| 4-Chlorobenzoate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.33 | ||||||||
| CAS no. | 141583-20-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 4-chlorobenzoate—CoA ligase (EC 6.2.1.33) is an enzyme that catalyzes the chemical reaction
- 4-chlorobenzoate + CoA + ATP 4-chlorobenzoyl-CoA + AMP + diphosphate
The 3 substrates of this enzyme are 4-chlorobenzoate, CoA, and ATP, whereas its 3 products are 4-chlorobenzoyl-CoA, AMP, and diphosphate.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate degradation. It employs one cofactor, magnesium.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1T5D and 1T5H.
References
- Dunaway-Mariano D, Babbitt PC (1994). "On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway". Biodegradation. 5 (3–4): 259–76. doi:10.1007/BF00696464. PMID 7765837. S2CID 13250105.
- Loffler F, Muller R, Lingens F (1992). "Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. CBS3". Biol. Chem. Hoppe-Seyler. 373 (10): 1001–7. doi:10.1515/bchm3.1992.373.2.1001. PMID 1418673.
- Chang KH, Liang PH, Beck W, Scholten JD, Dunaway-Mariano D (1992). "Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3". Biochemistry. 31 (24): 5605–10. doi:10.1021/bi00139a025. PMID 1610806.
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