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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

Reaction

N-acetyl-D-glucosamine 6-phosphate
+
H2O
=
D-glucosamine 6-phosphate
+
acetate

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

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.25 N-acetylglucosamine-6-phosphate deacetylase

Crystallization

Crystallization on EC 3.5.1.25 - N-acetylglucosamine-6-phosphate deacetylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 18°C, precipitant is sodium dihydrogen phosphate, X-ray diffraction structure determination and analysis at 2.0-2.9 A resolution
purified recombinant His6-tagged enzyme MSNagA in both ligand-free form and in complex with the N-acetyl-D-glucosamine-6-phosphate substrate, X-ray diffraction structure determination and analysis at 2.6 and 2.0 A resolutions, respectively, molecular replacement