Enzyme

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     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.136
Description:Polysialic-acid O-acetyltransferase.
Cath: 2.160.10.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.136
BRENDA Enzyme Link: BRENDA 2.3.1.136
KEGG Enzyme Link: KEGG2.3.1.136
BioCyc Enzyme Link: BioCyc 2.3.1.136
ExPASy Enzyme Link: ExPASy2.3.1.136
EC2PDB Enzyme Link: EC2PDB 2.3.1.136
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.136
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.136
IntEnz Enzyme Link: IntEnz 2.3.1.136
MEDLINE Enzyme Link: MEDLINE 2.3.1.136
MSA:

2.3.1.136;

Phylogenetic Tree:

2.3.1.136;

Uniprot:
M-CSA:
RHEA:11608 [(2->8)-N-acetyl-alpha-D-neuraminosyl](n) + n acetyl-CoA = [(2->8)-N,O(9)-diacetyl-alpha-D-neuraminosyl](n) + n CoA
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S;H0;+0:4]-[C;H0;+0:5](-[CH3;+0:6])=[O;H0;+0:7].[*:8]-[S;H0;+0:9]-[C;H0;+0:10](-[CH3;+0:11])=[O;H0;+0:12].[*:13]-[S;H0;+0:14]-[C;H0;+0:15](-[CH3;+0:16])=[O;H0;+0:17].[*:18]-[S;H0;+0:19]-[C;H0;+0:20](-[CH3;+0:21])=[O;H0;+0:22].[*:23]=[C;H0;+0:24](-[*:25])-[S;H0;+0:26]-[*:27]>>[*:27]-[SH;+0:26].[*:3]-[SH;+0:4].[*:8]-[SH;+0:9].[*:13]-[SH;+0:14].[*:18]-[SH;+0:19].[*:23]=[C;H0;+0:24](-[*:25])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO.Schulz EC, Bergfeld AK, Ficner R, Mühlenhoff M2011 Mar 121390252
Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1.Bergfeld AK, Claus H, Vogel U, Mühlenhoff M2007 Jul 2717519228
Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus.Deszo EL, Steenbergen SM, Freedberg DI, Vimr ER2005 Apr 1215809431

RHEA:11604 [(2->8)-N-acetyl-alpha-D-neuraminosyl](n) + n acetyl-CoA = [(2->8)-O(7),N-diacetyl-alpha-D-neuraminosyl](n) + n CoA
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S;H0;+0:4]-[C;H0;+0:5](-[CH3;+0:6])=[O;H0;+0:7].[*:8]-[S;H0;+0:9]-[C;H0;+0:10](-[CH3;+0:11])=[O;H0;+0:12].[*:13]-[S;H0;+0:14]-[C;H0;+0:15](-[CH3;+0:16])=[O;H0;+0:17].[*:18]-[S;H0;+0:19]-[C;H0;+0:20](-[CH3;+0:21])=[O;H0;+0:22].[*:23]=[C;H0;+0:24](-[*:25])-[S;H0;+0:26]-[*:27]>>[*:27]-[SH;+0:26].[*:3]-[SH;+0:4].[*:8]-[SH;+0:9].[*:13]-[SH;+0:14].[*:18]-[SH;+0:19].[*:23]=[C;H0;+0:24](-[*:25])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO.Schulz EC, Bergfeld AK, Ficner R, Mühlenhoff M2011 Mar 121390252
Biochemical characterization of the polysialic acid-specific O-acetyltransferase NeuO of Escherichia coli K1.Bergfeld AK, Claus H, Vogel U, Mühlenhoff M2007 Jul 2717519228
Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus.Deszo EL, Steenbergen SM, Freedberg DI, Vimr ER2005 Apr 1215809431