S
IPR018523

Isocitrate lyase/phosphorylmutase, conserved site

InterPro entry
Short nameIsocitrate_lyase_ph_CS

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 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.

Other enzymes also belong to this family including carboxyvinyl-carboxyphosphonate phosphorylmutase (
2.7.8.23
) which catalyses the conversion of 1-carboxyvinyl carboxyphosphonate to 3-(hydrohydroxyphosphoryl) pyruvate carbon dioxide, and phosphoenolpyruvate mutase (
5.4.2.9
), which is involved in the biosynthesis of phosphinothricin tripeptide antiobiotics.

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

  • None

cellular component

  • None

Cross References

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.