Isocitrate lyase family

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1f61A:9-427 1f8mC:9-427 1f8iD:9-427 1igwD:7-434 1dquA:14-535 1zlpB:104-184 1ujqB:80-161 1o5qA:80-161 1xg4A:80-161 1xg3C:80-161 1mumA:80-161 1oqfB:80-161 1mzxA:80-161

Isocitrate lyase family
Isocitrate lyase family
Identifiers
Symbol	ICL
Pfam	PF00463
InterPro	IPR000918
PROSITE	PDOC00145
SCOP2	1f8m / SCOPe / SUPFAM
CDD	cd00377
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1f61A:9-427 1f8mC:9-427 1f8iD:9-427 1igwD:7-434 1dquA:14-535 1zlpB:104-184 1ujqB:80-161 1o5qA:80-161 1xg4A:80-161 1xg3C:80-161 1mumA:80-161 1oqfB:80-161 1mzxA:80-161

Isocitrate lyase family is a family of evolutionarily related proteins.

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.

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

Subfamilies[edit]

References[edit]

^ Beeching JR (1989). "High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis". Protein Seq. Data Anal. 2 (6): 463–466. PMID 2696959.
^ Tanaka A, Atomi H, Ueda M, Hikida M, Hishida T, Teranishi Y (1990). "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization". J. Biochem. 107 (2): 262–266. doi:10.1093/oxfordjournals.jbchem.a123036. PMID 2361956.

This article incorporates text from the public domain Pfam and InterPro: IPR000918

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[PUB00005064-1] Beeching JR (1989). "High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis". Protein Seq. Data Anal. 2 (6): 463–466. PMID 2696959.

[PUB00002339-2] Tanaka A, Atomi H, Ueda M, Hikida M, Hishida T, Teranishi Y (1990). "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization". J. Biochem. 107 (2): 262–266. doi:10.1093/oxfordjournals.jbchem.a123036. PMID 2361956.

[1]

[2]