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MetaCyc Enzyme: acyl-CoA thioesterase 1, cytosolic

Gene: ACOT1 Accession Number: G-10780 (MetaCyc)

Synonyms: CTE1

Species: Homo sapiens

Summary:
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and free CoA. There are several such enzymes in humans, with localizations in cytosol (ACOT1), mitochondria (ACOT2), and peroxisomes (ACOT4) [Hunt06]. The ACOT1 gene was cloned and expressed in Escherichia coli, and the protein was purified [Hunt06].

Kinetic characterization of recombinant human ACOT1 and ACOT2 showed similar substrate specificities, with both enzymes being mainly active on long chain saturated acyl-CoAs of 12 to 20 carbon atoms and long chain unsaturated acyl-CoAs such as C16:1-CoA and C18:1-CoA [Hunt06]. The cytosolic enzyme displays high levels of activity on medium- and long chain acyl CoAs.

Kinetic parameters (Km/Vmax) [Hunt06]:

decanoyl-CoA (C10): 35.8 然/224 nmol/min/mg

lauroyl-CoA (C12): 3.6 然/700 nmol/min/mg

myristoyl-CoA (C14): 2.8 然/912 nmol/min/mg

palmitoyl-CoA (C16): 3.6 然/691 nmol/min/mg

stearoyl-CoA (C18): 2.4 然/597 nmol/min/mg

arachidoyl-CoA (C20): 2.0 然/520 nmol/min/mg

palmitoleyl-CoA (C16:1): 2.4 然/577 nmol/min/mg

oleoyl-CoA (C18:1-cis): 4.1 然/258 nmol/min/mg

oleoyl-CoA (trans) (C18:1-trans): 2.1 然/309 nmol/min/mg

Locations: cytosol

Molecular Weight of Polypeptide: 46.277 kD (from nucleotide sequence), 46.0 kD (experimental) [Hunt06 ]

Unification Links: ArrayExpress:Q86TX2 , Entrez-gene:641371 , PhosphoSite:Q86TX2 , PhylomeDB:Q86TX2 , Pride:Q86TX2 , Protein Model Portal:Q86TX2 , SMR:Q86TX2 , String:9606.ENSP00000311224 , UniProt:Q86TX2

Relationship Links: InterPro:IN-FAMILY:IPR006862 , InterPro:IN-FAMILY:IPR014940 , InterPro:IN-FAMILY:IPR016662 , Pfam:IN-FAMILY:PF04775 , Pfam:IN-FAMILY:PF08840

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol

Credits:
Created 30-Jul-2008 by Caspi R , SRI International


Enzymatic reaction of: eicosapentaenoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

(5Z,8Z,11Z,14Z,17Z)-icosapentaenoyl-CoA + H2O <=> (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate + 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.

In Pathways: eicosapentaenoate biosynthesis II (metazoa)


Enzymatic reaction of: oleoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.-

oleoyl-CoA + H2O <=> oleate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: oleate biosynthesis II (animals and fungi)


Enzymatic reaction of: stearoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

stearoyl-CoA + H2O <=> stearate + 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.

In Pathways: stearate biosynthesis I (animals)

Kinetic Parameters:

Substrate
Km (μM)
Citations
stearoyl-CoA
2.4
[Hunt06]


Enzymatic reaction of: decanoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

decanoyl-CoA + H2O <=> decanoate + 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.

Kinetic Parameters:

Substrate
Km (μM)
Citations
decanoyl-CoA
35.8
[Hunt06]


Enzymatic reaction of: arachidoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

arachidoyl-CoA + H2O <=> arachidate + 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.

Kinetic Parameters:

Substrate
Km (μM)
Citations
arachidoyl-CoA
2.0
[Hunt06]


Enzymatic reaction of: myristoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

myristoyl-CoA + H2O <=> myristate + 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.

Kinetic Parameters:

Substrate
Km (μM)
Citations
myristoyl-CoA
2.8
[Hunt06]


Enzymatic reaction of: lauroyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

lauroyl-CoA + H2O <=> laurate + 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.

Kinetic Parameters:

Substrate
Km (μM)
Citations
lauroyl-CoA
3.6
[Hunt06]


Enzymatic reaction of: palmitoyl-CoA hydrolase (acyl-CoA thioesterase 1, cytosolic)

EC Number: 3.1.2.2

palmitoyl-CoA + H2O <=> palmitate + 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.

In Pathways: palmitate biosynthesis I (animals and fungi)

Kinetic Parameters:

Substrate
Km (μM)
Citations
palmitoyl-CoA
3.6
[Hunt06]


References

Hunt06: Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE (2006). "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs." FASEB J 20(11);1855-64. PMID: 16940157


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 Tue Nov 25, 2014, BIOCYC13B.