Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.83
Description:UDP-N-acetylgalactosamine diphosphorylase.
Cath: 3.90.550.10; 2.160.10.10; 3.40.1630.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.83
BRENDA Enzyme Link: BRENDA 2.7.7.83
KEGG Enzyme Link: KEGG2.7.7.83
BioCyc Enzyme Link: BioCyc 2.7.7.83
ExPASy Enzyme Link: ExPASy2.7.7.83
EC2PDB Enzyme Link: EC2PDB 2.7.7.83
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.83
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.83
IntEnz Enzyme Link: IntEnz 2.7.7.83
MEDLINE Enzyme Link: MEDLINE 2.7.7.83
MSA:

2.7.7.83;

Phylogenetic Tree:

2.7.7.83;

Uniprot:
M-CSA:
RHEA:34363 H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-galactosamine
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
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
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