOC00145Isocitrate lyase signature
Isocitrate lyase (EC 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 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 that can be used as a signature pattern for this type of enzyme.
ICL is evolutionary related to two other type of enzymes:
- Carboxyphosphonoenolpyruvate phosphonomutase (EC 2.7.8.23) (CPEP mutase). It forms a carbon-phosphorus bond in a rearrangement leading from carboxyphosphonoenolpyruvate (CPEP) to phosphinopyruvate.
- Phosphoenolpyruvate phosphomutase (EC 5.4.2.9) (PEP mutase) [3]. It forms a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate.
May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Beeching J.R. |
| Title | High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis. | |
| Source | Protein Seq. Data Anal. 2:463-466(1989). | |
| PubMed ID | 2696959 |
| 2 | Authors | Atomi H. Ueda M. Hikida M. Hishida T. Teranishi Y. Tanaka A. |
| Title | Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization. | |
| Source | J. Biochem. 107:262-266(1990). | |
| PubMed ID | 2361956 |
| 3 | Authors | Huang K. Li Z. Jia Y. Dunaway-Mariano D. Herzberg O. |
| Title | Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate. | |
| Source | Structure 7:539-548(1999). | |
| PubMed ID | 10378273 |
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