EC - UDP-N-acetylglucosamine diphosphorylase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
UDP-N-acetylglucosamine diphosphorylase
Other names:
acetylglucosamine 1-phosphate uridylyltransferase
GlmU uridylyltransferase
UDP-N-acetylglucosamine pyrophosphorylase
UDP-GlcNAc pyrophosphorylase
UDP-acetylglucosamine pyrophosphorylase
UTP:2-acetamido-2-deoxy-α-D-glucose-1-phosphate uridylyltransferase
uridine diphosphate-N-acetylglucosamine pyrophosphorylase
uridine diphosphoacetylglucosamine phosphorylase
uridine diphosphoacetylglucosamine pyrophosphorylase
N-acetylglucosamine-1-phosphate uridyltransferase
Systematic name:
UTP:N-acetyl-α-D-glucosamine-1-phosphate uridylyltransferase



Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-α-D-galactosamine 1-phosphate (cf. EC, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00094
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003977
CAS Registry Number: 9023-06-7
UniProtKB/Swiss-Prot: (618) [show] [UniProt]


  1. Pattabiramin, T.N. and Bachhawat, B.K.
    Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain.
    Biochim. Biophys. Acta 50 : 129-134 (1961). [PMID: 13733356]
  2. Strominger, J.L. and Smith, M.S.
    Uridine diphosphoacetylglucosamine pyrophosphorylase.
    J. Biol. Chem. 234 : 1822-1827 (1959). [PMID: 13672971]
  3. Mengin-Lecreulx, D., van Heijenoort, J.
    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.
    J. Bacteriol. 176 : 5788-5795 (1994). [PMID: 8083170]
  4. Gehring, A. M., Lees, W. J., Mindiola, D. J., Walsh, C. T., Brown, E. D.
    Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
    Biochemistry 35 : 579-585 (1996). [PMID: 8555230]
  5. Wang-Gillam, A., Pastuszak, I., Elbein, A. D.
    A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc.
    J. Biol. Chem. 273 : 27055-27057 (1998). [PMID: 9765219]
  6. Olsen, L. R., Roderick, S. L.
    Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
    Biochemistry 40 : 1913-1921 (2001). [PMID: 11329257]
  7. Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F., Bourne, Y.
    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.
    EMBO J. 20 : 6191-6202 (2001). [PMID: 11707391]

[EC created 1965, modified 2012]