F
IPR006254

Isocitrate lyase

InterPro entry
Short nameIsocitrate_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

3.The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism. Luttik MA, Kotter P, Salomons FA, van der Klei IJ, van Dijken JP, Pronk JT. J Bacteriol 182, 7007-13, (2000). PMID: 11092862

4.2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes. Brock M, Darley D, Textor S, Buckel W. Eur J Biochem 268, 3577-86, (2001). PMID: 11422389

GO terms

cellular component

  • None

Cross References

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