UDP-N-acetylglucosamine diphosphorylase

UDP-N-acetylglucosamine diphosphorylase
N-acetyl glucosamine 1-phosphate uridyltransferase homotrimer, Mycobacterium tuberculosis
Identifiers
EC no.2.7.7.23
CAS no.9023-06-7
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) is an enzyme that catalyzes the reversible chemical reaction

2D representation of the chemical structure of uridine triphosphate .
uridine triphosphate
+
 
2D representation of the chemical structure of Q27101910.
(1)
 
 
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
PPi
 
2D representation of the chemical structure of uridine diphosphate N-acetylglucosamine.
uridine diphosphate N-acetylglucosamine

The enzyme first characterised from sheep brain combines uridine triphosphate and N-acetyl-α-D-glucosamine 1-phosphate (1) to give uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), with pyrophosphate (PPi) as a byproduct. Initially, the enzyme was found to be catalysing the breakdown of UDP-GlcNAc but subsequent studies of the enzyme from Escherichia coli showed it to be involved in the biosynthesis of that compound.

The crystal structure of two human isoforms of the enzyme have been determined.

Nomenclature

This enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase. Other names in common use include UDP-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine pyrophosphorylase, UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate, uridylyltransferase, UDP-GlcNAc pyrophosphorylase, GlmU uridylyltransferase, Acetylglucosamine 1-phosphate uridylyltransferase, UDP-acetylglucosamine pyrophosphorylase, uridine diphosphate-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, and acetylglucosamine 1-phosphate uridylyltransferase.

References

  1. ↑ Strominger, Jack L.; Smith, Mildred S. (1959). "Uridine Diphosphoacetylglucosamine Pyrophosphorylase". Journal of Biological Chemistry. 234 (7): 1822–1827. doi:10.1016/S0021-9258(18)69933-8. PMID 13672971.
  2. ↑ Pattabiraman, T.N.; Bachhawat, B.K. (1961). "Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain". Biochimica et Biophysica Acta. 50: 129–134. doi:10.1016/0006-3002(61)91068-X. PMID 13733356.
  3. ↑ Mengin-Lecreulx, D.; Van Heijenoort, J. (1994). "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". Journal of Bacteriology. 176 (18): 5788–5795. doi:10.1128/jb.176.18.5788-5795.1994. PMC 196783. PMID 8083170.
  4. ↑ Gehring, Amy M.; Lees, Watson J.; Mindiola, Daniel J.; Walsh, Christopher T.; Brown, Eric D. (1996). "Acetyltransfer Precedes Uridylyltransfer in the Formation of UDP- N -acetylglucosamine in Separable Active Sites of the Bifunctional GlmU Protein of Escherichia coli". Biochemistry. 35 (2): 579–585. doi:10.1021/bi952275a. PMID 8555230.
  5. ↑ Wang-Gillam, Andrea; Pastuszak, Irena; Elbein, Alan D. (1998). "A 17-Amino Acid Insert Changes UDP-N-Acetylhexosamine Pyrophosphorylase Specificity from UDP-GalNAc to UDP-GlcNAc". Journal of Biological Chemistry. 273 (42): 27055–27057. doi:10.1074/jbc.273.42.27055. PMID 9765219.
  6. ↑ Olsen, Laurence R.; Roderick, Steven L. (2001). "Structure of the Escherichia coli GlmU Pyrophosphorylase and Acetyltransferase Active Sites,". Biochemistry. 40 (7): 1913–1921. doi:10.1021/bi002503n. PMID 11329257.
  7. ↑ Peneff, Caroline; Ferrari, Paul; Charrier, Véronique; et al. (2001). "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". The EMBO Journal. 20 (22): 6191–6202. doi:10.1093/emboj/20.22.6191. PMC 125729. PMID 11707391.
  8. ↑ Enzyme 2.7.7.23 at KEGG Pathway Database.