EC number:2.3.1.7

Enzyme

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EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.7
Description:Carnitine O-acetyltransferase.
Alternative Name: Carnitine acetylase.
Prosite: PDOC00402;
PDB:
PDBScop
Cath: 1.10.275.20; 1.20.1280.180; 1.20.5.3450; 3.30.559.10; 3.30.559.40; 3.30.559.70;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.7
BRENDA Enzyme Link: BRENDA 2.3.1.7
KEGG Enzyme Link: KEGG2.3.1.7
BioCyc Enzyme Link: BioCyc 2.3.1.7
ExPASy Enzyme Link: ExPASy2.3.1.7
EC2PDB Enzyme Link: EC2PDB 2.3.1.7
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.7
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.7
IntEnz Enzyme Link: IntEnz 2.3.1.7
MEDLINE Enzyme Link: MEDLINE 2.3.1.7

EC number:2.3.1.7

MSA:

2.3.1.7;
Phylogenetic Tree:

2.3.1.7;
Uniprot:
M-CSA:
RHEA:21136 (R)-carnitine + acetyl-CoA = CoA + O-acetyl-(R)-carnitine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and properties of carnitine acetyltransferase from rat liver.Miyazawa S, Ozasa H, Furuta S, Osumi T, Hashimoto T1983 Feb6404901
Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase.Govindasamy L, Kukar T, Lian W, Pedersen B, Gu Y, Agbandje-McKenna M, Jin S, McKenna R, Wu D2004 Jun15099582