2.3.1.137: carnitine O-octanoyltransferase
This is an abbreviated version!
For detailed information about carnitine O-octanoyltransferase, go to the full flat file.
Word Map on EC 2.3.1.137
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2.3.1.137
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peroxisomal
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acyl-coas
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beta-oxidation
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malonyl-coa
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acylcarnitine
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palmitoyl-coa
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ketogenesis
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decanoyl-coa
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carnitine-dependent
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crats
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arrhythmogenesis
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2-bromopalmitate
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cpt-ii
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malonyl-coa-sensitive
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etomoxir
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palmitoylcarnitine
- 2.3.1.137
- peroxisomal
- acyl-coas
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beta-oxidation
- malonyl-coa
- acylcarnitine
- palmitoyl-coa
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ketogenesis
- decanoyl-coa
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carnitine-dependent
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crats
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arrhythmogenesis
- 2-bromopalmitate
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cpt-ii
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malonyl-coa-sensitive
- etomoxir
- palmitoylcarnitine
Reaction
Synonyms
carnitine acyltransferase, Carnitine medium-chain acyltransferase, carnitine octanoyltransferase, COT, CRAT, CrOT, easily solubilized mitochondrial carnitine palmitoyltransferase, medium-chain carnitine acyltransferase, medium-chain/long-chain carnitine acyltransferase, More, overt mitochondrial carnitine palmitoyltransferase, short-chain carnitine acyltransferase
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Reaction
Reaction on EC 2.3.1.137 - carnitine O-octanoyltransferase
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octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
acyl-binding hydrophobic pocket structure involving residues G553, C323, and Met335, the acyl-CoA substrate chain length specificity is determined by G553, Met335 is important for catalysis
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
acyl-CoA substrate specificity is determined by Gly553, active site structure and substrate positioning modeling
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octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
catalytic mechanism, active site structure, substrate recognition mechanism, amino acid residues 343, 564 and 553 determine the acyl-CoA substrate specificity, catalytic residue is His343
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