Glucosamine-1-phosphate N-acetyltransferase

Glucosamine-1-phosphate N-acetyltransferase
Identifiers
EC no.2.3.1.157
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157) is an enzyme that catalyzes the chemical reaction

2D representation of the chemical structure of Q27094063.
(1)
+
 
acetyl-CoA
 
 
 
Rightward reaction arrow
 
 
 
2D representation of the chemical structure of Q27101910.
(2)
+ coenzyme A
 

The two substrates of this enzyme characterised from Escherichia coli are α-D-glucosamine 1-phosphate (1) and acetyl-CoA. Its two products are N-acetyl-α-D-glucosamine 1-phosphate (2) and coenzyme A. The enzyme is part of the biosynthetic pathway to UDP-N-acetylglucosamine.

UDP-N-acetylglucosamine

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2OI5​, PDB: 2OI6​, and PDB: 2OI7​.

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ Enzyme 2.3.1.157 at KEGG Pathway Database.