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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-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-phenylacetamidobenzoic acid + H2O
phenylacetate + 2-aminobenzoic acid
-
-
-
-
?
2-thienylmethylpenicillin + H2O
6-aminopenicillanate + sulfo-(5-sulfothiophen-2-yl)-acetic acid
-
-
-
-
?
3-phenylacetamidobenzoic acid + H2O
phenylacetate + 3-aminobenzoic acid
-
-
-
-
?
4-hydroxyphenylacetamide + 6-aminopenicillanic acid
?
-
-
-
r
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
-
-
-
r
6-aminopenicillanic acid + p-hydroxyphenylglycine methyl ester
amoxicillin + methanol
-
-
-
-
?
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-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-aminocephalosporanic acid + (R)-mandelic acid
7-[(1-hydroxy-1-phenyl)-acetamido]-3-acetoxymethyl-D3-cephem-4-carboxylic acid
-
-
-
-
?
7-aminodeacetoxycephalosporanic acid + (R)-2-phenylglycine methylester
cephalexin + ?
-
-
-
-
?
7-aminodeacetoxycephalosporanic acid + 2-benzoxazolon-3-yl-acetic acid methyl ester
?
-
-
-
?
7-aminodeacetoxycephalosporanic acid + phenylacetic acid methyl ester
?
-
-
-
?
7-phenylacetamidoacetoxycephalosporanic acid + H2O
?
-
-
-
-
?
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
-
-
?
amoxicillin + H2O
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
-
-
-
r
amoxillin + H2O
D-4-hydroxyphenylglycine + 6-aminopenicillanic acid
-
-
-
r
ampicillin + H2O
(R)-2-phenylglycine + 6-aminopenicillanic acid
ampicillin + H2O
?
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
benzylpenicilloic acid + H2O
?
-
-
-
-
?
cefadroxil + H2O
?
-
-
-
r
cephalexin + H2O
7-aminodesacetoxycephalosporanic acid + D-phenylglycine
-
-
-
r
cephalexin + H2O
D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
-
-
-
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
-
-
-
-
?
cephalosporin + H2O
7-aminocephalosporanic acid + an amino acid
cephalosporin G + H2O
7-aminodeacetoxycephalosporanate + phenylacetic acid
-
-
-
-
r
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-(-)-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
-
-
-
r
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-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 + ?
-
-
-
?
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
-
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
glutarate + 7-aminocephalosporanic acid
-
-
-
-
?
hydroxyphenylglycineamide + 7-aminodeacetoxycephalosporanic acid
cefadroxil + NH3
-
-
-
-
?
isobutoxymethylpenicillin + H2O
6-aminopenicillanate + carbonic acid isopropyl ester
-
-
-
-
?
N-(5-nitro-2-pyridyl)-phenylacetamide + H2O
phenylacetate + 5-nitropyridin-2-amine
-
-
-
-
?
N-(phenylacetyl)glycine + H2O
phenylacetic acid + glycine
-
-
-
?
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-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-tert-leucine + H2O
tert-leucine + phenylacetate
experimentally determined E-value (enantioselectivity) towards racemic mixtures of alpha- and beta-amino acids: 75
-
-
?
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
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: 60
-
-
?
N-phenylacetyl-DL-leucine + H2O
?
-
-
-
-
?
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
-
-
-
-
?
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 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-G + H2O
6-aminopenicillanic acid + phenylacetic acid
-
-
-
-
?
phenylacetamide + 6-aminopenicillanic acid
?
-
-
-
r
phenylacetamide + H2O
?
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
additional information
?
-
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-[(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
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
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
-
-
-
-
?
cephalosporin + H2O
7-aminocephalosporanic acid + an amino acid
-
-
-
?
cephalosporin + H2O
7-aminocephalosporanic acid + an amino acid
-
-
-
-
?
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxicillin + NH3
-
-
-
-
r
D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
amoxicillin + 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
-
-
-
-
r
D-phenylglycine amide + 7-aminodesacetoxycephalosporanic acid
cephalexin + NH3
-
kinetically controlled synthesis
-
-
r
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 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-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 + 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
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-aminopenicillanic acid
-
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanic acid
-
-
-
?
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
?
-
-
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
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
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
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Bauer, K.; Kaufmann, W.; Ludwig, S.A.
A simplified determination of penicillin amidase from E. coli
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352
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The isolation and kinetics of penicillin amidase from Escherichia coli
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The preparation and kinetics of immobilised penicillin amidase from Escherichia coli
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Escherichia coli
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The penicillin acylase from Escherichia coli ATCC 11105 consists of two dissimilar subunits
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-
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Properties of penicillin amidase immobilized by copolymerization with acrylamide
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Colorimetric assay of penicillin amidase activity using phenylacetyl-aminobenzoic acid as substrate
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Kinetics of the enzymatic synthesis of benzylpenicillin
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Escherichia coli
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Enzymatic acylation of 6-aminopenicillanic acid
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Escherichia coli
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Phenylalkylsulfonyl derivatives as covalent inhibitors of penicillin amidase
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Kinetic studies on the mechanism of the penicillin amidase-catalysed synthesis of ampicillin and benzylpenicillin
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Ampicillin- and cephalhexin-synthesis catalyzed by E. coli penicillin amidase. yield increase due to substrate recycling.
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Hydrophobic interaction chromatography of penicillin amidase
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Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11 105
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Penicillin amidase from E. coli. A direct spectrophotometric method of determining the enzymes activity
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Preparation and properties of penicillin amidase immobilized in polyelectrolyte complexes
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Escherichia coli
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Improvement of the catalytic properties of penicillin G acylase from Escherichia coli ATCC 11105 by selection of a new substrate specificity
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Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase
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Purification and kinetics of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105
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-
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Kinetic investigation of penicillin G acylase from a mutant strain of Escheria coli ATCC 11105 immobilized on oxirane-acrylic beads
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Expression, purification and crystallization of penicillin G acylase from Escherichia coli ATCC 11105
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Stability and stabilisation of penicillin acylase
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74
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Improvement of posttranslational bottlenecks in the production of penicillin amidase in recombinant Escherichia coli strains
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2003
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Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli
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Phenylacetyl group as enzyme-cleavable aminoprotection of purine nucleosides
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Genetic construction of catalytically active cross-species heterodimer penicillin G amidase
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-
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The dependency of the stereoselectivity of penicillin amidases enzymes with R-specific S1 and S-specific S'1-subsites on temperature and primary structure
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-
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Proteolytic processing of penicillin amidase from Alcaligenes faecalis cloned in Escherichia coli yields several active forms
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-
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Role of the intracellular proteolysis in the production of the periplasmic penicillin amidase in Escherichia coli
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22
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2000
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-
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Ignatova, Z.; Enfors, S.O.; Hobbie, M.; Taruttis, S.; Vogt, C.; Kasche, V.
The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli
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26
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2000
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Escherichia coli (P06875)
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Bergeron, L.M.; Tokatlian, T.; Gomez, L.; Clark, D.S.
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Romero, O.; Vergara, J.; Fernandez-Lafuente, R.; Guisan, J.M.; Illanes, A.; Wilson, L.
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Blum, J.K.; Deaguero, A.L.; Perez, C.V.; Bommarius, A.S.
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Improving the diastereoselectivity of penicillin G acylase for ampicillin synthesis from racemic substrates
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Escherichia coli (P06875)
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Escherichia coli, Escherichia coli JE5505
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Adediran, S.A.; Pratt, R.F.
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Achromobacter sp., Alcaligenes faecalis, Achromobacter xylosoxidans, Bacillus badius, Bacillus subtilis, Lysinibacillus sphaericus, Fusarium oxysporum, Providencia rettgeri, Escherichia coli (P06875), Kluyvera cryocrescens (P07941), Rhizobium viscosum (P31956), Priestia megaterium (Q60136)
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Grulich, M.; Brezovsky, J.; Stepanek, V.; Palyzova, A.; Kyslikova, E.; Kyslik, P.
Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.
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Escherichia coli (P06875), Achromobacter sp. CCM 4824 (Q3ZEF0)
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Ayakar, S.; Yadav, G.
Development of novel support for penicillin acylase and its application in 6-aminopenicillanic acid production
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Escherichia coli (P06875)
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Nupur, N.; Ashish, E.Y.; Debnath, M.
Preparation and biochemical property of penicillin G amidase-loaded alginate and alginate/chitosan hydrogel beads
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2016
Escherichia coli
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