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Literature summary for 3.1.2.27 extracted from
- Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism (2002), J. Biol. Chem., 277, 1128-1138.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | fasting induces the enzyme | Mus musculus | |
| PPARII | peroxisomal proliferator activated receptor-II activates the enzyme, regulatory function, fasting-mediated induction in vivo, dependent on the peroxisomal proliferator WY-14,643 | Mus musculus |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PTE-2, DNA and amino acid sequence determination and analysis, location on chromosome 20q12-q13, expression in Escherichia coli, expression as GFP-fusion protein in human skin fibroblasts showing targeting to the peroxisomes | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 4-chloromercuribenzoate | 50% inhibition at 0.001 mM | Mus musculus | |
| acyl-CoA | enzyme is substrate-inhibited at 0.005-0.01 mM of acyl-CoAs with chain length longer than C10 | Mus musculus | |
| CoA | product inhibition with regulatory function, 50% inhibition at 0.01-0.015 mM | Mus musculus | |
| DTNB | 50% inhibition at 0.15 mM | Mus musculus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Mus musculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| peroxisome | - |
Mus musculus | 5777 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 35886 | - |
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE | Mus musculus |
| 36000 | - |
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE | Mus musculus |
| 70000 | - |
recombinant enzyme, gel filtration | Mus musculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-trans-decenoyl-CoA + H2O | Mus musculus | substrate is a beta-oxidation intermediate, low activity | 2-trans-decenoate + CoA | - |
? | |
| 3-hydroxypalmitoyl-CoA + H2O | Mus musculus | substrate is a beta-oxidation intermediate, low activity | 3-hydroxypalmitate + CoA | - |
? | |
| chenodeoxycholoyl-CoA + H2O | Mus musculus | - |
chenodeoxycholate + CoA | - |
? | |
| choloyl-CoA + H2O | Mus musculus | - |
cholate + CoA | - |
? | |
| hydroxymethylglutaryl-CoA + H2O | Mus musculus | - |
hydroxymethylglutarate + CoA | - |
? | |
| additional information | Mus musculus | the enzyme functions as a major regulator of peroxisomal lipid metabolism, the enzyme competes with the bile acid-CoA:amino acid N-acyltranferase for bile acid-CoAs as substrates | ? | - |
? | |
| trihydroxycoprostanoyl-CoA + H2O | Mus musculus | - |
trihydroxycoprostanate + CoA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | P58137 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| choloyl-CoA + H2O = cholate + CoA | the catalytic triad is formed by Asp233, Ser255, and Gln305 | Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | lower enzyme content | Mus musculus | - |
| kidney | high enzyme content | Mus musculus | - |
| liver | - |
Mus musculus | - |
| muscle | lower enzyme content | Mus musculus | - |
| testis | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-trans-decenoyl-CoA + H2O | substrate is a beta-oxidation intermediate, low activity | Mus musculus | 2-trans-decenoate + CoA | - |
? | |
| 3-hydroxypalmitoyl-CoA + H2O | substrate is a beta-oxidation intermediate, low activity | Mus musculus | 3-hydroxypalmitate + CoA | - |
? | |
| chenodeoxycholoyl-CoA + H2O | - |
Mus musculus | chenodeoxycholate + CoA | - |
? | |
| chenodeoxycholoyl-CoA + H2O | best substrate | Mus musculus | chenodeoxycholate + CoA | - |
? | |
| choloyl-CoA + H2O | - |
Mus musculus | cholate + CoA | - |
? | |
| choloyl-CoA + H2O | best substrate | Mus musculus | cholate + CoA | - |
? | |
| hydroxymethylglutaryl-CoA + H2O | - |
Mus musculus | hydroxymethylglutarate + CoA | - |
? | |
| additional information | the enzyme functions as a major regulator of peroxisomal lipid metabolism, the enzyme competes with the bile acid-CoA:amino acid N-acyltranferase for bile acid-CoAs as substrates | Mus musculus | ? | - |
? | |
| additional information | the enzyme shows broad specificity for substrates and (branched) acyl-CoA chain lengths | Mus musculus | ? | - |
? | |
| trihydroxycoprostanoyl-CoA + H2O | - |
Mus musculus | trihydroxycoprostanate + CoA | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acyl-CoA thioesterase | - |
Mus musculus |
| peroxisomal acyl-coA thioesterase | - |
Mus musculus |
| PTE-2 | - |
Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Mus musculus |
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