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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: acyl-coA hydrolase (long chain)

Gene: CESdD1 Accession Number: G-9360 (MetaCyc)

Synonyms: ACH D1

Species: Canis lupus familiaris

Subunit composition of acyl-coA hydrolase (long chain) = [CESdD1]3
         acyl-coA hydrolase (long chain) subunit = CESdD1

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

Gene-Reaction Schematic: ?

Instance reactions of [an acyl-CoA + H2O → a carboxylate + coenzyme A + H+] (3.1.2.20):
i1: propanoyl-CoA + H2O → propanoate + coenzyme A + H+ (3.1.2.18)

i2: decanoyl-CoA + H2O → decanoate + coenzyme A + H+ (3.1.2.2)

i3: arachidoyl-CoA + H2O → arachidate + coenzyme A + H+ (3.1.2.2)

i4: palmitoyl-CoA + H2O → palmitate + coenzyme A + H+ (3.1.2.2)

i5: stearoyl-CoA + H2O → stearate + coenzyme A + H+ (3.1.2.2)

i6: myristoyl-CoA + H2O → myristate + coenzyme A + H+ (3.1.2.2)

i7: lauroyl-CoA + H2O → laurate + coenzyme A + H+ (3.1.2.2)

GO Terms:

Cellular Component: GO:0005789 - endoplasmic reticulum membrane


Enzymatic reaction of: acyl-coA hydrolase (long chain)

EC Number: 3.1.2.20

an acyl-CoA + H2O <=> a carboxylate + coenzyme A + H+

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.

Summary:
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].


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 28, 2014, biocyc12.