4-chlorobenzoate—CoA ligase
| 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
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1T5D and 1T5H.
References
[edit]- 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.
