|Gene:||GNA||Accession Number: G-10031 (MetaCyc)|
Species: Giardia intestinalis
The subunit structure of the Giardia intestinalis (previously known as Giardia lamblia) enzyme has not been reported.
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 recombinant enzyme from Saccharomyces cerevisiae expressed in Escherichia coli has been determined. Gel filtration chromatography and crystallographic analysis indicated a homodimeric structure for the yeast enzyme [Peneff01]. Reviewed in [Milewski06].
Molecular Weight of Polypeptide: 22.817 kD (from nucleotide sequence)
|Cellular Component:||GO:0005829 - cytosol [Macechko92]|
Enzymatic reaction of: glucosamine 6-phosphate N-acetylase
Synonyms: glucosamine 6-phosphate N-acetyltransferase, glucosamine-phosphate N-acetyltransferase, GNA
EC Number: 22.214.171.124
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-galactosamine biosynthesis II
Glucosamine 6-phosphate N-acetylase from Giardia intestinalis (Giardia lamblia) was assayed in homogenates of encysting or non-encysting organisms [Macechko92].
pH(opt): 5 [Macechko92]
Lopez03: Lopez AB, Sener K, Jarroll EL, van Keulen H (2003). "Transcription regulation is demonstrated for five key enzymes in Giardia intestinalis cyst wall polysaccharide biosynthesis." Mol Biochem Parasitol 128(1);51-7. PMID: 12706796
Macechko92: Macechko PT, Steimle PA, Lindmark DG, Erlandsen SL, Jarroll EL (1992). "Galactosamine-synthesizing enzymes are induced when Giardia encyst." Mol Biochem Parasitol 56(2);301-9. PMID: 1484552
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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