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Literature summary extracted from

  • Stein, R.L.
    Enzymatic hydrolysis of p-nitroacetanilide: mechanistic studies of the aryl acylamidase from Pseudomonas fluorescens (2002), Biochemistry, 41, 991-1000.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.13 0.012
-
p-nitroacetanilide 25°C, pH 8 Pseudomonas fluorescens
3.5.1.13 0.018
-
4-nitrophenyl acetate 25°C, pH 8 Pseudomonas fluorescens
3.5.1.13 0.02
-
p-nitroacetanilide 25°C, pH 10 Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.13 Pseudomonas fluorescens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.13 4-nitrophenyl acetate + H2O
-
Pseudomonas fluorescens ?
-
?
3.5.1.13 p-nitroacetanilide + H2O studies on the mechanism of the reaction Pseudomonas fluorescens p-nitroaniline + acetate
-
r
3.5.1.13 p-nitrophenyl acetate + H2O
-
Pseudomonas fluorescens p-nitrophenol + acetate
-
r

Synonyms

EC Number Synonyms Comment Organism
3.5.1.13 AAA
-
Pseudomonas fluorescens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.13 8 11 maximal activity in this range of pH, enzyme is inactive below pH 7.5 Pseudomonas fluorescens