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
ECTree
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Engineering
Engineering on EC 2.3.1.137 - carnitine O-octanoyltransferase
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R518N
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site-directed mutagenesis, mutant shows 1650fold increased Km for L-carnitine, only slightly affected Km for acyl-CoA and kcat compared to the wild-type enzyme
S552A
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site-directed mutagenesis, mutant shows 17fold increased Km for L-carnitine compared to the wild-type enzyme
S554X
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site-directed mutagenesis, mutant shows 10fold decreased kcat compared to the wild-type enzyme
C323M
site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, altered acyl-CoA substrate specificity compared to the wild-type enzyme, highly increased specificity for octanoyl-CoA
G553M
site-directed mutagenesis, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
M335A
site-directed mutagenesis, reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
M335V
site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
G553M
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site-directed mutagenesis, the mutant enzyme shows altered substrate specificity: highly reduced activity with medium- and long-chain acyl-CoAs and increased activity with acetyl-CoA and butanoyl-CoA compared to the wild-type enzyme
additional information
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the carnitine acetyl-transferase, specific for acetyl-CoA/short-chain acyl-CoAs, can be modified to an enzyme with elevated carnitine octanoyltransferase activity by mutation of Met564 to Gly, overview