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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: glucosamine 6-phosphate N-acetylase

Gene: GNA Accession Number: G-10031 (MetaCyc)

Species: Giardia intestinalis

Summary:
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].

The recombinant enzyme from Giardia intestinalis has been expressed in Escherichia coli as a GST-fusion protein and purified. The fusion protein was shown to be enzymatically active [Lopez03b].

Locations: cytosol

Molecular Weight of Polypeptide: 22.817 kD (from nucleotide sequence)

Unification Links: Protein Model Portal:Q868I8 , UniProt:Q868I8

Relationship Links: Entrez-Nucleotide:PART-OF:AY185915 , InterPro:IN-FAMILY:IPR000182 , InterPro:IN-FAMILY:IPR016181 , Pfam:IN-FAMILY:PF00583 , Prosite:IN-FAMILY:PS51186

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0005829 - cytosol [Macechko92]

Credits:
Created 14-May-2007 by Fulcher CA , SRI International


Enzymatic reaction of: glucosamine 6-phosphate N-acetylase

Synonyms: glucosamine 6-phosphate N-acetyltransferase, glucosamine-phosphate N-acetyltransferase, GNA

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-galactosamine biosynthesis II

Summary:
Glucosamine 6-phosphate N-acetylase from Giardia intestinalis (Giardia lamblia) was assayed in homogenates of encysting or non-encysting organisms [Macechko92].

Kinetic Parameters:

Substrate
Km (μM)
Citations
D-glucosamine 6-phosphate
7500.0
[Macechko92]
acetyl-CoA
15000.0
[Macechko92]

pH(opt): 5 [Macechko92]


References

Lopez03b: 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

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 Sun Nov 23, 2014, BIOCYC13A.