Isocitrate lyase

Isocitrate Lyase
Homotetrameric structure of Isocitrate lyase from E. coli. Based on PDB 1IGW.[1]
Identifiers
EC no.4.1.3.1
CAS no.9045-78-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Isocitrate lyase family
Identifiers
SymbolICL
PfamPF00463
InterProIPR000918
PROSITEPDOC00145
SCOP21f8m / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Isocitrate lyase (EC 4.1.3.1), or ICL, is an enzyme in the glyoxylate cycle that catalyzes the cleavage of isocitrate to succinate and glyoxylate.[2][3] Together with malate synthase, it bypasses the two decarboxylation steps of the tricarboxylic acid cycle (TCA cycle) and is used by bacteria, fungi, and plants.[4]

The systematic name of this enzyme class is isocitrate glyoxylate-lyase (succinate-forming). Other names in common use include isocitrase, isocitritase, isocitratase, threo-Ds-isocitrate glyoxylate-lyase, and isocitrate glyoxylate-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism.

  1. ^ Britton KL, Abeysinghe IS, Baker PJ, Barynin V, Diehl P, Langridge SJ, et al. (September 2001). "The structure and domain organization of Escherichia coli isocitrate lyase". Acta Crystallographica. Section D, Biological Crystallography. 57 (Pt 9): 1209–18. doi:10.1107/S0907444901008642. PMID 11526312.
  2. ^ Beeching JR (December 1989). "High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis". Protein Sequences & Data Analysis. 2 (6): 463–6. PMID 2696959.
  3. ^ Atomi H, Ueda M, Hikida M, Hishida T, Teranishi Y, Tanaka A (February 1990). "Peroxisomal isocitrate lyase of the n-alkane-assimilating yeast Candida tropicalis: gene analysis and characterization". Journal of Biochemistry. 107 (2): 262–6. doi:10.1093/oxfordjournals.jbchem.a123036. PMID 2361956.
  4. ^ Dunn MF, Ramírez-Trujillo JA, Hernández-Lucas I (October 2009). "Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis". Microbiology. 155 (Pt 10): 3166–75. doi:10.1099/mic.0.030858-0. PMID 19684068.