Literature summary for 3.5.1.4 extracted from

Novo, C.; Farnaud, S.; Tata, R.; Clemente, A.; Brown, P.R.
Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity (2002), Biochem. J., 365, 731-738.

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Protein Variants

Protein Variants	Comment	Organism
E59D	inactive mutant	Pseudomonas aeruginosa
E59Q	inactive mutant	Pseudomonas aeruginosa
K134B	inactive mutant	Pseudomonas aeruginosa
K134R	200fold reduction in activity compared to wild type enzyme	Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.5	-	p-nitroacetanilide	strain AI3	Pseudomonas aeruginosa
0.63	-	p-nitroacetanilide	strain 10A	Pseudomonas aeruginosa
1.17	-	p-nitroacetanilide	strain 8A	Pseudomonas aeruginosa
1.98	-	p-nitroacetanilide	strain 3B	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	P11436	-	-

Purification (Commentary)

Purification (Comment)	Organism
affinity chromatography on an acetamide epoxy-activated Sepharose column	Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
p-nitroacetanilide + H2O	-	Pseudomonas aeruginosa	p-nitroaniline + acetate	-	?

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Release 2023.1 (January 2023)