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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: glucosamine-6-phosphate N-acetyltransferase 1

Gene: Gnpnat1 Accession Number: G-10022 (MetaCyc)

Synonyms: EMeg32

Species: Mus musculus

Summary:
Recombinant mouse glucosamine-6-phosphate acetyltransferase 1 has been expressed in both Escherichia coli and insect cells. The subunit relative molecular mass was estimated by SDS-PAGE, but the subunit structure was not determined [Boehmelt00].

Glucosamine-6-phosphate N-acetyltransferase is a member of the Gcn5-related N-acetyltransferases that catalyze the transfer of an acetyl group of acetyl-CoA to the primary amine of an acceptor substrate. The crystal structure of the enzyme from Saccharomyces cerevisiae has been determined and indicated a homodimeric structure [Peneff01]. Reviewed in [Milewski06].

Locations: late endosome membrane, Golgi membrane, lysosomal membrane

Map Position: [44,298,298 <- 44,310,673]

Molecular Weight of Polypeptide: 20.791 kD (from nucleotide sequence), 21 kD (experimental) [Boehmelt00 ]

Unification Links: Entrez-gene:54342 , Mint:MINT-1605392 , PhosphoSite:Q9JK38 , Pride:Q9JK38 , Protein Model Portal:Q9JK38 , SMR:Q9JK38 , String:Q9JK38 , UniProt:Q9JK38

Relationship Links: InterPro:IN-FAMILY:IPR000182 , InterPro:IN-FAMILY:IPR016181 , Pfam:IN-FAMILY:PF13508 , Prosite:IN-FAMILY:PS51186

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0000139 - Golgi membrane [Boehmelt00]
GO:0005765 - lysosomal membrane [Boehmelt00]
GO:0031902 - late endosome membrane [Boehmelt00]

Credits:
Created 20-Apr-2007 by Fulcher CA , SRI International


Enzymatic reaction of: glucosamine-6-phosphate acetyltransferase (glucosamine-6-phosphate N-acetyltransferase 1)

Synonyms: glucosamine-6-phosphate N-acetyltransferase, phosphoglucosamine acetyltransferase, acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase, EMeg32/mGlcN6P-AT

EC Number: 2.3.1.4

D-glucosamine 6-phosphate + acetyl-CoA <=> N-acetyl-D-glucosamine 6-phosphate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: UDP-N-acetyl-D-glucosamine biosynthesis II

Summary:
Kinetic parameters for murine glucosamine-6-phosphate acetyltransferase were determined for the recombinant, his-tagged enzyme expressed in insect cells using a baculovirus vector [Boehmelt00].

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-glucosamine 6-phosphate
40.0
[Boehmelt00]
acetyl-CoA
120.0
[Boehmelt00]


References

Boehmelt00: Boehmelt G, Fialka I, Brothers G, McGinley MD, Patterson SD, Mo R, Hui CC, Chung S, Huber LA, Mak TW, Iscove NN (2000). "Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association." J Biol Chem 275(17);12821-32. PMID: 10777580

Milewski06: Milewski S, Gabriel I, Olchowy J (2006). "Enzymes of UDP-GlcNAc biosynthesis in yeast." Yeast 23(1);1-14. PMID: 16408321

Peneff01: Peneff C, Mengin-Lecreulx D, Bourne Y (2001). "The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase." J Biol Chem 276(19);16328-34. PMID: 11278591


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC14A.