Any feedback?
Literature summary extracted from
- Molecular recognition of fluorine impacts substrate selectivity in the fluoroacetyl-CoA thioesterase FlK (2014), Biochemistry, 53, 2053-2063.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.2.29 | Streptomyces cattleya | Q1EMV2 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.2.29 | additional information | chemical, kinetic, and structural mechanism for the selectivity for fluoroacetyl-CoA. Following substrate binding, fluoroacetyl-CoA reacts with Glu50 to acylate this side chain. After enzyme acylation, a proton is abstracted by His 76 to generate an enolate that can break down through a proposed ketene intermediate. The pro-R proton of fluoroacetyl-CoA is specifically abstracted. The selectivity for the fluoroacetyl-CoA substrate appears to rely not only on the enhanced polarization provided by the electronegative fluorine substitution but also on molecular recognition of fluorine in both formation and breakdown of the acyl-enzyme intermediate to control active site reactivity | Streptomyces cattleya | ? | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.2.29 | FlK | - |
Streptomyces cattleya |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
