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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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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 Sat Dec 20, 2014, BIOCYC13A.