PROSITE documentation PDOC010314-hydroxybenzoyl-CoA thioesterase family active site
4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) is an enzyme from Pseudomonas CBS-3, a soil-dwelling microbe that survives on 4-chlorobenzoate as its sole carbon source. This enzyme [1] catalyzes the last of the three steps in the pathway from 4-chlorobenzoate to hydroxybenzoate, the cleavage of the thioester bond of 4-hydroxybenzoyl-CoA to form hydroxybenzoate.
4-hydroxybenzoyl-CoA thioesterase is a protein of 141 amino-acid residues that assemble as an homotetramer. An aspartate in the N-terminal domain is thought to participate in the catalytic mechanism.
This enzyme is evolutionary related to a number of uncharacterized proteins:
- Escherichia coli hypothetical protein ybgC.
- Aquifex aeolicus hypothetical protein AQ_1494.
- Haemophilus influenzae hypothetical protein HI0386.
- Helicobacter pylori hypothetical protein HP0496.
- Synechocystis strain PCC 6803 hypothetical protein slr0204.
- Synechocystis strain PCC 6803 hypothetical protein sll0410.
We developed a signature pattern based on the region surrounding the potential active site residue.
Last update:July 1999 / First entry.
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| 1 | Authors | Benning M.M. Wesenberg G. Liu R. Taylor K.L. Dunaway-Mariano D. Holden H.M. |
| Title | The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3. | |
| Source | J. Biol. Chem. 273:33572-33579(1998). | |
| PubMed ID | 9837940 |
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