|Gene:||CESdD1||Accession Number: G-9360 (MetaCyc)|
Synonyms: ACH D1
Species: Canis lupus familiaris
Locations: endoplasmic reticulum membrane
Molecular Weight of Polypeptide: 60 kD (experimental) [Hosokawa01 ]
Molecular Weight of Multimer: 174 kD (experimental) [Hosokawa01]
Relationship Links: Entrez-Nucleotide:PART-OF:AB023629
Instance reactions of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (188.8.131.52):
|Cellular Component:||GO:0005789 - endoplasmic reticulum membrane|
Enzymatic reaction of: acyl-coA hydrolase (long chain)
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
Acyl-coA hydrolase (long chain) has been cloned and purified from dog liver microsomes, and shown to be a member of the carboxyesterase (CES) family. The enzyme is a homotrimer, and is specific for long chain molecules. The highest activity was that toward C14 acyl-chain-length acyl-CoA, followed by that toward C16 acyl-CoA. there was no activity towards acetyl-coA. The hydrolytic activities toward saturated and unsaturated acyl-CoAs were similar for C18 acyl-CoA esters, stearoyl-, and oleoyl-CoAs. The purified enzyme also showed hydrolytic activities toward certain prodrugs with ester bonds. Behavior of the enzyme during puirification suggests that it is a glycoprotein bearing a high-mannose-type sugar moiety [Hosokawa01].
Hosokawa01: Hosokawa M, Suzuki K, Takahashi D, Mori M, Satoh T, Chiba K (2001). "Purification, molecular cloning, and functional expression of dog liver microsomal acyl-CoA hydrolase: a member of the carboxylesterase multigene family." Arch Biochem Biophys 389(2);245-53. PMID: 11339814
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493