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- ******************************
- * Isocitrate 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 perfectly conserved hexapeptide that can be used
- as a signature pattern for this type of enzyme.
-
- -Consensus pattern: K-K-C-G-H-M
- [C is a putative active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: May 1991 / Text revised.
-
- [ 1] Beeching J.R.
- Protein Seq. Data Anal. 2:463-466(1989).
- [ 2] Atomi H., Ueda M., Hikida M., Hishida T., Teranishi Y., Tanaka A.
- J. Biochem. 107:262-266(1990).
-