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(+)-methyl mandelate + H2O
?
-
-
-
-
?
(R) -2-(4-hydroxyphenyl)glycine amide + H2O
(R) -2-(4-hydroxyphenyl)glycine + hydroxylamine
-
-
-
?
(R)-2-phenylglycine amide + H2O
(R)-2-phenylglycine + hydroxylamine
(R)-2-phenylglycine methyl ester + H2O
(R)-2-phenylglycine + methanol
(R)-beta-phenylalanine + phenylacetamide
N-phenylacetyl-(R)-beta-phenylalanine + ?
-
the acylation reaction is highly preferential for the acylation of (R)-beta-phenylalanine
-
-
?
(R)-mandelic acid methyl ester + H2O
?
-
-
-
-
?
(R)-N-acetylphenylglycine + H2O
?
-
S-specific, the stereoselectivity of the reaction decreases almost by one order of magnitude from 5°C to 45°C
-
?
(R)-p-hydroxyphenylglycinamide + H2O
?
-
R-specific, the stereoselectivity of the reaction decreases almost by one order of magnitude from 5°C to 45°C
-
?
(R)-phenylglycinamide + H2O
?
-
R-specific, the stereoselectivity of the reaction decreases almost by one order of magnitude from 5°C to 45°C
-
?
(S)-N-acetylphenylglycine + H2O
?
-
S-specific, the stereoselectivity of the reaction decreases almost by one order of magnitude from 5°C to 45°C
-
?
(S)-p-hydroxyphenylglycinamide + H2O
?
-
R-specific, the stereoselectivity of the reaction decreases almost by one order of magnitude from 5°C to 45°C
-
?
(S)-phenylglycinamide + H2O
?
-
R-specific, the stereoselectivity of the reaction decreases almost by one order of magnitude from 5°C to 45°C
-
?
2-furylmethylpenicillin + H2O
6-aminopenicillanate + furan-2-yl-acetic acid
-
-
-
?
2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O
5-amino-2-nitrobenzoic acid + phenoxyacetate
2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O
?
-
-
-
?
2-nitro-5-phenoxyacetamide benzoic acid + H2O
?
-
-
-
?
2-nitro-5-phenylacetamidobenzoic acid + H2O
phenylacetate + 2-aminobenzoic acid
-
-
-
-
?
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid + H2O
?
-
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]-benzoic acid + H2O
5-amino-2-nitrobenzoic acid + ?
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]-benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
2-phenyl-N-(4-sulfamoylphenyl)acetamide + H2O
phenylacetate + 2-amino-4-sulfamoylphenol
-
-
-
-
?
2-phenylacetamidobenzoic acid + H2O
phenylacetate + 2-aminobenzoic acid
-
-
-
-
?
2-thienylmethylpenicillin + H2O
6-aminopenicillanate + sulfo-(5-sulfothiophen-2-yl)-acetic acid
-
-
-
-
?
3-nitro-6-phenylacetaminobenzoic acid + H2O
6-nitrophenol + ?
-
-
-
-
?
3-nitro-6-phenylacetaminobenzoic acid + H2O
?
3-phenylacetamidobenzoic acid + H2O
phenylacetate + 3-aminobenzoic acid
-
-
-
-
?
4-chloro-L-phenylalanine + phenylacetamide
N-[(4-chlorophenyl)acetyl]-L-tyrosine + NH3
-
-
-
-
?
4-fluoro-L-phenylalanine + phenylacetamide
N-[(4-fluorophenyl)acetyl]-L-tyrosine + NH3
-
-
-
-
?
4-hydroxyphenylacetamide + 6-aminopenicillanic acid
?
4-methyl-L-phenylalanine + phenylacetamide
N-[(4-methylphenyl)acetyl]-L-tyrosine + NH3
-
-
-
-
?
4-nitro-L-phenylalanine + phenylacetamide
N-[(4-nitrophenyl)acetyl]-L-tyrosine + NH3
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-phenylacetamidobenzoic acid + H2O
phenylacetate + 4-aminobenzoic acid
-
-
-
-
?
5-nitro-3-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetate + 3-amino-5-nitro-benzoic acid
-
-
-
-
?
5-[[(2R)-2-amino-2-phenylethanoyl]amino]-2-nitrobenzoic acid + H2O
5-amino-2-nitrobenzoic acid + (R)-2-phenylglycine
-
-
-
?
6-aminopenicillanate + phenylacetic acid
penicillin G + H2O
6-aminopenicillanic acid + methyl n-hexanoate
dihydropenicillin F + methanol
-
-
-
-
?
6-aminopenicillanic acid + methyl n-octanoate
penicillin K + methanol
-
-
-
-
?
6-aminopenicillanic acid + p-hydroxyphenylglycine methyl ester
amoxicillin + methanol
-
-
-
-
?
6-aminopenicillanic acid + phenoxyacetic acid
penicillin V + H2O
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
6-nitro-3-(phenylacetamido)benzoic acid + H2O
3-amino-6-nitrobenzoic acid + ?
-
-
-
-
?
6-nitro-3-(phenylacetamido)benzoic acid + H2O
?
6-nitro-3-(phenylacetamido)benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
-
?
6-nitro-3-phenylacetamide benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-phenylacetamide benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
6-nitro-3-phenylacetamido-benzoic acid + H2O
?
6-nitro-3-phenylacetamidobenzoic acid + H2O
?
6-nitro-3-[(phenylacetyl)amino]benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
7-amino-3-deacetoxycephalosporanic acid + phenylglycine methyl ester
cephalexin + ?
-
-
-
-
?
7-amino-3-propenyl-cephalosporanic acid + 4-hydroxy-D-phenylglycine methyl ester
cefprozil + ?
-
-
-
?
7-amino-deacetoxycephalosporanic acid + phenylacetic acid
deacetoxycephalosporin G + H2O
-
-
-
-
?
7-amino-desacetoxycephalosporanic acid + D-alpha-phenylglycine methylester
?
-
acylating activity
-
-
?
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide
cephalexin
-
high reactant concentrations
-
-
r
7-aminocephalosporanic acid + (R)-mandelic acid
7-[(1-hydroxy-1-phenyl)-acetamido]-3-acetoxymethyl-D3-cephem-4-carboxylic acid
-
-
-
-
?
7-aminocephalosporanic acid + D-alpha-phenylglycine methylester
?
-
acylating activity
-
-
?
7-aminodeacetoxycephalosporanic acid + (R)-2-phenylglycine methylester
cephalexin + ?
-
-
-
-
?
7-aminodeacetoxycephalosporanic acid + 2-benzoxazolon-3-yl-acetic acid methyl ester
?
-
-
-
?
7-aminodeacetoxycephalosporanic acid + phenoxyacetic acid
deacetoxycephalosporin V + H2O
-
-
-
-
?
7-aminodeacetoxycephalosporanic acid + phenylacetic acid methyl ester
?
-
-
-
?
7-phenylacetamidoacetoxycephalosporanic acid + H2O
?
-
-
-
-
?
aculeacin A + H2O
?
recombinant enzyme
-
-
?
allopurinol + vinyl acetate
1-(4-oxo-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-1-yl)ethyl acetate
-
Markovnikov addition, decrease in activity in the order vinyl acetate, vinyl pentanoate, vinyl decanoate
-
-
?
allopurinol + vinyl decanoate
1-(4-oxo-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-1-yl)ethyl decanoate
-
Markovnikov addition, decrease in activity in the order vinyl acetate, vinyl pentanoate, vinyl decanoate
-
-
?
allopurinol + vinyl pentanoate
1-(4-oxo-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-1-yl)ethyl pentanoate
-
Markovnikov addition, decrease in activity in the order vinyl acetate, vinyl pentanoate, vinyl decanoate
-
-
?
allylmercaptomethylpenicillin + H2O
?
-
poor substrate
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxillin + H2O
D-4-hydroxyphenylglycine + 6-aminopenicillanic acid
amoxycillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
ampicillin + H2O
6-aminopenicillanic acid + (R)-2-phenylglycine
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
benzylpenicilloic acid + H2O
?
-
-
-
-
?
beta-(alpha-toluylamido)-propionic acid + H2O
?
-
poor substrate
-
-
?
capsaicin + H2O
?
-
-
-
?
carbenicillin + H2O
phenylpropanedioate + 6-aminopenicillate
-
-
-
?
cefamandole + H2O
(6R,7R)-7-amino-3-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (2R)-hydroxy(phenyl)acetic acid
-
-
-
-
?
cephadrine + H2O
?
Pseudomonas melanogenum
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
-
-
-
-
?
cephalexin + H2O
7-amino-3-methyl-8-oxo-5-thia-1-aza-bicyclo[4.2.0]oct-2-ene-2-carboxylic acid + D-phenylglycine
cephalexin + H2O
7-aminodesacetoxycephalosporanic acid + D-phenylglycine
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
r
cephaloglycin + H2O
(6R,7R)-7-amino-3-(hydroxymethyl)-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (2R)-amino(phenyl)acetic acid
Pseudomonas melanogenum
-
-
-
-
?
cephaloglycin + H2O
?
-
-
-
-
?
cephaloridine + H2O
(6R,7R)-7-amino-8-oxo-3-[(pyridin-1-ium-1-yl)methyl]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + (thiophen-2-yl)acetic acid
cephaloridine + H2O
thiophen-2-ylacetic acid + (6R,7R)-7-amino-8-oxo-3-(pyridinium-1-yl-methyl)-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
-
?
cephalosporanic acid V + H2O
?
-
-
-
-
?
cephalosporin + H2O
7-aminocephalosporanic acid + an amino acid
cephalosporin C + H2O
7-aminocephalosporanic acid + (R)-2-aminohexadioic acid
-
2.4% of the activity compared to penicillin V
-
-
?
cephalosporin G + H2O
7-amino-desacetoxycephalosporanic acid + phenylacetic acid
-
-
-
-
?
cephalosporin G + H2O
7-aminodeacetoxycephalosporanate + phenylacetic acid
-
-
-
-
r
cephalosporin G + H2O
phenylacetic acid + 7-aminodeacetoxycephalosporanate
-
-
-
-
?
cephalothin + H2O
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (thiophen-2-yl)acetic acid
cephalothin + H2O
thiophen-2-ylacetic acid + (6R,7R)-3-acetoxymethyl-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
-
?
cephradine + H2O
(2R)-amino(cyclohexa-1,4-dien-1-yl)acetic acid + (6R,7R)-7-amino-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
-
-
-
?
D,L-N-phenylacetylalanine + H2O
?
-
poor substrate
-
-
?
D-(-)-alpha-aminophenylacetic acid 4-nitroanilide + H2O
D-(-)-alpha-aminophenylacetic acid + 4-nitrophenol
-
-
-
-
?
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
D-2-nitro-5[(phenylglycyl)amino]benzoic acid + H2O
?
-
-
-
-
?
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxicillin + NH3
D-alpha-aminobenzylpenicillin + H2O
6-aminopenicillanate + DL-alpha-aminophenylacetic acid
-
-
-
?
D-hydroxyphenylglycine methyl ester + H2O
?
D-phenylglycine amide + 6-aminopenicillanic acid
ampicillin + NH3
D-phenylglycine amide + 7-aminodeacetoxycephalosporanic acid
cephalexin + ?
-
-
-
?
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
D-phenylglycine amide + 7-aminodesacetoxymethyl-3-chlorocephalosporanic acid
cephaclor + ?
-
-
-
?
D-phenylglycine amide + H2O
D-phenylglycine + NH3
-
-
-
-
?
D-phenylglycine methyl ester + 6-aminopenicillanic acid
methanol + ampicillin
-
-
-
r
D-phenylglycine methyl ester + 6-aminopenicillic acid
ampicillin + methanol
-
high ratio of synthesis to hydrolysis at up to 200 mM 6-aminopenicillic acid and 500 mM D-phenylglycine methyl ester at 25°C and pH 6.5. When concentration of 6-aminopenicillic acid reaches saturation, rate of hydrolysis tends toward zero
-
-
r
D-phenylglycine methyl ester + 7-aminodeacetoxycephalosporanic acid
cephalexin + ?
-
-
-
?
D-phenylglycine methyl ester + 7-aminodesacetoxymethyl-3-chlorocephalosporanic acid
cephaclor + ?
-
-
-
?
delta2-pentenylpenicillin + H2O
?
-
poor substrate
-
-
?
diethyl phenylmalonate + H2O
(+)-ethyl phenylmalonate + ethanol
-
the enantiomeric excess is higher than 98%, producing mainly the (+)-ethyl phenylmalonate ester
-
-
?
dimethyl phenylmalonate + H2O
(+)-methyl phenylmalonate + methanol
-
dimethyl phenylmalonate is fully hydrolyzed to methylphenylmalonate in only 2 h, but even after 10 h phenylmalonic acid is not detected. The enantiomeric excess is higher than 98%, producing mainly the (+)-methyl phenylmalonate ester
-
-
?
DL-alpha-hydroxybenzylpenicillin + H2O
6-aminopenicillanate + DL-alpha-hydroxyphenylacetic acid
-
-
-
?
ethyl 2-phenylacetate + H2O
2-phenylacetate + ethanol
-
-
-
-
?
ethyl 4-[(phenylacetyl)amino] benzoate + H2O
phenylacetate + 4-amino-ethylbenzoate
-
-
-
-
?
ethylthiomethylpenicillin + H2O
?
-
poor substrate
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
glutarate + 7-aminocephalosporanic acid
-
-
-
-
?
hydroxyphenylglycineamide + 7-aminodeacetoxycephalosporanic acid
cefadroxil + NH3
-
-
-
-
?
isobutoxymethylpenicillin + H2O
6-aminopenicillanate + carbonic acid isopropyl ester
-
-
-
-
?
L-phenylalanine + (2S)-2-amino-2-phenylethanamide
N-[(2S)-2-amino-2-phenylacetyl]-L-phenylalanine + NH3
-
-
-
-
?
L-phenylalanine + (2S)-2-hydroxy-2-phenylethanamide
N-[(2S)-2-hydroxy-2-phenylacetyl]-L-phenylalanine + NH3
-
-
-
-
?
L-phenylalanine + 2-(4-hydroxyphenyl)acetamide
N-[(4-hydroxyphenyl)acetyl]-L-phenylalanine + NH3
-
-
-
-
?
L-phenylalanine + methyl (2S)-hydroxy(4-hydroxyphenyl)ethanoate
N-[(2S)-2-hydroxy-2-phenylacetyl]-L-phenylalanine + methanol
-
-
-
-
?
L-phenylalanine + methyl (4-hydroxyphenyl)acetate
N-[(4-hydroxyphenyl)acetyl]-L-phenylalanine + methanol
-
-
-
-
?
L-phenylalanine + methyl phenylacetate
N-phenylacetyl-L-phenylalanine + methanol
-
-
-
-
?
L-phenylalanine + N-[(2S)-2-amino-2-phenylacetyl]-L-phenylalanine
N-[(2S)-2-amino-2-phenylacetyl]-L-phenylalanine + methanol
-
-
-
-
?
L-phenylalanine + phenylacetamide
N-phenylacetyl-L-phenylalanine + NH3
-
-
-
-
?
L-tyrosine + phenylacetamide
N-(phenylacetyl)-L-tyrosine + NH3
-
-
-
-
?
N,2-diphenylacetamide + H2O
phenylacetate + ?
-
-
-
-
?
N-(4-acetylphenyl)-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-acetylphenol
-
-
-
-
?
N-(4-bromophenyl)-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-bromophenol
-
-
-
-
?
N-(4-cyanophenyl)-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-cyanophenol
-
-
-
-
?
N-(4-methoxyphenyl)-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-methoxyphenol
-
-
-
-
?
N-(4-methylphenyl)-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-methylphenol
-
-
-
-
?
N-(4-nitrophenyl)-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-nitrophenol
-
-
-
-
?
N-(5-nitro-2-pyridyl)-phenylacetamide + H2O
phenylacetate + 5-nitropyridin-2-amine
-
-
-
-
?
N-(phenylacetyl)glycine + H2O
phenylacetic acid + glycine
-
-
-
?
N-methylphenylacetamide + H2O
?
-
poor substrate
-
-
?
N-phenylacetyl-alpha-homophenylalanine + H2O
homophenylalanine + phenylacetate
N-phenylacetyl-alpha-isoleucine + H2O
isoleucine + phenylacetate
N-phenylacetyl-alpha-leucine + H2O
leucine + phenylacetate
N-phenylacetyl-alpha-phenylalanine + H2O
phenylalanine + phenylacetate
N-phenylacetyl-alpha-tert-leucine + H2O
tert-leucine + phenylacetate
N-phenylacetyl-Asp + H2O
phenylacetic acid + Asp
-
-
-
?
N-phenylacetyl-Asp-Phe methyl ester + H2O
phenylacetic acid + Asp-Phe methyl ester
-
-
-
?
N-phenylacetyl-beta-homoleucine + H2O
beta-homoleucine + phenylacetate
N-phenylacetyl-beta-leucine + H2O
beta-leucine + phenylacetate
N-phenylacetyl-DL-leucine + H2O
?
-
-
-
-
?
N-phenylacetyl-DL-tert-leucine + H2O
L-tert-leucine + phenylacetate
-
enantioselective hydrolysis
-
-
?
N-phenylacetyl-Glu + H2O
phenylacetic acid + Glu
-
-
-
?
N-phenylacetyl-L-alpha-aminophenylacetic acid + H2O
?
-
-
-
-
?
N-phenylacetyl-Leu + H2O
phenylacetic acid + Leu
-
-
-
?
N-phenylacetyl-Phe + H2O
phenylacetic acid + Phe
-
-
-
?
N-phenylacetylglycine + H2O
?
-
-
-
-
?
n-propoxymethylpenicillin + H2O
6-aminopenicillanate + carbonic acid monopropyl ester
-
-
-
-
?
N-[4-(methylsulfonyl)phenyl]-2-phenylacetamide + H2O
phenylacetate + 2-amino-4-(methylsulfonyl)phenol
-
-
-
-
?
N2-phenylacetyl-2'-deoxyguanosine + H2O
phenylacetic acid + 2'-deoxyguanosine
N6-phenylacetyl-2'-deoxyadenosine + H2O
phenylacetic acid + 2'-deoxyadenosine
p-hydroxybenzylpenicillin + H2O
6-aminopenicillanate + p-hydroxyphenylacetic acid
-
-
-
?
penicillin + H2O
a carboxylate + 6-aminopenicillanate
-
-
-
?
penicillin dihydroF + H2O
6-aminopenicillanic acid + hexanoic acid
penicillin dihydroF + H2O
?
-
substrate of immobilized enzyme
-
-
?
penicillin F + H2O
6-aminopenicillanic acid + (3E)-hex-3-enoic acid
penicillin F + H2O
?
-
substrate of immobilized enzyme
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
penicillin G + H2O
6-aminopenicillanic acid + phenyl acetic acid
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
penicillin G + H2O
phenyl acetic acid + 6-aminopenicillanate
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanic acid
penicillin K + H2O
6-aminopenicillanic acid + octanoic acid
-
-
-
-
?
penicillin K + H2O
?
-
substrate of immobilized enzyme
-
-
?
penicillin K + H2O
octanoic acid + 6-aminopenicillanate
penicillin V + H2O
6-aminopenicillanate + phenoxyacetate
the conversion yields of 6-aminopenicillanate catalyzed by mutant enzyme T63S/S110C/N198Y reaches 98% with 20% (w/v) penicillin V as substrate, which is significantly higher than that of the wild-type enzyme (85%). The enhancement of specific activity of mutant enzyme is probably attributed to the changes in the number of hydrogen bonds within the molecules
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
penicillin V + H2O
phenoxyacetic acid + 6-aminopenicillanate
-
-
-
-
?
penicillin V sulfoxide + H2O
?
-
-
-
-
?
penicillin-G + H2O
6-aminopenicillanic acid + phenylacetic acid
phenoxyethylpenicillin + H2O
3-phenoxypropanoic acid + 6-aminopenicillanic acid
-
poor substrate
-
-
?
phenylacetamide + 6-aminopenicillanic acid
?
phenylacetamide + H2O
NH3 + ?
-
poor substrate
-
-
?
phenylacetamide + H2O
phenylacetate + NH3
-
-
-
-
?
phenylacetate 4-nitroanilide + H2O
phenylacetic acid + 4-nitrolaniline
-
-
-
-
?
phenylacetic acid + 6-aminopenicillanic acid
penicillin G
phenylacetic hydrazide + H2O
phenylacetate + hydrazine
-
-
-
-
?
phenylacetyl-2-naphthylamide + H2O
phenylacetate + 2-naphthylamine
-
-
-
-
?
phenylacetyl-4-aminobenzoic acid
4-aminobenzoic acid + phenylacetic acid
-
colometric assay
-
?
phenylacetyl-7-amido-4-methylcoumarin + H2O
phenylacetate + 7-amino-4-methylcoumarin
-
-
-
-
?
phenylacetyl-Gly + H2O
phenylacetic acid + glycine
-
-
-
?
phenylacetyl-L-asparagine + H2O
L-asparagine + phenylacetic acid
-
-
-
?
phenylacetyl-L-leucine + H2O
?
-
-
-
-
?
phenylacetylanthranilic acid + H2O
phenylacetate + 2-aminobenzoic acid
-
colometric assay
-
?
phenylacetylaspartame + H2O
phenylacetic acid + aspartame
-
-
-
?
phenylacetylglycine + 6-aminopenicillanic acid
penicillin G + glycine
phenylglycine methyl ester + aminopenicillanic acid
ampicillin + methanol
-
-
-
?
phenylglycineamide + 7-aminodeacetoxycephalosporanic acid
cefaclor + NH3
-
-
-
-
?
phenylglycinemethylester + 7-aminodeacetoxymethyl-3-chlorocephalosporanic acid
cephalexin + methanol
-
-
-
-
?
vanillylamine + methyl laurate
6-lauroyl-vanillylamide + methanol
-
-
-
-
?
vanillylamine + methyl myristate
6-myristoyl-vinillylamide + methanol
-
-
-
-
?
vanillylamine + methyl n-octanoate
6-octanoyl-vanillylamide + methanol
-
-
-
-
?
[(2R,3S),(2S,3R)]-cis-3-amino-azetidinone + phenoxy-acetic acid methyl ester
(2R,3S)-beta-lactam intermediate + methanol
-
-
-
-
?
additional information
?
-
(R)-2-phenylglycine amide + H2O
(R)-2-phenylglycine + hydroxylamine
-
-
-
?
(R)-2-phenylglycine amide + H2O
(R)-2-phenylglycine + hydroxylamine
-
-
-
?
(R)-2-phenylglycine amide + H2O
(R)-2-phenylglycine + hydroxylamine
-
-
-
?
(R)-2-phenylglycine amide + H2O
(R)-2-phenylglycine + hydroxylamine
-
-
-
?
(R)-2-phenylglycine methyl ester + H2O
(R)-2-phenylglycine + methanol
-
-
-
?
(R)-2-phenylglycine methyl ester + H2O
(R)-2-phenylglycine + methanol
-
-
-
?
(R)-2-phenylglycine methyl ester + H2O
(R)-2-phenylglycine + methanol
-
-
-
?
(R)-2-phenylglycine methyl ester + H2O
(R)-2-phenylglycine + methanol
-
-
-
?
2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O
5-amino-2-nitrobenzoic acid + phenoxyacetate
-
-
-
?
2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O
5-amino-2-nitrobenzoic acid + phenoxyacetate
-
-
-
?
2-nitro-5-(phenoxyacetamido)-benzoic acid + H2O
5-amino-2-nitrobenzoic acid + phenoxyacetate
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]-benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]-benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
?
2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
?
3-nitro-6-phenylacetaminobenzoic acid + H2O
?
-
-
-
-
?
3-nitro-6-phenylacetaminobenzoic acid + H2O
?
-
-
-
-
?
4-hydroxyphenylacetamide + 6-aminopenicillanic acid
?
-
-
-
r
4-hydroxyphenylacetamide + 6-aminopenicillanic acid
?
-
-
-
r
6-aminopenicillanate + phenylacetic acid
penicillin G + H2O
-
-
-
r
6-aminopenicillanate + phenylacetic acid
penicillin G + H2O
synthesis of penicillin G by enzyme is significantly better than by Escherichia coli enzyme
-
-
r
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
-
?
6-nitro-3-(phenylacetamido)-benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetate
-
-
-
?
6-nitro-3-(phenylacetamido)benzoic acid + H2O
?
-
-
-
-
?
6-nitro-3-(phenylacetamido)benzoic acid + H2O
?
-
-
-
?
6-nitro-3-phenylacetamide benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
-
-
-
?
6-nitro-3-phenylacetamide benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
-
-
-
-
?
6-nitro-3-phenylacetamido-benzoic acid + H2O
?
-
-
-
?
6-nitro-3-phenylacetamido-benzoic acid + H2O
?
-
-
-
?
6-nitro-3-phenylacetamidobenzoic acid + H2O
?
-
-
-
?
6-nitro-3-phenylacetamidobenzoic acid + H2O
?
-
-
-
?
6-nitro-3-[(phenylacetyl)amino]benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
-
-
-
?
6-nitro-3-[(phenylacetyl)amino]benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
-
-
-
-
?
6-nitro-3-[(phenylacetyl)amino]benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
-
-
-
r
6-nitro-3-[(phenylacetyl)amino]benzoic acid + H2O
3-amino-6-nitrobenzoic acid + phenylacetic acid
-
-
-
r
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
-
r
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
?
amoxillin + H2O
D-4-hydroxyphenylglycine + 6-aminopenicillanic acid
-
-
-
r
amoxillin + H2O
D-4-hydroxyphenylglycine + 6-aminopenicillanic acid
-
-
-
r
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
?
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
-
r
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
r
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
-
-
-
r
ampicillin + H2O
6-aminopenicillanic acid + (R)-2-phenylglycine
-
-
-
-
?
ampicillin + H2O
6-aminopenicillanic acid + (R)-2-phenylglycine
Pseudomonas melanogenum
-
-
-
r
ampicillin + H2O
6-aminopenicillanic acid + (R)-2-phenylglycine
-
-
-
?
ampicillin + H2O
?
-
-
-
?
ampicillin + H2O
?
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
highly specific
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
complete hydrolysis at low substrate concentrations
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
highly specific
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
complete hydrolysis at low substrate concentrations
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
higher activity of enzyme immobilised on the amino support suggests that interactions occurring between the amino carrier and the glycan favours a more correct orientation of the protein making it accessible to substrates
-
-
?
cefadroxil + H2O
?
-
-
-
r
cefadroxil + H2O
?
-
-
-
r
cephalexin + H2O
7-amino-3-methyl-8-oxo-5-thia-1-aza-bicyclo[4.2.0]oct-2-ene-2-carboxylic acid + D-phenylglycine
Pseudomonas melanogenum
-
-
-
-
?
cephalexin + H2O
7-amino-3-methyl-8-oxo-5-thia-1-aza-bicyclo[4.2.0]oct-2-ene-2-carboxylic acid + D-phenylglycine
-
-
-
?
cephalexin + H2O
7-aminodesacetoxycephalosporanic acid + D-phenylglycine
-
-
-
-
?
cephalexin + H2O
7-aminodesacetoxycephalosporanic acid + D-phenylglycine
-
-
-
-
?
cephalexin + H2O
7-aminodesacetoxycephalosporanic acid + D-phenylglycine
-
-
-
r
cephalexin + H2O
7-aminodesacetoxycephalosporanic acid + D-phenylglycine
-
-
-
r
cephaloridine + H2O
(6R,7R)-7-amino-8-oxo-3-[(pyridin-1-ium-1-yl)methyl]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + (thiophen-2-yl)acetic acid
-
-
-
-
?
cephaloridine + H2O
(6R,7R)-7-amino-8-oxo-3-[(pyridin-1-ium-1-yl)methyl]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + (thiophen-2-yl)acetic acid
-
-
-
-
?
cephalosporin + H2O
7-aminocephalosporanic acid + an amino acid
-
-
-
?
cephalosporin + H2O
7-aminocephalosporanic acid + an amino acid
-
-
-
-
?
cephalothin + H2O
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (thiophen-2-yl)acetic acid
-
-
-
-
?
cephalothin + H2O
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (thiophen-2-yl)acetic acid
-
-
-
-
?
cephalothin + H2O
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (thiophen-2-yl)acetic acid
-
-
-
-
?
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
r
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
-
-
-
r
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxicillin + NH3
-
-
-
-
r
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxicillin + NH3
-
-
-
r
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxicillin + NH3
-
-
-
r
D-hydroxyphenylglycine methyl ester + H2O
?
-
-
-
?
D-hydroxyphenylglycine methyl ester + H2O
?
-
-
-
?
D-phenylglycine amide + 6-aminopenicillanic acid
ampicillin + NH3
-
-
-
-
r
D-phenylglycine amide + 6-aminopenicillanic acid
ampicillin + NH3
-
-
-
r
D-phenylglycine amide + 6-aminopenicillanic acid
ampicillin + NH3
-
-
-
r
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
-
kinetically controlled synthesis
-
-
r
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
-
-
-
-
r
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
-
kinetically controlled synthesis
-
-
r
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
-
kinetically controlled synthesis
-
-
r
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
-
kinetically controlled synthesis
-
-
r
N-phenylacetyl-alpha-homophenylalanine + H2O
homophenylalanine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 80
-
-
?
N-phenylacetyl-alpha-homophenylalanine + H2O
homophenylalanine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 80
-
-
?
N-phenylacetyl-alpha-isoleucine + H2O
isoleucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 80
-
-
?
N-phenylacetyl-alpha-isoleucine + H2O
isoleucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 80
-
-
?
N-phenylacetyl-alpha-leucine + H2O
leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 80
-
-
?
N-phenylacetyl-alpha-leucine + H2O
leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 80
-
-
?
N-phenylacetyl-alpha-phenylalanine + H2O
phenylalanine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 90
-
-
?
N-phenylacetyl-alpha-phenylalanine + H2O
phenylalanine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 90
-
-
?
N-phenylacetyl-alpha-tert-leucine + H2O
tert-leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 105
-
-
?
N-phenylacetyl-alpha-tert-leucine + H2O
tert-leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 75
-
-
?
N-phenylacetyl-beta-homoleucine + H2O
beta-homoleucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 85
-
-
?
N-phenylacetyl-beta-homoleucine + H2O
beta-homoleucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 55
-
-
?
N-phenylacetyl-beta-leucine + H2O
beta-leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 68
-
-
?
N-phenylacetyl-beta-leucine + H2O
beta-leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 60
-
-
?
N2-phenylacetyl-2'-deoxyguanosine + H2O
phenylacetic acid + 2'-deoxyguanosine
-
-
-
?
N2-phenylacetyl-2'-deoxyguanosine + H2O
phenylacetic acid + 2'-deoxyguanosine
-
-
-
?
N6-phenylacetyl-2'-deoxyadenosine + H2O
phenylacetic acid + 2'-deoxyadenosine
-
-
-
?
N6-phenylacetyl-2'-deoxyadenosine + H2O
phenylacetic acid + 2'-deoxyadenosine
-
-
-
?
penicillin dihydroF + H2O
6-aminopenicillanic acid + hexanoic acid
-
-
-
-
?
penicillin dihydroF + H2O
6-aminopenicillanic acid + hexanoic acid
-
-
-
?
penicillin dihydroF + H2O
6-aminopenicillanic acid + hexanoic acid
-
-
-
?
penicillin F + H2O
6-aminopenicillanic acid + (3E)-hex-3-enoic acid
-
-
-
-
?
penicillin F + H2O
6-aminopenicillanic acid + (3E)-hex-3-enoic acid
-
-
-
?
penicillin F + H2O
6-aminopenicillanic acid + (3E)-hex-3-enoic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
a tryptophan residue is important for binding substrate penicillin G
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
-
-
-
r
penicillin G + H2O
6-aminopenicillanic acid + phenyl acetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenyl acetic acid
penicillin G acylase is a type II penicillin acylase
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenyl acetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
r
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
r
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
r
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
enzyme specific for penicillin G
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
function in nature not fully understood, possibly functions to degrade phenylacetylated compounds in order to generate phenylacetic acid which can be used as carbon source
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
r
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
?
penicillin G + H2O
phenyl acetic acid + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenyl acetic acid + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
penicillin G acylases preferentially hydrolyze penicillin G, i.e. benzylpenicillin
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetate + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
product detection by reaction with substrate 6-nitro-3-(phenylacetamido)benzoic acid
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
detection of product 6-aminopenicillanate by reaction with p-dimethylaminobenzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
product detection by p-dimethylamine benzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
product detection by p-dimethylamine benzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
detection of product 6-aminopenicillanate by reaction with p-dimethylaminobenzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
hydrolysis of penicillin G to obtain 6-aminopenicillanate in a batch reactor
detection of product 6-aminopenicillanate by reaction with p-dimethylaminobenzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
hydrolysis of penicillin G to obtain 6-aminopenicillanate in a batch reactor
detection of product 6-aminopenicillanate by reaction with p-dimethylaminobenzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
detection by reaction with p-dimethyl-aminobenzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
product detection by p-dimethylamine benzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
catalysis of the reverse reaction at low pH or low water activity
-
-
r
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
product detection by p-dimethylamine benzaldehyde
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanic acid
-
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanic acid
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanic acid
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanic acid
-
-
-
?
penicillin K + H2O
octanoic acid + 6-aminopenicillanate
-
-
-
?
penicillin K + H2O
octanoic acid + 6-aminopenicillanate
-
-
-
?
penicillin K + H2O
octanoic acid + 6-aminopenicillanate
-
-
-
?
penicillin K + H2O
octanoic acid + 6-aminopenicillanate
preferred substrate for the wild-type enzyme
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
the enzyme is highly specific towards penicillin V
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
penicillin G: negligible activity, ampicillin or amoxicillin: no activity
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
poor substrate
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
poor substrate
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
substrate of soluble and immobilized enzyme
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
-
?
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
-
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
specific for penicillin V
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
involvement of serine and tryptophan in the enzyme activity
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
?
penicillin V + H2O
phenoxyacetate + 6-aminopenicillinate
-
-
-
?
penicillin-G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
penicillin-G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
phenylacetamide + 6-aminopenicillanic acid
?
-
-
-
r
phenylacetamide + 6-aminopenicillanic acid
?
-
-
-
r
phenylacetamide + H2O
?
-
-
-
-
?
phenylacetamide + H2O
?
-
-
-
-
?
phenylacetamide + H2O
?
-
poor substrate
-
-
?
phenylacetamide + H2O
?
-
poor substrate
-
-
?
phenylacetic acid + 6-aminopenicillanic acid
penicillin G
-
-
-
r
phenylacetic acid + 6-aminopenicillanic acid
penicillin G
-
-
-
r
phenylacetylglycine + 6-aminopenicillanic acid
penicillin G + glycine
-
-
-
r
phenylacetylglycine + 6-aminopenicillanic acid
penicillin G + glycine
-
-
-
r
additional information
?
-
-
no activity with cefaclor, cephalexin, ampicillin, dicloxacillin or cephalosporin G
-
-
?
additional information
?
-
-
substrate specificity with phenylacetyl p-substituted anilides, overview
-
-
?
additional information
?
-
-
no activity in hydrolysis of conjugated bile salts
-
-
?
additional information
?
-
substrate specificity, overview. No activity with ampicillin, amoxicillin, or cephalosporin. Penicillin G is a poor substrate
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with ampicillin, amoxicillin, or cephalosporin. Penicillin G is a poor substrate
-
-
?
additional information
?
-
-
overview on best substrates for similar organisms
-
-
?
additional information
?
-
-
intracellular proteolysis in the cytoplasm is one of the important steps that limit the yield of active penicillin amidase from the translational product pre-pro-peniciliin amidase. Glucose and temperature are important parameters, determining the degradation rate of the proteolytically sensitive pre-pro-penicillin amidase
-
?
additional information
?
-
-
penicillin acylase is able to both hydrolyze and synthesize beta-lactam antibiotics
-
-
?
additional information
?
-
-
other natural penicillins
-
-
?
additional information
?
-
-
overview on best substrates for similar organisms
-
-
?
additional information
?
-
-
autoproteolytic processing of the alpha and beta subunit
-
-
?
additional information
?
-
-
no activity with cephapirin, cefotaximen cephalosporin, and penicillin N
-
-
?
additional information
?
-
-
no activity with n-heptylpenicillin, 2-(phenylthio)-ethylpenicillin, dimethoxyphenylpenicillin, and 5-methyl-3-phenyl-4-isoxazolylpenicillin
-
-
?
additional information
?
-
-
no activity with n-heptylpenicillin, 2-(phenylthio)-ethylpenicillin, dimethoxyphenylpenicillin, and 5-methyl-3-phenyl-4-isoxazolylpenicillin
-
-
?
additional information
?
-
Pseudomonas melanogenum
-
other natural penicillins
-
-
?
additional information
?
-
the acylase shows a marked preference for penicillin K over penicillin G, substrate specificity, overview
-
-
?
additional information
?
-
-
the acylase shows a marked preference for penicillin K over penicillin G, substrate specificity, overview
-
-
?
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2.5
2-benzoxazolon-3-yl-acetic acid methyl ester
-
pH 6.8, 25°C
0.63
2-nitro-5-(phenoxyacetamido)-benzoic acid
pH 6.6, 40°C
1.6
2-nitro-5-phenoxyacetamide benzoic acid
-
0.081
2-nitro-5-phenylacetamidobenzoic acid
-
pH 7.5, 25°C
0.00614 - 0.03
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
0.0005 - 30.39
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
0.147
2-phenyl-N-(4-sulfamoylphenyl)acetamide
-
pH 7.0, 25°C
0.00063
2-phenylacetamidobenzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.0004
3-phenylacetamidobenzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.027 - 0.114
4-Hydroxyphenylacetamide
0.031
4-nitrophenyl acetate
-
-
0.0003
4-phenylacetamidobenzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.07 - 0.23
5-nitro-3-[(phenylacetyl)amino]benzoic acid
0.0083 - 0.0197
6-nitro-3-(phenylacetamido)-benzoic acid
0.0176
6-nitro-3-phenylacetamide benzoic acid
-
pH 7.5, 37°C
0.012 - 0.02
6-nitro-3-phenylacetamidobenzoic acid
0.000015 - 0.027
6-nitro-3-[(phenylacetyl)amino]benzoic acid
0.01
7-phenylacetamidodeacetoxycephalosporanic acid
-
-
0.399 - 41.26
amoxicillin
0.105
amoxycillin
pH 7.4, 37°C, recombinant enzyme
0.0031 - 4.5
benzylpenicillin
2
benzylpenicilloic acid
-
-
0.0519
carbenicillin
pH 7.4, 37°C, recombinant enzyme
1.79
cephadrine
Pseudomonas melanogenum
-
-
1.96
cephaloglycin
Pseudomonas melanogenum
-
-
0.0164 - 0.1
cephaloridine
0.0156 - 0.042
cephalothin
3.2
D-(-)-alpha-aminophenylacetic acid p-nitroanilide
-
-
0.646 - 1.3
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid
9.1 - 12.2
D-4-hydroxyphenylglycine amide
1.6723 - 51.15
D-hydroxyphenylglycine methyl ester
-
2 - 30
D-phenylglycine amide
0.045
ethyl 2-phenylacetate
-
-
-
0.153
ethyl 4-[(phenylacetyl)amino] benzoate
-
pH 7.0, 25°C
0.137
N,2-diphenylacetamide
-
pH 7.0, 25°C
0.23
N-(4-acetylphenyl)-2-phenylacetamide
-
pH 7.0, 25°C
0.171
N-(4-bromophenyl)-2-phenylacetamide
-
pH 7.0, 25°C
0.16
N-(4-cyanophenyl)-2-phenylacetamide
-
pH 7.0, 25°C
0.162
N-(4-methoxyphenyl)-2-phenylacetamide
-
pH 7.0, 25°C
0.121
N-(4-methylphenyl)-2-phenylacetamide
-
pH 7.0, 25°C
0.095
N-(4-nitrophenyl)-2-phenylacetamide
-
pH 7.0, 25°C
0.00051
N-(5-nitro-2-pyridyl)-phenylacetamide
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.159
N-[4-(methylsulfonyl)phenyl]-2-phenylacetamide
-
pH 7.0, 25°C
0.8
N2-phenylacetyl-2'-deoxyguanosine
-
pH 7.8, 25°C
0.46
N6-phenylacetyl-2'-deoxyadenosine
-
pH 7.8, 25°C
0.82 - 5.6
penicillin dihydroF
0.00001 - 164
penicillin G
0.0002 - 0.156
phenylacetamide
0.0004
phenylacetate 4-nitroanilide
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.097
phenylacetate p-nitroanilide
-
-
0.0002
phenylacetyl-2-naphthylamide
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.4
phenylacetyl-3-aminobenzoic acid
-
-
0.18
phenylacetyl-4-aminobenzoic acid
-
-
0.000012
phenylacetyl-7-amido-4-methylcoumarin
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.95
phenylacetyl-anthranilic acid
-
-
5.2
phenylacetyl-Gly
-
pH 7.8, 25°C
0.67
phenylacetylaspartame
-
pH 7.8, 25°C
0.08
phenylacetylglycine
-
-
additional information
additional information
-
0.00614
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
-
pH 7.0, 25°C, mutant N241G
0.0102
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
-
pH 7.0, 25°C, mutant N241S
0.03
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
-
pH 7.0, 25°C
0.0005
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
alphaF146Y mutant protein, pH 7.5, 25°C
0.015
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C
0.026
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
wild type protein, pH 7.5, 25°C
0.098
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
betaF24A mutant protein, pH 7.5, 25°C
0.116
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
alphaF146A mutant protein, pH 7.5, 25°C
0.272
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
alphaF146Q mutant protein, pH 7.5, 25°C
0.386
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
alphaF146R mutant protein, pH 7.5, 25°C
0.551
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
betaF24S mutant protein, pH 7.5, 25°C
0.797
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
betaF24P mutant protein, pH 7.5, 25°C
0.9919
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, soluble enzyme
7.9
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates
30.39
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, cross-linked enzyme aggregates
0.027
4-Hydroxyphenylacetamide
pH 7.0, 30°C
0.114
4-Hydroxyphenylacetamide
pH 7.0, 30°C
0.07
5-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 7.5, 25°C, native enzyme
0.14
5-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 7.5, 25°C, fresh immobilized cross-linked enzyme aggregates
0.23
5-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 7.5, 25°C, mature immobilized cross-linked enzyme aggregates
0.0083
6-nitro-3-(phenylacetamido)-benzoic acid
pH 7.4, 37°C, recombinant enzyme
0.0197
6-nitro-3-(phenylacetamido)-benzoic acid
-
pH and temperature not specified in the publication
0.012
6-nitro-3-phenylacetamidobenzoic acid
-
pH 7.5, 25°C, enzyme form PA5.3
0.017
6-nitro-3-phenylacetamidobenzoic acid
-
pH 7.5, 25°C, enzyme form PA5.5
0.02
6-nitro-3-phenylacetamidobenzoic acid
-
pH 7.5, 25°C
0.000015
6-nitro-3-[(phenylacetyl)amino]benzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.004
6-nitro-3-[(phenylacetyl)amino]benzoic acid
pH 7.0, 30°C
0.027
6-nitro-3-[(phenylacetyl)amino]benzoic acid
pH 8.0, 37°C
0.399
amoxicillin
pH 7.0, 30°C
1.007
amoxicillin
pH 7.0, 30°C, soluble enzyme
1.07
amoxicillin
pH 7.0, 30°C
7.31
amoxicillin
pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates
41.26
amoxicillin
pH 7.0, 30°C, cross-linked enzyme aggregates
0.0944
ampicillin
pH 7.4, 37°C, recombinant enzyme
0.575
ampicillin
pH 7.0, 30°C
1.9
ampicillin
-
mutant alphaR145L
2.5
ampicillin
pH 7.0, 30°C
3.6
ampicillin
-
wild-type enzyme
4.34
ampicillin
Pseudomonas melanogenum
-
-
4.6
ampicillin
-
mutant alphaR145S
5.2
ampicillin
-
mutant alphaR145G
0.0031
benzylpenicillin
-
-
0.0046
benzylpenicillin
-
-
0.005
benzylpenicillin
-
pH 7.5, 25°C
0.0065
benzylpenicillin
-
pH 7.5, 25°C, mutant enzyme T206G/S213G/T219G
0.007
benzylpenicillin
-
pH 7.5, 25°C, mutant enzyme T206G//S213G
0.008
benzylpenicillin
-
pH 7.5, 25°C, enzyme form PA5..5 and PA5.3
0.008
benzylpenicillin
-
pH 7.5, 25°C, mutant enzyme T206G and wild-type enzyme
0.01
benzylpenicillin
-
pH 7.5, 25°C
0.016
benzylpenicillin
-
pH 7.5, 40°C
0.018
benzylpenicillin
-
pH 7.5, 25°C
0.061
benzylpenicillin
-
pH 7.5, 40°C, presence of 50 mM 2,3-butanedione
0.065
benzylpenicillin
-
pH 7.5, 40°C, presence of 10 mM phenylglyoxal
0.67
benzylpenicillin
-
-
0.8
benzylpenicillin
-
immobilized enzyme
4.5
benzylpenicillin
-
37°C, pH 8.7
0.284
cefadroxil
pH 7.0, 30°C
0.646
cefadroxil
pH 7.0, 30°C
0.0255
cephalexin
pH 7.4, 37°C, recombinant enzyme
1.3
cephalexin
pH 7.0, 30°C
1.5
cephalexin
pH 7.0, 30°C
1.61
cephalexin
Pseudomonas melanogenum
-
-
0.0164
cephaloridine
pH 7.4, 37°C, recombinant enzyme
0.0156
cephalothin
pH 7.4, 37°C, recombinant enzyme
0.646
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid
pH 7.0, 30°C
1.3
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid
pH 7.0, 30°C
9.1
D-4-hydroxyphenylglycine amide
pH 7.0, 30°C
12.2
D-4-hydroxyphenylglycine amide
pH 7.0, 30°C
1.6723
D-hydroxyphenylglycine methyl ester
pH 7.0, 30°C, soluble enzyme
-
11.74
D-hydroxyphenylglycine methyl ester
pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates
-
51.15
D-hydroxyphenylglycine methyl ester
pH 7.0, 30°C, cross-linked enzyme aggregates
-
2 - 3
D-phenylglycine amide
-
mutant alphaR145G
9.1
D-phenylglycine amide
-
mutant alphaR145L
12
D-phenylglycine amide
pH 7.0, 30°C
13
D-phenylglycine amide
-
mutant alphaR145S
27
D-phenylglycine amide
-
wild-type enzyme
30
D-phenylglycine amide
pH 7.0, 30°C
0.82
penicillin dihydroF
pH 8.0, 40°C recombinant enzyme
5.6
penicillin dihydroF
-
pH 8.0, 45°C
1.39
penicillin F
pH 8.0, 40°C recombinant enzyme
15.1
penicillin F
-
pH 8.0, 45°C
0.00001
penicillin G
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.0046
penicillin G
pH 7.4, 37°C, recombinant enzyme
0.0089
penicillin G
pH 8.0, 37°C
0.012
penicillin G
pH 7.0, 30°C
0.013
penicillin G
pH 7.0, 30°C
0.016
penicillin G
-
unmodified enzyme
0.051
penicillin G
-
enzyme modified with 2-hydroxy 5-nitrobenzylbromide
0.054
penicillin G
-
enzyme modified with N-bromosuccinamide
0.42
penicillin G
pH and temperature not specified in the publication
1.83
penicillin G
pH and temperature not specified in the publication
2.7
penicillin G
pH 7.5, 50°C
3
penicillin G
-
pH 8.0, 40°C
4.22
penicillin G
-
immobilized enzyme
13.4
penicillin G
pH 5.5, 65°C, recombinant mutant L24F
15.5
penicillin G
pH 5.5, 65°C, recombinant mutant L188F
17.8
penicillin G
pH 5.5, 65°C, recombinant mutant S189F
19
penicillin G
-
pH 7.8, 25°C
19.5
penicillin G
-
pH 7.0, 40°C, free enzyme
36.5
penicillin G
pH 5.5, 65°C, recombinant mutant I57F
37.6
penicillin G
pH 5.5, 65°C, recombinant mutant L24F/I57F
43.3
penicillin G
pH 5.5, 65°C, recombinant mutant L188F/S189F
44.4
penicillin G
pH 5.5, 65°C, recombinant mutant L188F/L24F/I57F
47.4
penicillin G
-
pH 7.0, 40°C, immobilized enzyme
56.19
penicillin G
-
soluble enzyme, pH and temperature not specified in the publication
58.18
penicillin G
pH 8.0, 40°C recombinant enzyme
64.84
penicillin G
-
enzyme immobilized on alginate beads, pH and temperature not specified in the publication
87.08
penicillin G
-
enzyme immobilized on alginate/chitosan hybrid beads, pH and temperature not specified in the publication
155.8
penicillin G
-
pH 8.0, 45°C
164
penicillin G
pH 5.5, 65°C, recombinant wild-type enzyme
0.05
penicillin K
pH 5.5, 65°C, recombinant mutant L24F/I57F
0.1
penicillin K
pH 5.5, 65°C, recombinant mutants L188F and S189F
0.12
penicillin K
pH 5.5, 65°C, recombinant mutant L24F
0.14
penicillin K
pH 8.0, 40°C recombinant enzyme
0.15
penicillin K
pH 5.5, 65°C, recombinant mutant L188F/L24F/I57F
0.27
penicillin K
pH 5.5, 65°C, recombinant mutant I57F
0.32
penicillin K
pH 5.5, 65°C, recombinant wild-type enzyme
1
penicillin K
-
pH 8.0, 45°C
0.0393
Penicillin V
pH 7.4, 37°C, recombinant enzyme
3.68
Penicillin V
pH 8.0, 40°C recombinant enzyme
15.4
Penicillin V
-
pH 8.0, 45°C
17.1
Penicillin V
-
immobilized enzyme
21.95
Penicillin V
pH 6.0, 37°C, wild-type enzyme
26.39
Penicillin V
pH 6.0, 37°C, mutant enzyme T63S/S110C/N198Y
40
Penicillin V
pH 6.6, 40°C
0.0002
phenylacetamide
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.03
phenylacetamide
pH 7.0, 30°C
0.156
phenylacetamide
pH 7.0, 30°C
additional information
additional information
-
further values of mutants
-
additional information
additional information
-
temperature dependence of Km-value for (R)- and (S)p-hydroxyphenylglycineamide
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics, overview
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
MichaelisMenten kinetics
-
additional information
additional information
-
MichaelisMenten kinetics
-
additional information
additional information
-
kinetic results on the hydrolysis of a series of 4-substituted anilides catalyzed by penicillin G acylase from Alcaligenes faecalis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.2
(R) -2-(4-hydroxyphenyl)glycine amide
-
-
1.01 - 6.08
(S)-N-acetylphenylglycine
0.1
2-benzoxazolon-3-yl-acetic acid methyl ester
-
pH 6.8, 25°C
106.4
2-nitro-5-phenoxyacetamide benzoic acid
-
0.204 - 15
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
15.7 - 145.3
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
40.03
2-phenyl-N-(4-sulfamoylphenyl)acetamide
-
pH 7.0, 25°C
2.3
2-phenylacetamidobenzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
2.5
3-phenylacetamidobenzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
29 - 47
4-Hydroxyphenylacetamide
170
4-nitrophenyl acetate
-
-
3
4-phenylacetamidobenzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
0.9 - 1.2
5-nitro-3-[(phenylacetyl)amino]benzoic acid
58.3
6-nitro-3-(phenylacetamido)-benzoic acid
pH 7.4, 37°C, recombinant enzyme
20 - 82
6-nitro-3-phenylacetamidobenzoic acid
16 - 68.8
6-nitro-3-[(phenylacetyl)amino]benzoic acid
50
7-phenylacetamidoacetoxycephalosporanic acid
-
-
14.67 - 142.3
amoxicillin
56.2
amoxycillin
pH 7.4, 37°C, recombinant enzyme
21 - 190
benzylpenicillin
40
benzylpenicilloic acid
-
-
63.7
carbenicillin
pH 7.4, 37°C, recombinant enzyme
0.54
D-(-)-alpha-aminophenylacetic acid 4-nitroanilide
-
-
12 - 14
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid
2 - 16
D-4-hydroxyphenylglycine amide
11.61 - 102.6
D-hydroxyphenylglycine methyl ester
-
2.7 - 57
D-phenylglycine amide
170
ethyl 2-phenylacetate
-
-
-
41.05
ethyl 4-[(phenylacetyl)amino] benzoate
-
pH 7.0, 25°C
49.17
N,2-diphenylacetamide
-
pH 7.0, 25°C
35.94
N-(4-acetylphenyl)-2-phenylacetamide
-
pH 7.0, 25°C
43.07
N-(4-bromophenyl)-2-phenylacetamide
-
pH 7.0, 25°C
33.84
N-(4-cyanophenyl)-2-phenylacetamide
-
pH 7.0, 25°C
33.81
N-(4-methoxyphenyl)-2-phenylacetamide
-
pH 7.0, 25°C
37.93
N-(4-methylphenyl)-2-phenylacetamide
-
pH 7.0, 25°C
15.14
N-(4-nitrophenyl)-2-phenylacetamide
-
pH 7.0, 25°C
7.8
N-(5-nitro-2-pyridyl)-phenylacetamide
-
25°C, pH 7.0, 10% dimethylsulfoxide
12000
N-phenylacetyl-Glu
-
-
29.49
N-[4-(methylsulfonyl)phenyl]-2-phenylacetamide
-
pH 7.0, 25°C
18
N2-phenylacetyl-2'-deoxyguanosine
-
pH 7.8, 25°C
2
N6-phenylacetyl-2'-deoxyadenosine
-
pH 7.8, 25°C
4.2 - 14.75
penicillin dihydroF
0.32 - 35.58
penicillin K
6.38 - 270.8
Penicillin V
20 - 55
phenylacetate 4-nitroanilide
1.9
phenylacetyl-2-naphthylamide
-
25°C, pH 7.0, 10% dimethylsulfoxide
3.2
phenylacetyl-7-amido-4-methylcoumarin
-
25°C, pH 7.0, 10% dimethylsulfoxide
47
phenylacetyl-Gly
-
pH 7.8, 25°C
35
phenylacetylaspartame
-
pH 7.8, 25°C
additional information
additional information
-
temperature dependence of turnover-numer for R- and S-p-hydroxyphenylglycineamide
-
1.01
(S)-N-acetylphenylglycine
-
pH 7.5
6.08
(S)-N-acetylphenylglycine
-
pH 7.5
0.204
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
-
pH 7.0, 25°C, mutant N241S
0.354
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
-
pH 7.0, 25°C, mutant N241G
15
2-nitro-5-[(phenyl-acetyl)amino]benzoic acid
-
pH 7.0, 25°C, wild-type enzyme
15.7
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, cross-linked enzyme aggregates
17.6
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, soluble enzyme
18
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
145.3
2-nitro-5-[(phenylacetyl)amino]-benzoic acid
pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates
29
4-Hydroxyphenylacetamide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
47
4-Hydroxyphenylacetamide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
0.9
5-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 7.5, 25°C, fresh immobilized cross-linked enzyme aggregates
1
5-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 7.5, 25°C, mature immobilized cross-linked enzyme aggregates
1.2
5-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 7.5, 25°C, native enzyme
20
6-nitro-3-phenylacetamidobenzoic acid
-
pH 7.5, 25°C
77
6-nitro-3-phenylacetamidobenzoic acid
-
pH 7.5, 25°C, enzyme form PA5..5
82
6-nitro-3-phenylacetamidobenzoic acid
-
pH 7.5, 25°C, enzyme form PA5..3
16
6-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 10.0, 25°C, ionic strength 0.12 M
20
6-nitro-3-[(phenylacetyl)amino]benzoic acid
-
25°C, pH 7.0, 10% dimethylsulfoxide
24
6-nitro-3-[(phenylacetyl)amino]benzoic acid
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
26
6-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 9.1, 25°C, ionic strength 0.12 M
27
6-nitro-3-[(phenylacetyl)amino]benzoic acid
-
pH 8.0, 25°C, ionic strength 0.12 M
68.8
6-nitro-3-[(phenylacetyl)amino]benzoic acid
pH 8.0, 37°C
14.67
amoxicillin
pH 7.0, 30°C, cross-linked enzyme aggregates
15
amoxicillin
pH 7.0, 30°C
16.9
amoxicillin
pH 7.0, 30°C, soluble enzyme
17
amoxicillin
pH 7.0, 30°C
142.3
amoxicillin
pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates
11
ampicillin
-
-
14
ampicillin
-
mutant alphaR145S
16
ampicillin
pH 7.0, 30°C
20
ampicillin
-
mutant alphaR145L
23
ampicillin
-
mutant alphaR145G
25
ampicillin
pH 7.0, 30°C
37
ampicillin
-
wild-type enzyme
49.5
ampicillin
pH 7.4, 37°C, recombinant enzyme
21
benzylpenicillin
-
pH 7.5, 40°C, presence of 10 mM phenylglyoxal
27
benzylpenicillin
-
pH 7.5, 40°C, presence of 50 mM 2,3-butanedione
50
benzylpenicillin
-
pH 7.5, 25°C
56.5
benzylpenicillin
-
pH 7.5, 25°C
63
benzylpenicillin
-
pH 7.5, 40°C
75
benzylpenicillin
-
pH 7.5, 25°C, enzyme form PA5..5
80
benzylpenicillin
-
pH 7.5, 25°C, enzyme form PA5..3
80
benzylpenicillin
-
pH 7.5, 25°C, wild-type enzyme
120
benzylpenicillin
-
pH 7.5, 25°C, mutant enzyme T206G
140
benzylpenicillin
-
pH 7.5, 25°C, mutant enzyme T206G//S213G
190
benzylpenicillin
-
pH 7.5, 25°C, mutant enzyme T206G/S213G/T219G
13
cefadroxil
pH 7.0, 30°C
32
cefadroxil
pH 7.0, 30°C
20
cephalexin
pH 7.0, 30°C
29
cephalexin
pH 7.0, 30°C
34.2
cephalexin
pH 7.4, 37°C, recombinant enzyme
33
cephaloridine
-
-
66.9
cephaloridine
pH 7.4, 37°C, recombinant enzyme
25
cephalothin
-
-
78.3
cephalothin
pH 7.4, 37°C, recombinant enzyme
12
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
14
D-2-nitro-5-[(phenylacetyl)amino]benzoic acid
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
2 - 8
D-4-hydroxyphenylglycine amide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
16
D-4-hydroxyphenylglycine amide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
11.61
D-hydroxyphenylglycine methyl ester
pH 7.0, 30°C, soluble enzyme
-
11.73
D-hydroxyphenylglycine methyl ester
pH 7.0, 30°C, cross-linked enzyme aggregates
-
102.6
D-hydroxyphenylglycine methyl ester
pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates
-
2.7
D-phenylglycine amide
-
mutant alphaR145S
3 - 6
D-phenylglycine amide
-
wild-type enzyme
3.4
D-phenylglycine amide
-
mutant alphaR145G
6.8
D-phenylglycine amide
-
mutant alphaR145L
25
D-phenylglycine amide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
57
D-phenylglycine amide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
4.2
penicillin dihydroF
-
pH 8.0, 45°C
14.75
penicillin dihydroF
pH 8.0, 40°C recombinant enzyme
1.9
penicillin F
-
pH 8.0, 45°C
3.33
penicillin F
pH 8.0, 40°C recombinant enzyme
0.02
penicillin G
pH 5.5, 65°C, recombinant mutant L188F/S189F
0.13
penicillin G
pH 5.5, 65°C, recombinant mutant L188F/L24F/I57F
0.3
penicillin G
pH 5.5, 65°C, recombinant mutant L24F/I57F
0.44
penicillin G
pH 5.5, 65°C, recombinant mutant I57F
0.54
penicillin G
pH 5.5, 65°C, recombinant mutant L188F
0.65
penicillin G
pH 5.5, 65°C, recombinant mutant S189F
0.85
penicillin G
pH 5.5, 65°C, recombinant mutant L24F
1.56
penicillin G
pH 5.5, 65°C, recombinant wild-type enzyme
2.1
penicillin G
pH 8.0, 37°C
2.2
penicillin G
-
pH 8.0, 45°C
10.95
penicillin G
pH 8.0, 40°C recombinant enzyme
25
penicillin G
pH 7.0, 30°C
39
penicillin G
pH 7.0, 30°C
50
penicillin G
-
pH 7.8, 25°C
50
penicillin G
-
25°C, pH 7.0, 10% dimethylsulfoxide
63
penicillin G
-
unmodified enzyme, enzyme modified with N-bromosuccinamide or enzyme modified with 2-hydroxy 5-nitrobenzylbromide
64.2
penicillin G
pH 7.4, 37°C, recombinant enzyme
72.7
penicillin G
pH 8.0, 37°C
0.32
penicillin K
pH 5.5, 65°C, recombinant mutant L24F
0.36
penicillin K
pH 5.5, 65°C, recombinant mutant S189F
0.43
penicillin K
pH 5.5, 65°C, recombinant mutant L188F
0.75
penicillin K
pH 5.5, 65°C, recombinant mutant L24F/I57F
1.43
penicillin K
pH 5.5, 65°C, recombinant mutant L188F/L24F/I57F
4.91
penicillin K
pH 5.5, 65°C, recombinant mutant I57F
5.6
penicillin K
pH 5.5, 65°C, recombinant wild-type enzyme
33.3
penicillin K
-
pH 8.0, 45°C
35.58
penicillin K
pH 8.0, 40°C recombinant enzyme
6.38
Penicillin V
pH 6.0, 37°C, wild-type enzyme
48.4
Penicillin V
pH 7.4, 37°C, recombinant enzyme
70.3
Penicillin V
-
pH 8.0, 45°C
77.92
Penicillin V
pH 8.0, 40°C recombinant enzyme
94.59
Penicillin V
pH 6.0, 37°C, mutant enzyme T63S/S110C/N198Y
23
phenylacetamide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
46
phenylacetamide
pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma
50
phenylacetamide
-
25°C, pH 7.0, 10% dimethylsulfoxide
20
phenylacetate 4-nitroanilide
-
25°C, pH 7.0, 10% dimethylsulfoxide
55
phenylacetate 4-nitroanilide
-
-
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Q3C/P751C
-
temperature optimum is three degrees higher than for wild-type. Half-life of mutant at 55°C is increased by 50%
T206G
-
specific activity of the mutant enzyme is 60% higher compared to the wild-type enzyme, pI is 5.5
T206G/G213G
-
mutant enzyme with 1.9fold increased specific activity compared to completely processed wild-type enzyme, mutation stabilizes the precursor form, pI value is 5.6
T206G/S213G
-
construction of a mutant with extended C-terminus of the A-chain comprising parts of the connecting linker peptide showing almost 2fold increased activity and 3fold higher specificity compared to the wild-type enzyme, overview
T206G/S213G/T219G
-
mutant enzyme with 2.3fold increased specific activity compared to completely processed wild-type enzyme
T206P
-
mutant undergoes normal proteolytic processing leading to a completely processed enzyme with pI 5.3
C1A
no activity, catalytic residue
C1S
no activity, catalytic residue
A149Q
activity is too low to measure thermal stability
A305D
mutation in beta-subunit. Half-life at 50°C is 1.6fold higher than wild-type value. Activity is about 60% of wild-type value
A545K
mutation in beta-subunit. Half-life at 50°C is about 80% of wild-type value. Activity is about 80% of wild-type value
A80R
mutation in alpha-subunit. Half-life at 50°C is 2.6fold higher than wild-type value. Activity is 1.6fold higher than wild-type value
A84P
mutation in beta-subunit. Half-life at 50°C is 1.3fold higher than wild-type value. Activity is identical to wild-type value
alphaF146A
mutant selective for (S)-ampicillin synthesis
alphaF146Q
mutant selective for (S)-ampicillin synthesis
alphaF146R
mutant selective for (S)-ampicillin synthesis
betaF24A/alphaF146Y
very low amidase activity
betaF24C
mutant selective for (R)-ampicillin synthesis
betaF24P
mutant selective for (R)-ampicillin synthesis
betaF24S
mutant selective for (R)-ampicillin synthesis
betaF24T
used as negative control because of the negative effect on synthetic and hydrolytic activities
betaF24T/alphaF146Y
used as negative control because of the negative effect on synthetic and hydrolytic activities
C290C
-
20% decrease in production of penicillin G acylase activity
D13K
-
mutation in beta-subunit, no change in enzyme stability or kinetic properties, but improved stability after immobilization on glyoxyl-agarose
E130T
mutation in alpha-subunit. Half-life at 50°C is about 60% of wild-type value. Activity is about 1.2fold higher than wild-type value
E272K
-
mutation in beta-subunit, no change in enzyme stability or kinetic properties, but improved stability after immobilization on glyoxyl-agarose
F146A
-
mutation in alpha-subunit. 99% of ampicillin synthesis activity compared to wild-type
F146C
-
mutation in alpha-subunit. 241% of ampicillin synthesis activity compared to wild-type
F146D
-
mutation in alpha-subunit. No ampicillin synthesis activity
F146E
-
mutation in alpha-subunit. 13% of ampicillin synthesis activity compared to wild-type
F146G
-
mutation in alpha-subunit. 61% of ampicillin synthesis activity compared to wild-type
F146H
-
mutation in alpha-subunit. 174% of ampicillin synthesis activity compared to wild-type
F146I
-
mutation in alpha-subunit. 135% of ampicillin synthesis activity compared to wild-type
F146K
-
mutation in alpha-subunit. 120% of ampicillin synthesis activity compared to wild-type
F146M
-
mutation in alpha-subunit. 85% of ampicillin synthesis activity compared to wild-type
F146N
-
mutation in alpha-subunit. 151% of ampicillin synthesis activity compared to wild-type
F146P
-
mutation in alpha-subunit. 112% of ampicillin synthesis activity compared to wild-type
F146Q
-
mutation in alpha-subunit. 114% of ampicillin synthesis activity compared to wild-type
F146R
-
mutation in alpha-subunit. 3% of ampicillin synthesis activity compared to wild-type
F146S
-
mutation in alpha-subunit. 238% of ampicillin synthesis activity compared to wild-type
F146T
-
mutation in alpha-subunit. 376% of ampicillin synthesis activity compared to wild-type
F146V
-
mutation in alpha-subunit. 153% of ampicillin synthesis activity compared to wild-type
F146Y/F24A
-
mutation F24Y in beta-, F146Y in alpha-subunit, increased affinity for Calpha-substituted substrates
F71C
-
mutation in B-subunit shows a 100fold increase in kcat/Km towards glutaryl-L-leucine
F71L
-
mutation in B-subunit shows a 100fold increase in kcat/Km towards glutaryl-L-leucine
H26G
activity is too low to measure thermal stability
K299H
-
mutant shows very low processing and 90% loss of activity
K299Q
-
mutant enzyme shows no processing
K299S
-
mutant enzyme shows no processing
L100E
mutation in beta-subunit. Half-life at 50°C is 1.2fold higher than wild-type value. Activity is about 50% of wild-type value
M90R
mutation in alpha-subunit. Half-life at 50°C is nearly identical to wild-type value. Activity is about 70% of wild-type value
N241G
-
site-directed mutagensis of subunit B residue, leads to reduced activity compared to the wild-type enzyme
N241S
-
site-directed mutagensis of subunit B residue, leads to reduced activity compared to the wild-type enzyme
N348D
mutation in beta-subunit. Half-life at 50°C is 1.5fold higher than wild-type value. Activity is nearly identical to wild-type value
Q118E
activity is too low to measure thermal stability
R145A
-
mutation in alpha-subunit. 154% of ampicillin synthesis activity compared to wild-type
R145C
-
mutation in alpha-subunit. 169% of ampicillin synthesis activity compared to wild-type
R145D
-
mutation in alpha-subunit. 15% of ampicillin synthesis activity compared to wild-type
R145E
-
mutation in alpha-subunit. 6% of ampicillin synthesis activity compared to wild-type
R145F
-
mutation in alpha-subunit. 131% of ampicillin synthesis activity compared to wild-type
R145G
-
mutation in alpha-subunit. 256% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor
R145H
-
mutation in alpha-subunit. 78% of ampicillin synthesis activity compared to wild-type
R145I
-
mutation in alpha-subunit. 120% of ampicillin synthesis activity compared to wild-type
R145K
-
mutation in alpha-subunit. 145% of ampicillin synthesis activity compared to wild-type
R145L
-
mutation in alpha-subunit. 237% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor
R145M
-
mutation in alpha-subunit. 129% of ampicillin synthesis activity compared to wild-type
R145N
-
mutation in alpha-subunit. 173% of ampicillin synthesis activity compared to wild-type
R145P
-
mutation in alpha-subunit. 137% of ampicillin synthesis activity compared to wild-type
R145Q
-
mutation in alpha-subunit. 158% of ampicillin synthesis activity compared to wild-type
R145S
-
mutation in alpha-subunit. 192% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor
R145T
-
mutation in alpha-subunit. 127% of ampicillin synthesis activity compared to wild-type
R145V
-
mutation in alpha-subunit. 127% of ampicillin synthesis activity compared to wild-type
R145W
-
mutation in alpha-subunit. 103% of ampicillin synthesis activity compared to wild-type
R145Y
-
mutation in alpha-subunit. 37% of ampicillin synthesis activity compared to wild-type
R276K
-
mutation in beta-subunit, no change in enzyme stability or kinetic properties, but improved stability after immobilization on glyoxyl-agarose
S374T
mutation in beta-subunit. Half-life at 50°C is about 90% of wild.type value. Activity about 50% of wild-type value
S9E
activity is too low to measure thermal stability
T121D
mutation in alpha-subunit. Half-life at 50°C is about 70% of wild-type value. Activity is about 40% of wild-type value
T150N
mutation in alpha-subunit. Half-life at 50°C is 1.5fold higher than wild-type value. Activity is about 50% of wild-type value
T263G
-
slowly processing mutant enzyme
T289C
-
production of penicillin G acylase activity is 92% improved
T289G
-
production of penicillin G acylase activity is 20% improved
T289S
-
production of penicillin G acylase activity is 85% improved
T311P/Q312A
mutation in beta-subunit. Half-life at 50°C is 2fold higher than wild-type value. Activity is about 90% of wild-type value
V184K
mutation in beta-subunit. Half-life at 50°C is about 60% of wild-type value. Activity is about 60% of wild-type value
V359L
mutation in beta-subunit. Half-life at 50°C is 1.4fold higher than wild-type value. Activity is about 60% of wild-type value
V400L
mutation in beta-subunit. Half-life at 50°C is 1.8fold higher than wild-type value. Activity is about 75% of wild-type value
V56R/T32Y
-
mutation of beta-subunit, plus F146Y in alpha-subunit, 2.3% of wild-type activity with substrate penicillin G, 460% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
V56R/T32Y/I177Y
-
mutation of beta-subunit, plus F146Y in alpha-subunit, 1.8% of wild-type activity with substrate penicillin G, 490% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
V56R/T32Y/I177Y/P49Q
-
mutation of beta-subunit, plus F146Y in alpha-subunit, 1.3% of wild-type activity with substrate penicillin G, 510% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
V56R/T32Y/I177Y/P49Q/W154Y
-
mutation of beta-subunit, plus F146Y in alpha-subunit, 1.2% of wild-type activity with substrate penicillin G, 600% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
V56R/T32Y/I177Y/P49Q/W154Y/F24L
-
mutation of beta-subunit, plus F146Y in alpha-subunit, 0.3% of wild-type activity with substrate penicillin G, 760% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
V97K
activity is too low to measure thermal stability
W25Y
mutation in alpha-subunit. Half-life at 50°C is 2.7fold higher than wild-type value. Activity is 1.4fold higher than wild-type value
K375N
-
destabilisation of transition state
M168V
-
highly decreased specificity constants
S1C
replacement of serine of the beta-subunit with cysteine results in a fully processed but inactive enzyme
S1G
the second mutant in which the N-terminal serine is replaced by glycine remains in the unprocessed and inactive form
C1A
-
no catalytic activity, precursor form pre-C1S is not processed
C1S
-
no catalytic activity, precursor form pre-C1S is not processed
N175A
-
no catalytic activity, about 50% of precursor form pre-N175A is processed
N198Y
the mutant enzyme shows 1.36fold higher specific activity compared to wild-type enzyme
N198Y/S110C
the mutant enzyme shows 2.26fold higher specific activity compared to wild-type enzyme
T63S
the mutant enzyme shows 11.14fold higher specific activity compared to wild-type enzyme
T63S/N198Y
the mutant enzyme shows 4.6fold higher specific activity compared to wild-type enzyme
T63S/S110C
the mutant enzyme shows 3.97fold higher specific activity compared to wild-type enzyme
T63S/S110C/N198Y
the mutant enzyme shows 12.4fold higher specific activity and 11.3fold higher catalytic efficiency compared to wild-type enzyme. The mutant enzyme has a potential for large-scale industrial application for 6-aminopenicillanic acid production
D22E
the specific activity is 10.9% compared to wild-type enzyme. Protein expression yields is 34 mg/ml compared to 262 mg/ml for the native enzyme
D22N
the specific activity is 5.1% compared to wild-type enzyme. Protein expression yields is 2.5 mg/ml compared to 262 mg/ml for the native enzyme
R19H
the specific activity is 6% compared to wild-type enzyme. Protein expression yields is 121 mg/ml compared to 262 mg/ml for the native enzyme
R215L
the specific activity is 7.4% compared to wild-type enzyme. Protein expression yields is 5.6 mg/ml compared to 262 mg/ml for the native enzyme
W23F
the specific activity is 4% compared to wild-type enzyme. Protein expression yields is 6.9 mg/ml compared to 262 mg/ml for the native enzyme
W23F/W87Y
the specific activity is 0.13% compared to wild-type enzyme. Protein expression yields is 3.3 mg/ml compared to 262 mg/ml for the native enzyme
W23I
the specific activity is 0.9% compared to wild-type enzyme. Protein expression yields is 7.1 mg/ml compared to 262 mg/ml for the native enzyme
W23I/W87N
the specific activity is 0.02% compared to wild-type enzyme. Protein expression yields is 3.6 mg/ml compared to 262 mg/ml for the native enzyme
W87N
the specific activity is 81.2% compared to wild-type enzyme. Protein expression yields is 196.8 mg/ml compared to 262 mg/ml for the native enzyme
W87Y
the specific activity is 1.5% compared to wild-type enzyme. Protein expression yields is 6.7 mg/ml compared to 262 mg/ml for the native enzyme
R19H
-
the specific activity is 6% compared to wild-type enzyme. Protein expression yields is 121 mg/ml compared to 262 mg/ml for the native enzyme
-
R215L
-
the specific activity is 7.4% compared to wild-type enzyme. Protein expression yields is 5.6 mg/ml compared to 262 mg/ml for the native enzyme
-
W23F
-
the specific activity is 4% compared to wild-type enzyme. Protein expression yields is 6.9 mg/ml compared to 262 mg/ml for the native enzyme
-
W87Y
-
the specific activity is 1.5% compared to wild-type enzyme. Protein expression yields is 6.7 mg/ml compared to 262 mg/ml for the native enzyme
-
F145A
-
alpha chain, no formation of cephalexin, no activity with nitrophenylacetylaminobenzoic acid
F145L
-
alpha chain, no formation of cephalexin, no activity with nitrophenylacetylaminobenzoic acid
F145Y
-
alpha chain, slightly increased formation of cephalexin, 32% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
K430A/K427A
-
mutation in beta-chain. Mutant shows a good stability to solvent and thermostability
V24F
-
beta chain, no effect on the formation of cephalexin, 11% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
Y144R
-
alpha chain, reduced formation of cephalexin, 72% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
Y144R/V24F
-
Y144R on alpha chain, V24F on beta chain, reduced formation of cephalexin, 4% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
N272D
mutation at beta-subunit results in a drastic decrease of activity
N272V
mutation at beta-subunit results in a drastic decrease of activity
S1A
mutation at beta-subunit results in an inactive enzyme
S1C
mutation at beta-subunit results in an inactive enzyme
S1D
mutation at beta-subunit results in an inactive enzyme
S1H
mutation at beta-subunit results in an inactive enzyme
S1K
mutation at beta-subunit results in an inactive enzyme
V70A
mutation at beta-subunit results in a drastic decrease of activity
V70D
mutation at beta-subunit results in a drastic decrease of activity
N272D
-
mutation at beta-subunit results in a drastic decrease of activity
-
S1A
-
mutation at beta-subunit results in an inactive enzyme
-
S1C
-
mutation at beta-subunit results in an inactive enzyme
-
V70A
-
mutation at beta-subunit results in a drastic decrease of activity
-
V70D
-
mutation at beta-subunit results in a drastic decrease of activity
-
I57F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G, Km for penicillin G is 4.5fold, while the catalytic efficiency remains at wild-type value
L188F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G, penicillin G binding is 10fold improved compared to the wild-type enzyme
L188R
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G
L188R/S189F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G
L24F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G, penicillin G binding is 12fold improved compared to the wild-type enzyme
L24F/I57F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G
L24F/I57F/L188F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G
L24F/I57F/L188R/S189F
site-directed mutagenesis, inactive mutant
S189F
site-directed mutagenesis, the substrate specificity of the mutant shifts from penicillin K to penicillin G, penicillin G binding is 9fold improved compared to the wild-type enzyme
alphaF146Y
bad catalyst for synthesis
alphaF146Y
mutant selective for (S)-ampicillin synthesis
betaF24A
mutant selective for (R)-ampicillin synthesis
betaF24A
reduced hydrolytic activity towards amides of phenylglycine
F146L
-
mutation in alpha-subunit,3fold increase in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile
F146L
-
mutation in alpha-subunit. 169% of ampicillin synthesis activity compared to wild-type
F146W
-
mutation in alpha-subunit, 40fold decrease in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile
F146W
-
mutation in alpha-subunit. 10% of ampicillin synthesis activity compared to wild-type
F146Y
-
alpha-subunit, increased affinity for Calpha-substituted substrates
F146Y
-
mutation in alpha-subunit, 40fold decrease in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile
F146Y
-
mutation in alpha-subunit. No ampicillin synthesis activity
F24A
-
beta-subunit, increased affinity for Calpha-substituted substrates, 20fold reduced affinity for phenylacetic acid
F24A
-
mutation in beta-subunit, 3fold increase in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile
F24A
-
mutation in the beta-subunit produces a protein with a higher synthesis/hydrolysis ratio, increased acylase activity, and more resistance to inhibition by phenyl acetic acid
F24A
-
suppressed hydrolysis rate of N-phenylacetyl-L-Gln and N-phenylacetyl-L-Glu, respectively, compared to wild-type enzyme
V56R
-
mutation of beta-subunit, 12% of wild-type activity with substrate penicillin G, 230% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
V56R
-
mutation of beta-subunit, plus F146Y in alpha-subunit, 5% of wild-type activity with substrate penicillin G, 280% of wild-type activity with cephalosporin acylase substrate glutaryl-7-aminocephalosporanic acid
S290G
site-directed mutagenesis of the internal proteolytic cleavage site of the pro-enzyme
S290G
-
site-directed mutagenesis of the internal proteolytic cleavage site of the pro-enzyme
-
K427A
-
mutation in beta-chain. Half-life is improved by 60% compared to wild-type enzyme
K427A
-
mutation in beta-chain. Mutant shows a great stability to organic solvents
K430A
-
mutation in beta-chain. Half-life is improved by 166% compared to wild-type enzyme
K430A
-
mutation in beta-chain. Mutant shows a good stability to solvent and thermostability
additional information
-
a cross-species penicillin G amidase gene coding for an alpha-peptide and a linker peptide from K. citrophila and a beta-peptide from Escherichia coli constructed and cloned in Escherichia coli. In comparison with the two wild-type enzymes the hybrid enzyme has a higher turnover-number for benzylpenicillin, ampicillin and 6-nitro-3-phenylacetamido-benzoic acid. The KM-values are between the values of the wild-type enzymes or close ro that of K. citrophila
additional information
-
addition of a tag of three lysine residues alternating with three glycines to C-terminus of enzyme results in improvement of the immobilization efficiency on glyoxyl agarose and the catalytic protperties of immobilized enzyme, but impairs posttranslational steps of overexpressed protein maturation
additional information
-
conjugation of Saccharomyces cerevisiae mannan with enzyme yielding neoglycoproteins containing 42 to 67% saccharides. Significant increase in half-life at 37°C and 50°C of both free enzyme and concanavalin A-linked enzyme
additional information
construction hybrids of the penicillin acylase-encoding genes from Eacherichia coli and Kluyvera cryocrescens, with additional point mutations. The hybrid enzymes display a 40-90% increase in the relative rate of acyl transfer to the beta-lactam nucleus during ampicillin synthesis. This increase is not accompanied by a reduction of synthetic activity. Similar improvements in acyl transfer are obtained for the synthesis of amoxicillin, cephalexin and cefadroxil making the new hybrid enzymes interesting candidates for the biocatalytic synthesis of several beta-lactam antibiotics
additional information
-
the mutant enzyme contains 85 exposed Glu-plus-Asp residues, while the native enzyme exposed in the surface only 77 acidic residues. Such an increase in the number of negative charges reduces the isoelectric point of the mutant enzyme from 6.4 to 4.3. The native enzyme does not become significantly immobilized on any of the three supports (DEAE and two supports coated with polyethyleneimine of different sizes), while the mutant enzyme becomes fully immobilized on them. The use of restrictive conditions during the enzyme adsorption on anionic exchangers (pH 5 and high ionic strength) further increases the strength of adsorption and the enzyme stability in the presence of organic solvents, suggesting that these conditions allow the penetration of the enzyme inside the polymeric beds, thus becoming fully covered with the polymer. After the enzyme inactivation, it can be desorbed to reuse the support
additional information
-
construction of a fusion protein, consisting of Pseudomonas Sec- or Tat-specific signal peptides, the elastase propeptide and the mature penicillin G acylase, termed a TatProPGA hybrid. the mature protein, expressed from a TatProPGA hybrid, is not only found in the extracellular medium and the periplasm, but also in the cytoplasm as assessed by comparison to the reporter beta-lactamase protein
additional information
-
directed evolution of penicillin acylase using phage display technology for extending its specificity. Fusion of the penicillin acylase to fd phage coat protein III and used pIII secretion signal sequence instead of penicillin acylase, which couples gene and enzyme on phage particle and can is useful for directed evolution of penicillin acylase. Penicillin acylase is functionally displayed on phage surface. Determination by site-directed mutagenesis of the effect of Ser B1 and Asn B241 variants on post-translational maturation of phage fused penicillin acylase, overview
additional information
-
effect of the degree of cross-linking on the properties of different cross-linked enzyme aggregates, CLEAs, of penicillin acylase, overview
additional information
-
immobilization of the enzyme, quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase under different conditions by confocal fluorescent microscopy, overview. Comparison of fresh aggregates and mature aggregates. The aggregate size might regulate the extent of covalent modification of the enzyme and thereby influence the catalytic properties of cross-linked enzyme aggregates
additional information
-
penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane, immobilized enzyme specific activity is 145 U/g, and a 2.4fold increase in activity compared to the free enzyme. The immobilized enzyme retains almost 50% activity after 107 days and 50 cycles of operation, method evaluation and enzyme stability, overview. Effect of different ionic molecules/compounds as ligands coupled to membrane on enzyme immobilization, best is Brilliant green
additional information
-
penicillin G acylase immobilization using highly porous cellulose-based polymeric membrane, immobilized enzyme specific activity is 145 U/g, and a 2.4fold increase in activity compared to the free enzyme. The immobilized enzyme retains almost 50% activity after 107 days and 50 cycles of operation, method evaluation and enzyme stability, overview. Effect of different ionic molecules/compounds as ligands coupled to membrane on enzyme immobilization, best is Brilliant green
-
additional information
-
a cross-species penicillin G amidase gene coding for an alpha-peptide and a linker peptide from Kluyvera citrophila and a beta-peptide from Escherichia coli constructed and cloned in Escherichia coli. In comparison with the two wild-type enzymes the hybrid enzyme has a higher turnover-number for benzylpenicillin, ampicillin and 6-nitro-3-phenylacetamido-benzoic acid. The Km-values are between the values of the wild-type enzymes or close ro that of Kluyvera citrophila
additional information
-
transversion mutation of thymine to guanine at position 1163 results in 90% and 50% of activity loss in penicillin G acylase activity on penicillin G and phenylacetyl-L-leucine respectively
additional information
-
leader peptide was replaced by the Bacillus megaterium LipA counterpart, changing the signal peptide increases the amount of secreted enzyme
additional information
-
immobilization of the enzyme on mesocellular silica foams from 0.1 M phosphate buffer, pH 7.0, the immobilized enzyme activity depends on molecular crowding and applied to catalysis in non-aqueous medium, addition of dextran, method optimization, using different enzyme preparations, organic solvents and mesocellular silica foams-dextran mixtures, overview
additional information
-
immobilization of the recombinant enzyme by covalent linking to epoxy-activated beads in homogenous distribution to avoid enzyme aggregate formation, and usage as biocatalyst. The immobilized enzyme shows altered optimal reaction conditions and enlarged substrate specificity, as well as increased thermal stability compared to the soluble enzyme, it can be recycled 30times in consecutive batch reactions, overview
additional information
substrate specificity change through engineering: generation of a set of enzyme variants containing between one and four amino acid replacements, with altered catalytic properties in the hydrolyses of penicillins K and G. The introduction of a single phenylalanine residue in position alpha188, alpha189, or beta24 improves the Km for penicillin G between 9 and 12fold, and the catalytic efficiency of these variants for penicillin G was improved up to 6.6fold
additional information
-
substrate specificity change through engineering: generation of a set of enzyme variants containing between one and four amino acid replacements, with altered catalytic properties in the hydrolyses of penicillins K and G. The introduction of a single phenylalanine residue in position alpha188, alpha189, or beta24 improves the Km for penicillin G between 9 and 12fold, and the catalytic efficiency of these variants for penicillin G was improved up to 6.6fold
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