|Gene:||Gnpnat1||Accession Number: G-10022 (MetaCyc)|
Species: Mus musculus
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 ]
|Cellular Component:||GO:0000139 - Golgi membrane
GO:0005765 - lysosomal membrane [Boehmelt00]
GO:0031902 - late endosome membrane [Boehmelt00]
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: 18.104.22.168
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
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].
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
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
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