EC number:2.7.7.23

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.23
Description:UDP-N-acetylglucosamine diphosphorylase.
Alternative Name: UDP-N-acetylglucosamine pyrophosphorylase.
N-acetylglucosamine-1-phosphate uridyltransferase.
Prosite: PDOC00094;
PDB:
PDBScop
Cath: 3.90.550.10; 2.160.10.10; 3.40.1630.20;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.23
BRENDA Enzyme Link: BRENDA 2.7.7.23
KEGG Enzyme Link: KEGG2.7.7.23
BioCyc Enzyme Link: BioCyc 2.7.7.23
ExPASy Enzyme Link: ExPASy2.7.7.23
EC2PDB Enzyme Link: EC2PDB 2.7.7.23
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.23
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.23
IntEnz Enzyme Link: IntEnz 2.7.7.23
MEDLINE Enzyme Link: MEDLINE 2.7.7.23

EC number:2.7.7.23

MSA:

2.7.7.23;
Phylogenetic Tree:

2.7.7.23;
Uniprot:
M-CSA:
RHEA:13509 H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:7]-[*:8].[H+;H0:9]>>[*:8]-[OH;+0:7].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
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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
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y2001 Nov 1511707391
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.Olsen LR, Roderick SL2001 Feb 2011329257
A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc.Wang-Gillam A, Pastuszak I, Elbein AD1998 Oct 169765219
Identification and characterization of a strict and a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis.Yang T, Echols M, Martin A, Bar-Peled M2010 Sep 120557289
Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis.Mengin-Lecreulx D, van Heijenoort J1994 Sep8083170
Structure and function of GlmU from Mycobacterium tuberculosis.Zhang Z, Bulloch EM, Bunker RD, Baker EN, Squire CJ2009 Mar19237750
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.Parikh A, Verma SK, Khan S, Prakash B, Nandicoori VK2009 Feb 2019121323
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y1999 Aug 210428949