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Literature summary for 3.5.1.25 extracted from

  • Xu, C.; Hall, R.; Cummings, J.; Raushel, F.M.
    Tight binding inhibitors of N-acyl amino sugar and N-acyl amino acid deacetylases (2006), J. Am. Chem. Soc., 128, 4244-4245.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
methyl phosphonamidates inhibitor 1 tetrahedral reaction intermediate analogues Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ 1 equivalent of zinc bound at the Mbeta site, the enzyme contains a binuclear metal center at the active site Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-D-glucosamine 6-phosphate + H2O Escherichia coli
-
D-glucosamine 6-phosphate + acetate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene nagA
-

Reaction

Reaction Comment Organism Reaction ID
N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate catalytic mechanism, enzyme-substrate interaction analysis Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-glucosamine 6-phosphate + H2O
-
Escherichia coli D-glucosamine 6-phosphate + acetate
-
?

Synonyms

Synonyms Comment Organism
NagA
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics, inhibitor binding model Escherichia coli
0.000034
-
methyl phosphonamidates inhibitor 1 pH 7.5, 30°C, recombinant enzyme Escherichia coli