Enzyme

Download
EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.12
Description:Dihydrolipoyllysine-residue acetyltransferase.
Alternative Name: Transacetylase X.
Thioltransacetylase A.
Lipoylacetyltransferase.
Lipoic transacetylase.
Lipoic acid acetyltransferase.
Lipoic acetyltransferase.
Lipoate transacetylase.
Lipoate acetyltransferase.
Dihydrolipoyl acetyltransferase.
Dihydrolipoic transacetylase.
Dihydrolipoate acetyltransferase.
Dihydrolipoamide S-acetyltransferase.
Acetyl-CoA:dihydrolipoamide S-acetyltransferase.
Cath: 1.10.10.10; 1.20.120.530; 3.30.390.30; 3.30.559.10; 4.10.320.10; 3.40.50.920; 3.40.50.970; 3.50.50.60; 2.30.36.80; 2.40.50.100;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.12
BRENDA Enzyme Link: BRENDA 2.3.1.12
KEGG Enzyme Link: KEGG2.3.1.12
BioCyc Enzyme Link: BioCyc 2.3.1.12
ExPASy Enzyme Link: ExPASy2.3.1.12
EC2PDB Enzyme Link: EC2PDB 2.3.1.12
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.12
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.12
IntEnz Enzyme Link: IntEnz 2.3.1.12
MEDLINE Enzyme Link: MEDLINE 2.3.1.12
MSA:

2.3.1.12;

Phylogenetic Tree:

2.3.1.12;

Uniprot:
M-CSA:
RHEA:33151 (R)-dihydrolipoamide + acetyl-CoA = (R)-S(6)-acetyldihydrolipoamide + CoA
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

RHEA:17017 (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Enzymatic thioltransacetylation.BRADY RO, STADTMAN ER1954 Dec13221570