CATH Classification

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 5TIF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids.
Grisewood, M.J., Hernandez Lozada, N.J., Thoden, J.B., Gifford, N.P., Mendez-Perez, D., Schoenberger, H.A., Allan, M.F., Floy, M.E., Lai, R.Y., Holden, H.M., Pfleger, B.F., Maranas, C.D.
ACS Catal