CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1110 | SGNH hydrolase |
Domain Context
CATH Clusters
| Superfamily | SGNH hydrolase |
| Functional Family | Multifunctional acyl-CoA thioesterase I |
Enzyme Information
| 3.1.1.2 |
Arylesterase.
based on mapping to UniProt P0ADA1
A phenyl acetate + H(2)O = a phenol + acetate.
-!- Acts on many phenolic esters. -!- It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases. -!- The natural substrates of the paraoxonases are lactones, with (+-)-5- hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate.
|
| 3.4.21.- |
Serine endopeptidases.
based on mapping to UniProt P0ADA1
|
| 3.1.2.2 |
Palmitoyl-CoA hydrolase.
based on mapping to UniProt P0ADA1
Palmitoyl-CoA + H(2)O = CoA + palmitate.
-!- Also hydrolyzes CoA thioesters of other long-chain fatty acids.
|
| 3.1.1.5 |
Lysophospholipase.
based on mapping to UniProt P0ADA1
2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate.
|
| 3.1.2.14 |
Oleoyl-[acyl-carrier-protein] hydrolase.
based on mapping to UniProt P0ADA1
Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.
-!- Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.
|
UniProtKB Entries (1)
| P0ADA1 |
TESA_ECOLI
Escherichia coli K-12
Thioesterase 1/protease 1/lysophospholipase L1
|
PDB Structure
| PDB | 1U8U |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement
Biochemistry
|