4-hydroxybenzoyl-CoA thioesterase
In enzymology, a 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) is an enzyme that catalyzes the chemical reaction
- 4-hydroxybenzoyl-CoA + H2O 4-hydroxybenzoate + CoA
4-hydroxybenzoyl-CoA thioesterase | |||||||||
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Identifiers | |||||||||
EC number | 3.1.2.23 | ||||||||
CAS number | 141583-19-9 | ||||||||
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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Thus, the two substrates of this enzyme are 4-hydroxybenzoyl-CoA and H2O, whereas its two products are 4-hydroxybenzoate and CoA.
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is 4-hydroxybenzoyl-CoA hydrolase. This enzyme participates in 2,4-dichlorobenzoate degradation.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1HN1, 1LO7, 1LO8, 1LO9, 1Q4S, 1Q4T, and 1Q4U.
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References
- 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.
- 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.
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