3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.6
BRENDA Enzyme Link: BRENDA 2.3.1.6
KEGG Enzyme Link: KEGG2.3.1.6
BioCyc Enzyme Link: BioCyc 2.3.1.6
ExPASy Enzyme Link: ExPASy2.3.1.6
EC2PDB Enzyme Link: EC2PDB 2.3.1.6
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.6
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.6
IntEnz Enzyme Link: IntEnz 2.3.1.6
MEDLINE Enzyme Link: MEDLINE 2.3.1.6
MSA:

2.3.1.6;

Phylogenetic Tree:

2.3.1.6;

Uniprot:
M-CSA:
RHEA:18821 acetyl-CoA + choline = acetylcholine + CoA
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
The amino terminus of the putative Drosophila choline acetyltransferase precursor is cleaved to yield the 67 kDa enzyme.Slemmon JR, Campbell GA, Selski DJ, Bramson HN1991 Feb1851526
Substrate binding and catalytic mechanism of human choline acetyltransferase.Kim AR, Rylett RJ, Shilton BH2006 Dec 1217144655
Structural insights and functional implications of choline acetyltransferase.Govindasamy L, Pedersen B, Lian W, Kukar T, Gu Y, Jin S, Agbandje-McKenna M, Wu D, McKenna R2004 Nov15477102