3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase
This is an abbreviated version!
For detailed information about N-acetylglucosamine-6-phosphate deacetylase, go to the full flat file.
Word Map on EC 3.5.1.25
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3.5.1.25
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deaminase
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chitin
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fructose-6-phosphate
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glcn-6-phosphate
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non-o1
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drug development
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diagnostics
- 3.5.1.25
- deaminase
- chitin
- fructose-6-phosphate
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glcn-6-phosphate
- non-o1
- drug development
- diagnostics
Reaction
Synonyms
2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase, acetylaminodeoxyglucosephosphate acetylhydrolase, acetylglucosamine phosphate deacetylase, CaNAG2/Dac1, deacetylase, acetylglucosaminephosphate, EC 3.5.1.80, GlcNAc 6-P deacetylase, GlcNAc-6-phosphate deacetylase, GlnNAc6P deacetylase, Lmo0956, Lmo0956 protein, Lmo2108, Lmo2108 protein, MMNagA, MSNagA, N-acetyl-D-glucosamine-6-phosphate deacetylase, N-acetylglucosamine 6-phosphate deacetylase, N-acetylglucosamine-6-P deacetylase, N-acetylglucosamine-6-phosphate de-N-acetylase, N-acetylglucosamine-6-phosphate deacetylase, NAG2, NagA, NAGPase
ECTree
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Subunits
Subunits on EC 3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase
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dimer
homotetramer
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determined by gel filtration chromatography, SAXS and analytical ultracentrifugation, dimer of dimers
tetramer
additional information
x * 41670, sequence calculation, x * 45498, recombinant His-tagged enzyme, mass spectrometry
?
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x * 41670, sequence calculation, x * 45498, recombinant His-tagged enzyme, mass spectrometry
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dimer
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NagA is an asymmetric dimer in solution, analytical ultracentrifugation and small-angle X-ray scattering data
dimer
Staphylococcus aureus USA300_TCH1516
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NagA is an asymmetric dimer in solution, analytical ultracentrifugation and small-angle X-ray scattering data
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tetramer
analysis of the dimer-dimer interface, the tertiary and quarternary structure, the apoenzyme shows conformational changes in two loops adjacent to the active site, crystal structure
tetramer
Vibrio cholerae serotype O1 Non-O1
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4 * 45000, SDS-PAGE
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enzyme structure comparisons, overview
additional information
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involvement of both subunits in binding substrate
additional information
Staphylococcus aureus USA300_TCH1516
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involvement of both subunits in binding substrate
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additional information
the enzyme contains four internal disulfide bonds, Cys246, Cys256, Cys274, and Cys350 that may contribute to the formation of six internal disulfide bridges. Tryptic peptide mapping of the enzyme, overview
additional information
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the enzyme contains four internal disulfide bonds, Cys246, Cys256, Cys274, and Cys350 that may contribute to the formation of six internal disulfide bridges. Tryptic peptide mapping of the enzyme, overview
additional information
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the enzyme contains four internal disulfide bonds, Cys246, Cys256, Cys274, and Cys350 that may contribute to the formation of six internal disulfide bridges. Tryptic peptide mapping of the enzyme, overview
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