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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: acyl-CoA thioesterase 2 (mitochondrial)

Gene: ACOT2 Accession Number: HS04318 (MetaCyc)

Synonyms: ZAP128, PTE2, peroxisomal long-chain acyl-coA thioesterase

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 mitochondrial enzyme displays high levels of activity on medium- and long chain acyl CoAs. The ACOT2 gene was cloned and expressed in Escherichia coli, and the protein was purified [Hunt06].

Kinetic parameters (Km/Vmax) [Hunt06]:

decanoyl-CoA (C10): 40.3 然/212 nmol/min/mg

lauroyl-CoA (C12): 8.9 然/681 nmol/min/mg

myristoyl-CoA (C14): 1.6 然/766 nmol/min/mg

palmitoyl-CoA (C16): 2.0 然/656 nmol/min/mg

stearoyl-CoA (C18): 2.8 然/488 nmol/min/mg

arachidoyl-CoA (C20): 4.8 然/408 nmol/min/mg

palmitoleyl-CoA (C16:1): 4.5 然/661 nmol/min/mg

oleoyl-CoA (C18:1-cis): 6.1 然/304 nmol/min/mg

oleoyl-CoA (trans) (C18:1-trans): 4.3 然/418 nmol/min/mg

Citations: [Jones00, Sherrington95]

Gene Citations: [Sherrington95]

Locations: mitochondrial lumen, peroxisome

Map Position: [67,799,645 -> 67,837,879]

Molecular Weight of Polypeptide: 53.238 kD (from nucleotide sequence), 46.0 kD (experimental) [Hunt06 ]

Unification Links: ArrayExpress:P49753 , Mint:MINT-5004303 , PhosphoSite:P49753 , PhylomeDB:P49753 , Pride:P49753 , Protein Model Portal:P49753 , SMR:P49753 , String:9606.ENSP00000238651 , UniProt:P49753

Relationship Links: Entrez-Nucleotide:PART-OF:L40401 , InterPro:IN-FAMILY:IPR006862 , InterPro:IN-FAMILY:IPR014940 , InterPro:IN-FAMILY:IPR016662 , PDB:Structure:3HLK , Pfam:IN-FAMILY:PF04775 , Pfam:IN-FAMILY:PF08840

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006637 - acyl-CoA metabolic process
Molecular Function: GO:0016290 - palmitoyl-CoA hydrolase activity
GO:0016787 - hydrolase activity
GO:0047617 - acyl-CoA hydrolase activity
GO:0052689 - carboxylic ester hydrolase activity
Cellular Component: GO:0005759 - mitochondrial matrix
GO:0005777 - peroxisome

Credits:
Created 31-Jul-2008 by Caspi R , SRI International


Enzymatic reaction of: palmitoyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)
palmitoyl-CoA
2.0


Enzymatic reaction of: stearoyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)
stearoyl-CoA
2.8


Enzymatic reaction of: myristoyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)
myristoyl-CoA
1.6


Enzymatic reaction of: lauroyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)
lauroyl-CoA
8.9


Enzymatic reaction of: decanoyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)
decanoyl-CoA
40.3


Enzymatic reaction of: arachidoyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)
arachidoyl-CoA
4.8


Enzymatic reaction of: oleoyl-CoA hydrolase (acyl-CoA thioesterase 2 (mitochondrial))

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)

Exons/Introns:


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

Jones00: Jones JM, Gould SJ (2000). "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase." Biochem Biophys Res Commun 275(1);233-40. PMID: 10944470

Sherrington95: Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K (1995). "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease." Nature 375(6534);754-60. PMID: 7596406


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, biocyc12.