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.

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

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.7 carnitine O-acetyltransferase

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Results	in table
6	Activating Compound
126	AA Sequence
12	Application
1	CAS Registry Number
19	Cloned(Commentary)
11	Crystallization (Commentary)
173	Disease/ Diagnostics
3	Expression
10	General Information
6	General Stability
3	IC50 Value
116	Inhibitors
37	Ki Value [mM]
188	KM Value [mM]
183	Localization
73	Molecular Weight [Da]
480	Natural Substrates/ Products (Substrates)
563	Organism
11	PDB ID
16	pH Optimum
6	pH Range
2	pH Stability
1	Posttranslational Modification
23	Protein Variants
57	Purification (Commentary)
5	Reaction
1	Reaction Type
156	Reference
233	Source Tissue
30	Specific Activity [micromol/min/mg]
12	Storage Stability
952	Substrates and Products (Substrate)
46	Subunits
97	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Range [°C]
3	Temperature Stability [°C]
24	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.7 - carnitine O-acetyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Columba sp.

-

487397, 487403, 487404, 487414

crystallized in the presence of L-carnitine by vapor diffusion method

Homo sapiens

P43155

659815

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

Homo sapiens

-

487431

peroxisomal enzyme

Homo sapiens

-

659194

crystallized as pure enzyme and in complex with its substrates carnitine and CoA

Mus musculus

-

657546

M564G and F565A mutant enzymes crystallized by sitting-drop vapor diffusion method

Mus musculus

-

659365

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

Mus musculus

P47934

674651

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°

Mus musculus

P47934

487433