2.3.1.7: carnitine O-acetyltransferase
This is an abbreviated version!
For detailed information about carnitine O-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.7
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2.3.1.7
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peroxisomal
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palmitoyltransferase
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beta-oxidation
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acyl-coas
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l-carnitine
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acyltransferases
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clofibrate
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palmitoyl-coa
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acylcarnitine
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proliferators
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hypolipidemic
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octanoyltransferase
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cyanide-insensitive
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propionylation
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cardos
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acetyl-l-carnitine
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carbazole
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carnitine-dependent
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cronbach
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alloy
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1,9a-dioxygenase
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coash
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peroxisome-associated
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palmitoylcarnitine
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nafenopin
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bezafibrate
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ciprofibrate
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food industry
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analysis
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medicine
- 2.3.1.7
- peroxisomal
- palmitoyltransferase
-
beta-oxidation
- acyl-coas
- l-carnitine
- acyltransferases
- clofibrate
- palmitoyl-coa
- acylcarnitine
- proliferators
-
hypolipidemic
-
octanoyltransferase
-
cyanide-insensitive
-
propionylation
- cardos
- acetyl-l-carnitine
- carbazole
-
carnitine-dependent
-
cronbach
-
alloy
-
1,9a-dioxygenase
- coash
-
peroxisome-associated
- palmitoylcarnitine
-
nafenopin
- bezafibrate
- ciprofibrate
- food industry
- analysis
- medicine
Reaction
Synonyms
acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine transferase, acuJ, CarAc, CARAT, carnitine acetyl coenzyme A transferase, carnitine acetyl transferase, carnitine acetylase, carnitine acetyltransferase, carnitine acetyltransferase CAT2, carnitine acetyltransferase Cat2p, carnitine acetyltransferase Yat1p, carnitine acetyltransferase Yat2p, carnitine-acetyl-CoA transferase, CAT, CAT2, CATC, CRAT, CT-CAT, CTN1, CTN2, CTN3, H-CAT, P-CAT, S-CAT1, S-CAT2, Yat1
ECTree
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Crystallization
Crystallization on EC 2.3.1.7 - carnitine O-acetyltransferase
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crystals grown by hanging-drop vapor-diffusion belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a: 137.65 A, b: 84.76 A, c: 57.65 A
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crystallized as pure enzyme and in complex with its substrates carnitine and CoA
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M564G and F565A mutant enzymes crystallized by sitting-drop vapor diffusion method
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sitting drop vapor diffusion method, high resolution crystal structure of wild-type murine carnitine acetyltransferase in a ternary complex with its substrates acetyl-CoA and carnitine, and the structure of the S554A/M564G double mutant in a ternary complex with the substrates CoA and hexanoylcarnitine
sitting drop vapor diffusion method, space group C2, cell dimensions for the free enzyme crystal a: 158.9 A, b: 89.6 A, c: 119.4 A, beta: 127.5°