CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.129 | Thiol Ester Dehydrase; Chain A |
|
3.10.129.10 | Hotdog Thioesterase |
Domain Context
CATH Clusters
| Superfamily | Hotdog Thioesterase |
| Functional Family |
Enzyme Information
| 3.1.2.29 |
Fluoroacetyl-CoA thioesterase.
based on mapping to UniProt Q1EMV2
Fluoroacetyl-CoA + H(2)O = fluoroacetate + CoA.
-!- Fluoroacetate is extremely toxic. -!- It reacts with CoA to form fluoroacetyl-CoA, which substitutes for acetyl CoA and reacts with EC 2.3.3.1 to produce fluorocitrate, a metabolite of which binds very tightly to EC 4.2.1.3 and halts the TCA cycle. -!- This enzyme hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance on the organisms that produce it. -!- It has been described in the poisonous plant Dichapetalum cymosum and the bacterium Streptomyces cattleya, both of which are fluoroacetate producers.
|
UniProtKB Entries (1)
| Q1EMV2 |
FLK_STRCT
Streptomyces cattleya
Fluoroacetyl-CoA thioesterase
|
PDB Structure
| PDB | 3P2R |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity.
Biochemistry
|
