Biology:Citrate (pro-3S)-lyase
| citrate (pro-3S)-lyase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.1.3.6 | ||||||||
| CAS number | 9012-83-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme citrate (pro-3S)-lyase (EC 4.1.3.6) catalyzes the chemical reaction
- citrate [math]\displaystyle{ \rightleftharpoons }[/math] acetate + oxaloacetate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is citrate oxaloacetate-lyase (forming acetate from the pro-S carboxymethyl group of citrate). Other names in common use include citrase, citratase, citritase, citridesmolase, citrate aldolase, citric aldolase, citrate lyase, citrate oxaloacetate-lyase, and citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetate]. This enzyme participates in citrate cycle and two-component system - general.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1U5H, 1U5V, 1Z6K, and 2HJ0.
References
- "Citridesmolase: its properties and mode of action". Biochim. Biophys. Acta 17 (2): 177–84. 1955. doi:10.1016/0006-3002(55)90348-6. PMID 13239657.
- "Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate". Eur. J. Biochem. 80 (2): 479–88. 1977. doi:10.1111/j.1432-1033.1977.tb11903.x. PMID 336371.
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