EC number:2.3.1.157

Enzyme

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EC Tree
     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.157
Description:Glucosamine-1-phosphate N-acetyltransferase.
Cath: 3.40.50.620; 3.90.550.10; 2.160.10.10; 3.40.1630.20; 3.40.50.300;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.157
BRENDA Enzyme Link: BRENDA 2.3.1.157
KEGG Enzyme Link: KEGG2.3.1.157
BioCyc Enzyme Link: BioCyc 2.3.1.157
ExPASy Enzyme Link: ExPASy2.3.1.157
EC2PDB Enzyme Link: EC2PDB 2.3.1.157
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.157
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.157
IntEnz Enzyme Link: IntEnz 2.3.1.157
MEDLINE Enzyme Link: MEDLINE 2.3.1.157

EC number:2.3.1.157

MSA:

2.3.1.157;
Phylogenetic Tree:

2.3.1.157;
Uniprot:
M-CSA:
RHEA:13725 acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.Gehring AM, Lees WJ, Mindiola DJ, Walsh CT, Brown ED1996 Jan 168555230
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.Olsen LR, Vetting MW, Roderick SL2007 Jun17473010
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.Olsen LR, Roderick SL2001 Feb 2011329257