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show all sequences of 3.5.1.13

Cloning and characterization of a novel amidase from Paracoccus sp. M-1, showing aryl acylamidase and acyl transferase activities

Shen, W.; Chen, H.; Jia, K.; Ni, J.; Yan, X.; Li, S.; Appl. Microbiol. Biotechnol. 94, 1007-1018 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene pamH, DNA and amino acid sequence determination and analysis, sequence comparison, cloning and expression of His6-tagged PamH in Escherichia coli strains DH5alpha and BL21 (DE3), respectively; gene pamh, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). The enzyme is only successfully expressed using autoinduction media under low-temperature incubation at 25°C, otherwise, the expressed proteins forms inclusion bodies
Paracoccus sp. M1-1
Engineering
Amino acid exchange
Commentary
Organism
K84A
no activity, part of the catalytic triad; site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
Paracoccus sp. M1-1
S159A
no activity, part of the catalytic triad; site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
Paracoccus sp. M1-1
S183A
no activity, part of the catalytic triad; site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
Paracoccus sp. M1-1
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
; 20-30% inhibition at 1 mM
Paracoccus sp. M1-1
2-mercaptoethanol
52% inhibition at 1 mM
Paracoccus sp. M1-1
4-chloromercuribenzoate
-
Paracoccus sp. M1-1
4-chloromercurybenzoate
-
Paracoccus sp. M1-1
Co2+
; 1 mM: 8.5% activity; strong inhibition
Paracoccus sp. M1-1
Cr2+
-
Paracoccus sp. M1-1
Cu2+
; 1 mM: 8.9% activity; strong inhibition
Paracoccus sp. M1-1
EDTA
; 20-30% inhibition at 1 mM
Paracoccus sp. M1-1
Fe2+
-
Paracoccus sp. M1-1
Hg2+
; 1 mM: 0% activity; complete inhibition
Paracoccus sp. M1-1
iodoacetamide
-
Paracoccus sp. M1-1
Ni2+
-
Paracoccus sp. M1-1
PMSF
; 10 mM: 9.8% activity; strong inhibition
Paracoccus sp. M1-1
SDS
-
Paracoccus sp. M1-1
Triton X-100
-
Paracoccus sp. M1-1
Tween-80
-
Paracoccus sp. M1-1
Zn2+
-
Paracoccus sp. M1-1
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.158
-
3',4'-dichloropropionanilide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
0.158
-
N-(3,4-dichlorophenyl)propanamide
pH 7.0, 35°C
Paracoccus sp. M1-1
0.158
-
N-(3,4-dichlorophenyl) propanamide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates at 1 mM
Paracoccus sp. M1-1
Mg2+
activates 1.1fold at 1 mM; activates 1.3fold at 1 mM
Paracoccus sp. M1-1
Mn2+
activates 1.1fold at 1 mM; activates 1.3fold at 1 mM
Paracoccus sp. M1-1
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
x * 52000, about, sequence calculation; x * 52000, recombinant enzyme, SDS-PAGE, x * 52390, sequence calculation
Paracoccus sp. M1-1
52390
-
x * 52000, recombinant enzyme, SDS-PAGE, x * 52390, sequence calculation
Paracoccus sp. M1-1
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paracoccus sp. M1-1
F6N111
; gene pamH
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate fractionation, ion exchange chromatography (DEAE-Sephadex, DEAE-Cellulose, gel filtration); recombinant His6-tagged PamH 5.8fold from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration; recombinant His6-tagged wild-type enzyme 5.82fold from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, dialysis, anion exchange chromatography, gel filtration, and ultrafiltration
Paracoccus sp. M1-1
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
39.8
-
N-(3,4-dichlorophenyl)propanamide, pH 7.0, 35°C; purified recombinant His6-tagged PamH, pH 7.0, 35°C
Paracoccus sp. M1-1
Storage Stability
Storage Stability
Organism
rapid loss of activity during purification and storage in Tris-HCl (10 mM, pH 8.0) buffer at 4°C or 20°C, with the addition of 10% glycerol and 50 mM NaCl prior to freezing activity is maintained for up to 3 months with only marginal losses
Paracoccus sp. M1-1
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3',4'-dichloropropionanilide + H2O
i.e. propanil
718672
Paracoccus sp. M1-1
3,4-dichloroaniline + propionate
-
-
-
?
benzamide + H2O
-
718672
Paracoccus sp. M1-1
benzoate + NH3
-
-
-
?
additional information
substrate specificity, overview. PamH is highly active on aromatic and short-chain aliphatic amides, e.g. benzamide and propionamide, moderately active on amino acid amides, and possesses weak urease activity. Of the anilides examined, only propanil is a good substrate for PamH. PamH is also able to catalyze the acyl transfer reaction to hydroxylamine for both amide and anilide substrates, including acetamide, propanil, and 4-nitroacetanilide, it shows the highest reaction rate with isobutyramide
718672
Paracoccus sp. M1-1
?
-
-
-
-
additional information
the PamH enzyme exhibits amidase activity, aryl acylamidase activity (EC 3.5.1.13), and acyl transferase activity. It shows excellent activity toward the majority of the aromatic and aliphatic amides, such as acetamide, propionamide, phenylacetamide, and benzamide. The aromatic amides, with substitutions of one or two carbons in the ring by a nitrogen, have a negative influence on amidase activity, leading to low specific activity values for pyrazinamide and nicotinamide. No activity is detectable on long-chain aliphatic amide hexanoamides. Amino acid amides are also hydrolyzed by the enzyme. The enzyme possesses urease activity, but N-methyl substituted is not hydrolyzed by the enzyme. The amidase shows low activity on asparagines (9%), L-glutamine (17%), and D-glutamine (13%) corresponding to benzamide (100%). The anilide substrate range of the enzyme is very narrow and cannot hydrolyze butachlor, acetochlor, 4-nitroacetanilide, p-chloroacetanilide, or other structurally analogous compounds
718672
Paracoccus sp. M1-1
?
-
-
-
-
N-(3,4-dichlorophenyl) propanamide + H2O
i.e. propanil
718672
Paracoccus sp. M1-1
3,4-dichloroaniline + propanoic acid
-
-
-
?
N-(3,4-dichlorophenyl)propanamide + H2O
no activity with butachlor, acetochlor, 4-nitroacetanilide, p-chloracetanilide
718672
Paracoccus sp. M1-1
3,4-dichloraniline + propanoate
-
-
-
?
propanamide + H2O
-
718672
Paracoccus sp. M1-1
propanoic acid + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 52000, about, sequence calculation; x * 52000, recombinant enzyme, SDS-PAGE, x * 52390, sequence calculation
Paracoccus sp. M1-1
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
; recombinant enzyme
Paracoccus sp. M1-1
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
70
activity range, profile overview
Paracoccus sp. M1-1
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
60
the purified recombinant wild-type enzyme is fairly stable up to 40°C, has 25% residual activity at 50°C after 1 h, and is completely inactivated at 60°C after 30 min
Paracoccus sp. M1-1
40
-
fairly stable up to 40°C, completely inactivated during 30 min at 60°C; purified recombinant enzyme, fairly stable up to, over 90% activity remaining after 1 h
Paracoccus sp. M1-1
50
-
25% residual activity after 1 h at 50°C, completely inactivated during 30 min at 60°C; purified recombinant enzyme, 25% activity remaining after 1 h
Paracoccus sp. M1-1
60
-
purified recombinant enzyme, 30 min, complete inactivation
Paracoccus sp. M1-1
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.8
-
3',4'-dichloropropionanilide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
2.8
-
N-(3,4-dichlorophenyl)propanamide
pH 7.0, 35°C
Paracoccus sp. M1-1
2.8
-
N-(3,4-dichlorophenyl) propanamide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
; recombinant enzyme
Paracoccus sp. M1-1
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
10
activity range, profile overview
Paracoccus sp. M1-1
6
9
activity range
Paracoccus sp. M1-1
6.5
9
highly active
Paracoccus sp. M1-1
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4
-
purified recombinant enzyme, 30% activity remaining after 1 h
Paracoccus sp. M1-1
4.5
10
purified recombinant enzyme, over 50% activity within this range at 35°C
Paracoccus sp. M1-1
4.5
-
purified recombinant enzyme, 60% activity remaining after 1 h
Paracoccus sp. M1-1
5
10
more than 70% activity after preincubation for 1 h; purified recombinant enzyme, over 70% activity remaining after 1 h
Paracoccus sp. M1-1
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Paracoccus sp. M1-1
isoelectric focusing; isoelectric focusing, recombinant enzyme
-
5.13
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pamH, DNA and amino acid sequence determination and analysis, sequence comparison, cloning and expression of His6-tagged PamH in Escherichia coli strains DH5alpha and BL21 (DE3), respectively; gene pamh, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3). The enzyme is only successfully expressed using autoinduction media under low-temperature incubation at 25°C, otherwise, the expressed proteins forms inclusion bodies
Paracoccus sp. M1-1
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K84A
no activity, part of the catalytic triad; site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
Paracoccus sp. M1-1
S159A
no activity, part of the catalytic triad; site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
Paracoccus sp. M1-1
S183A
no activity, part of the catalytic triad; site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
Paracoccus sp. M1-1
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
; 20-30% inhibition at 1 mM
Paracoccus sp. M1-1
2-mercaptoethanol
52% inhibition at 1 mM
Paracoccus sp. M1-1
4-chloromercuribenzoate
-
Paracoccus sp. M1-1
4-chloromercurybenzoate
-
Paracoccus sp. M1-1
Co2+
; 1 mM: 8.5% activity; strong inhibition
Paracoccus sp. M1-1
Cr2+
-
Paracoccus sp. M1-1
Cu2+
; 1 mM: 8.9% activity; strong inhibition
Paracoccus sp. M1-1
EDTA
; 20-30% inhibition at 1 mM
Paracoccus sp. M1-1
Fe2+
-
Paracoccus sp. M1-1
Hg2+
; 1 mM: 0% activity; complete inhibition
Paracoccus sp. M1-1
iodoacetamide
-
Paracoccus sp. M1-1
Ni2+
-
Paracoccus sp. M1-1
PMSF
; 10 mM: 9.8% activity; strong inhibition
Paracoccus sp. M1-1
SDS
-
Paracoccus sp. M1-1
Triton X-100
-
Paracoccus sp. M1-1
Tween-80
-
Paracoccus sp. M1-1
Zn2+
-
Paracoccus sp. M1-1
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.158
-
3',4'-dichloropropionanilide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
0.158
-
N-(3,4-dichlorophenyl)propanamide
pH 7.0, 35°C
Paracoccus sp. M1-1
0.158
-
N-(3,4-dichlorophenyl) propanamide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates at 1 mM
Paracoccus sp. M1-1
Mg2+
activates 1.1fold at 1 mM; activates 1.3fold at 1 mM
Paracoccus sp. M1-1
Mn2+
activates 1.1fold at 1 mM; activates 1.3fold at 1 mM
Paracoccus sp. M1-1
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
x * 52000, about, sequence calculation; x * 52000, recombinant enzyme, SDS-PAGE, x * 52390, sequence calculation
Paracoccus sp. M1-1
52390
-
x * 52000, recombinant enzyme, SDS-PAGE, x * 52390, sequence calculation
Paracoccus sp. M1-1
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate fractionation, ion exchange chromatography (DEAE-Sephadex, DEAE-Cellulose, gel filtration); recombinant His6-tagged PamH 5.8fold from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration; recombinant His6-tagged wild-type enzyme 5.82fold from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, dialysis, anion exchange chromatography, gel filtration, and ultrafiltration
Paracoccus sp. M1-1
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
39.8
-
N-(3,4-dichlorophenyl)propanamide, pH 7.0, 35°C; purified recombinant His6-tagged PamH, pH 7.0, 35°C
Paracoccus sp. M1-1
Storage Stability (protein specific)
Storage Stability
Organism
rapid loss of activity during purification and storage in Tris-HCl (10 mM, pH 8.0) buffer at 4°C or 20°C, with the addition of 10% glycerol and 50 mM NaCl prior to freezing activity is maintained for up to 3 months with only marginal losses
Paracoccus sp. M1-1
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3',4'-dichloropropionanilide + H2O
i.e. propanil
718672
Paracoccus sp. M1-1
3,4-dichloroaniline + propionate
-
-
-
?
benzamide + H2O
-
718672
Paracoccus sp. M1-1
benzoate + NH3
-
-
-
?
additional information
substrate specificity, overview. PamH is highly active on aromatic and short-chain aliphatic amides, e.g. benzamide and propionamide, moderately active on amino acid amides, and possesses weak urease activity. Of the anilides examined, only propanil is a good substrate for PamH. PamH is also able to catalyze the acyl transfer reaction to hydroxylamine for both amide and anilide substrates, including acetamide, propanil, and 4-nitroacetanilide, it shows the highest reaction rate with isobutyramide
718672
Paracoccus sp. M1-1
?
-
-
-
-
additional information
the PamH enzyme exhibits amidase activity, aryl acylamidase activity (EC 3.5.1.13), and acyl transferase activity. It shows excellent activity toward the majority of the aromatic and aliphatic amides, such as acetamide, propionamide, phenylacetamide, and benzamide. The aromatic amides, with substitutions of one or two carbons in the ring by a nitrogen, have a negative influence on amidase activity, leading to low specific activity values for pyrazinamide and nicotinamide. No activity is detectable on long-chain aliphatic amide hexanoamides. Amino acid amides are also hydrolyzed by the enzyme. The enzyme possesses urease activity, but N-methyl substituted is not hydrolyzed by the enzyme. The amidase shows low activity on asparagines (9%), L-glutamine (17%), and D-glutamine (13%) corresponding to benzamide (100%). The anilide substrate range of the enzyme is very narrow and cannot hydrolyze butachlor, acetochlor, 4-nitroacetanilide, p-chloroacetanilide, or other structurally analogous compounds
718672
Paracoccus sp. M1-1
?
-
-
-
-
N-(3,4-dichlorophenyl) propanamide + H2O
i.e. propanil
718672
Paracoccus sp. M1-1
3,4-dichloroaniline + propanoic acid
-
-
-
?
N-(3,4-dichlorophenyl)propanamide + H2O
no activity with butachlor, acetochlor, 4-nitroacetanilide, p-chloracetanilide
718672
Paracoccus sp. M1-1
3,4-dichloraniline + propanoate
-
-
-
?
propanamide + H2O
-
718672
Paracoccus sp. M1-1
propanoic acid + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 52000, about, sequence calculation; x * 52000, recombinant enzyme, SDS-PAGE, x * 52390, sequence calculation
Paracoccus sp. M1-1
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
; recombinant enzyme
Paracoccus sp. M1-1
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
70
activity range, profile overview
Paracoccus sp. M1-1
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
60
the purified recombinant wild-type enzyme is fairly stable up to 40°C, has 25% residual activity at 50°C after 1 h, and is completely inactivated at 60°C after 30 min
Paracoccus sp. M1-1
40
-
fairly stable up to 40°C, completely inactivated during 30 min at 60°C; purified recombinant enzyme, fairly stable up to, over 90% activity remaining after 1 h
Paracoccus sp. M1-1
50
-
25% residual activity after 1 h at 50°C, completely inactivated during 30 min at 60°C; purified recombinant enzyme, 25% activity remaining after 1 h
Paracoccus sp. M1-1
60
-
purified recombinant enzyme, 30 min, complete inactivation
Paracoccus sp. M1-1
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.8
-
3',4'-dichloropropionanilide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
2.8
-
N-(3,4-dichlorophenyl)propanamide
pH 7.0, 35°C
Paracoccus sp. M1-1
2.8
-
N-(3,4-dichlorophenyl) propanamide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
; recombinant enzyme
Paracoccus sp. M1-1
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
10
activity range, profile overview
Paracoccus sp. M1-1
6
9
activity range
Paracoccus sp. M1-1
6.5
9
highly active
Paracoccus sp. M1-1
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4
-
purified recombinant enzyme, 30% activity remaining after 1 h
Paracoccus sp. M1-1
4.5
10
purified recombinant enzyme, over 50% activity within this range at 35°C
Paracoccus sp. M1-1
4.5
-
purified recombinant enzyme, 60% activity remaining after 1 h
Paracoccus sp. M1-1
5
10
more than 70% activity after preincubation for 1 h; purified recombinant enzyme, over 70% activity remaining after 1 h
Paracoccus sp. M1-1
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Paracoccus sp. M1-1
isoelectric focusing; isoelectric focusing, recombinant enzyme
-
5.13
General Information
General Information
Commentary
Organism
evolution
PamH belongs to the amidase signature, AS, enzyme family. The Ser-Ser-Lys catalytic residues are highly conserved, indicating that there is an evolutionary relationship between the enzymes in the AS family; the enzyme belongs to the amidase signature enzyme family
Paracoccus sp. M1-1
additional information
the enzyme maintains a core alpha/beta/alpha structure and the G-(GAV)-S-(GS)2-GX-(GSAE)-(GSAVYCT)-X-(LIVMT)-(GSA)-X6-(GSAT)-X-(GA)-X-(DE)-X-(GA)-X-S-(LIVM)-R-X-P-(GSACTL) sequence motif
Paracoccus sp. M1-1
General Information (protein specific)
General Information
Commentary
Organism
evolution
PamH belongs to the amidase signature, AS, enzyme family. The Ser-Ser-Lys catalytic residues are highly conserved, indicating that there is an evolutionary relationship between the enzymes in the AS family; the enzyme belongs to the amidase signature enzyme family
Paracoccus sp. M1-1
additional information
the enzyme maintains a core alpha/beta/alpha structure and the G-(GAV)-S-(GS)2-GX-(GSAE)-(GSAVYCT)-X-(LIVMT)-(GSA)-X6-(GSAT)-X-(GA)-X-(DE)-X-(GA)-X-S-(LIVM)-R-X-P-(GSACTL) sequence motif
Paracoccus sp. M1-1
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
17.72
-
3',4'-dichloropropionanilide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
17.72
-
N-(3,4-dichlorophenyl) propanamide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
18
-
N-(3,4-dichlorophenyl)propanamide
pH 7.0, 35°C
Paracoccus sp. M1-1
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
17.72
-
3',4'-dichloropropionanilide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
17.72
-
N-(3,4-dichlorophenyl) propanamide
pH 7.0, 35°C, recombinant enzyme
Paracoccus sp. M1-1
18
-
N-(3,4-dichlorophenyl)propanamide
pH 7.0, 35°C
Paracoccus sp. M1-1
Other publictions for EC 3.5.1.13
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733190
Ma
Nitrilase superfamily aryl acy ...
Streptomyces sp. 211726, Streptomyces sp.
Appl. Microbiol. Biotechnol.
98
8583-8590
2014
2
-
1
-
3
-
5
-
-
1
1
2
-
5
-
-
1
-
-
1
3
-
10
1
1
1
3
-
1
1
1
-
-
-
-
2
-
1
-
-
3
-
-
5
-
-
-
1
1
2
-
-
-
1
-
1
3
-
10
1
1
1
3
-
1
1
1
-
-
1
1
-
-
-
718672
Shen
Cloning and characterization o ...
Paracoccus sp. M1-1
Appl. Microbiol. Biotechnol.
94
1007-1018
2012
-
-
1
-
3
-
17
3
-
3
2
-
-
3
-
-
1
-
-
-
1
1
7
1
1
1
4
3
1
3
4
-
-
1
-
-
-
1
-
-
3
-
-
17
-
3
-
3
2
-
-
-
-
1
-
-
1
1
7
1
1
1
4
3
1
3
4
1
-
2
2
-
3
3
720273
Acero
-
Two-step enzymatic functionali ...
Nocardia farcinica, Nocardia farcinica IFM 10152
J. Mol. Catal. B
79
54-60
2012
-
-
-
-
-
-
-
1
-
-
1
-
-
3
-
-
1
-
-
-
1
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
713035
Ko
Molecular characterization of ...
bacterium CSBL00001
Mol. Cells
29
485-492
2010
-
-
1
-
-
-
5
4
-
-
-
5
-
2
-
-
-
-
-
-
-
-
7
-
1
-
4
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
5
-
4
-
-
-
5
-
-
-
-
-
-
-
-
7
-
1
-
4
-
2
-
-
-
-
-
-
-
-
-
696876
Heumann
A novel aryl acylamidase from ...
Nocardia farcinica
Biotechnol. Bioeng.
102
1003-1011
2009
-
-
-
-
-
-
4
2
-
-
3
-
-
4
-
-
1
-
-
-
1
2
13
1
1
-
1
2
1
1
-
-
4
-
-
-
-
-
-
-
-
-
-
4
4
2
-
-
3
-
-
-
-
1
-
-
1
2
13
1
1
-
1
2
1
1
-
-
-
-
-
-
-
-
697902
Montenegro
Hydrolysis of acetylthiocoline ...
Bos taurus
FEBS J.
276
2074-2083
2009
-
-
-
-
-
-
2
2
-
-
-
-
-
3
-
-
1
-
-
1
1
-
2
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
1
-
1
1
-
2
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
711318
Rajesh
The aryl acylamidase activity ...
Gallus gallus
Biochimie
91
1087-1094
2009
-
-
-
-
-
-
4
-
-
-
-
-
-
3
-
-
1
-
-
3
-
-
1
-
1
-
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
3
4
-
-
-
-
-
-
-
-
-
1
-
3
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
711319
Rajesh
High aryl acylamidase activity ...
Bungarus, Daboia russelii, Echis carinatus, Naja oxiana
Biochimie
91
1450-1456
2009
-
4
-
-
-
-
2
-
4
-
-
-
-
7
-
-
-
-
-
4
-
-
4
-
4
-
-
-
4
-
-
-
-
-
-
-
4
-
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
4
-
-
4
-
4
-
-
-
4
-
-
-
-
4
4
-
-
-
678541
Montenegro
Human butyrylcholinesterase co ...
Homo sapiens
Biol. Chem.
389
425-432
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
4
7
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
4
7
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679183
Montenegro
The level of aryl acylamidase ...
Homo sapiens
Chem. Biol. Interact.
175
336-339
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
3
3
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
3
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697309
Li
Binding and hydrolysis of soma ...
Homo sapiens
Chem. Res. Toxicol.
21
421-431
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697867
Masson
Kinetic analysis of effector m ...
Homo sapiens
FEBS J.
275
2617-2631
2008
2
-
1
-
1
-
3
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
10
-
-
2
-
1
-
-
1
-
-
3
10
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
678058
Peterson
The dependence of enzyme activ ...
Pseudomonas fluorescens
Biochem. J.
403
615
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
679287
Boopathy
Human serum cholinesterase fro ...
Homo sapiens
Clin. Chim. Acta
380
151-156
2007
-
1
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
5
21
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
5
21
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681110
Masson
Aryl acylamidase activity of h ...
Homo sapiens
J. Enzyme Inhib. Med. Chem.
22
463-469
2007
-
-
-
-
-
-
1
1
-
-
-
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667330
Manoharan
Diisopropylfluorophosphate-sen ...
Homo sapiens
Arch. Biochem. Biophys.
452
186-188
2006
-
-
-
-
-
-
1
-
1
-
-
1
-
2
-
-
-
-
-
6
1
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
6
1
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
667928
Darvesh
On the active site for hydroly ...
Homo sapiens, Pseudomonas fluorescens
Bioorg. Med. Chem.
14
4586-4599
2006
-
-
-
-
-
-
-
8
-
-
-
1
-
3
-
-
-
1
-
1
2
-
27
1
2
-
-
11
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
1
-
-
-
-
-
1
2
-
27
1
2
-
-
11
2
-
-
-
-
-
-
-
-
-
668239
Allebrandt
Expression of acetylcholineste ...
Danio rerio
Chem. Biol. Interact.
157-158
353-355
2005
-
-
-
-
-
-
2
-
-
-
-
1
-
3
-
-
-
-
-
1
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
670800
Boopathy
Aryl acylamidase activity on a ...
Gallus gallus
Protein J.
23
325-333
2004
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
1
1
-
3
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
3
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
657938
Stein
Enzymatic hydrolysis of p-nitr ...
Pseudomonas fluorescens
Biochemistry
41
991-1000
2002
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
208992
Weitnauer
Aryl acylamidase activity exhi ...
Equus caballus, Gallus gallus
Neurosci. Lett.
254
153-156
1998
-
-
-
-
-
-
2
-
-
-
-
-
-
6
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208994
Costagli
Inhibition of cholinesterase-a ...
Electrophorus electricus, Equus caballus
Biochem. Pharmacol.
55
1733-1737
1998
-
-
-
-
-
-
28
-
-
-
-
-
-
4
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
28
-
-
-
-
-
-
-
-
-
-
-
3
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208993
Fukuda
Crystallization and preliminar ...
Tulipa gesneriana
Acta Crystallogr. Sect. D
53
342-344
1997
-
-
-
1
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208991
Hoagland
-
Rhizobacteria with exceptional ...
Pseudomonas sp., Pseudomonas sp. RA2
Pestic. Biochem. Physiol.
52
190-200
1995
-
-
-
-
-
-
1
6
-
-
-
2
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
6
-
-
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208971
Villarreal
A structure-activity study wit ...
Acinetobacter sp., Acinetobacter sp. DV1, Arthrobacter sp., Corynebacterium sp., Corynebacterium sp. DAK12
Appl. Environ. Microbiol.
60
3939-3944
1994
-
-
-
-
-
-
-
-
-
-
-
10
-
5
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208996
Checler
Cholinesterases display genuin ...
Electrophorus electricus
J. Neurochem.
62
756-763
1994
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208997
Jayanthi
Cholinesterases exhibiting ary ...
Homo sapiens
Clin. Chim. Acta
205
157-166
1992
1
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
208989
Khanna
Characteristics of a cytosolic ...
Felis catus, Homo sapiens, Mus musculus, Rattus norvegicus
J. Pharmacol. Exp. Ther.
262
1225-1231
1991
-
-
-
-
-
-
7
1
1
2
-
-
-
4
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
1
1
2
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
208990
Jun
-
The propanil hydrolyzing enzym ...
Oryza alta, Oryza australiensis, Oryza barthii, Oryza coarctata, Oryza collina, Oryza eichingeri, Oryza glaberrima, Oryza grandiglumis, Oryza latifolia, Oryza longiglumis, Oryza longistaminata, Oryza malabarensis, Oryza meyeriana var. granulata, Oryza minuta, Oryza officinalis, Oryza punctata, Oryza ridleyi, Oryza rufipogon, Oryza sativa
Pestic. Biochem. Physiol.
38
26-33
1990
-
-
-
-
-
-
-
12
-
-
-
-
-
19
-
-
-
-
-
-
-
-
19
-
12
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
19
-
12
-
-
-
12
-
-
-
-
-
-
-
-
-
208995
Vaughan
Aryl acylamidase from Rhodococ ...
Rhodococcus erythropolis
Appl. Microbiol. Biotechnol.
34
42-46
1990
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1
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3
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1
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3
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1
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208969
Boopathy
Chemical modification of the b ...
Homo sapiens
Eur. J. Biochem.
151
351-360
1985
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7
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2
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2
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7
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2
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208970
Majumdar
Chemical modification of acety ...
Electrophorus electricus, Ovis aries
Biochemistry
23
4088-4093
1984
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5
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3
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2
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2
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2
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208972
Gaynor
Subcellular localization of ri ...
Oryza sativa
Plant Physiol.
72
80-85
1983
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2
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1
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3
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2
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3
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208973
Hammond
Purification and properties of ...
Pseudomonas fluorescens
Eur. J. Biochem.
132
651-655
1983
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3
2
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2
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2
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1
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2
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1
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1
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3
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1
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1
2
2
1
1
1
1
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1
1
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208974
Hsu
Brain aryl acylamidase ...
Rattus norvegicus
Int. J. Biochem.
14
1037-1042
1982
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1
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4
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208975
Hsu
Rat brain aryl acylamidase: fu ...
Rattus norvegicus
Int. J. Biochem.
14
581-584
1982
7
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9
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208976
Majumdar
Essential and non-essential ph ...
Ovis aries
FEBS Lett.
146
335-338
1982
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1
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208977
George
The aryl acylamidases and thei ...
Homo sapiens
Eur. J. Biochem.
121
177-186
1981
1
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2
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2
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5
2
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1
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208978
George
The identity of the serotonin- ...
Electrophorus electricus, Homo sapiens, Ovis aries
Eur. J. Biochem.
111
511-524
1980
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15
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3
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6
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8
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3
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15
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3
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8
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3
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208979
Oommen
The association of the seroton ...
Platyrrhini
Eur. J. Biochem.
94
135-143
1979
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15
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2
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15
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1
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1
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2
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208980
Nakadai
-
Properties of arylamidase from ...
Aspergillus oryzae
Agric. Biol. Chem.
42
1291-1292
1978
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11
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1
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13
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4
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11
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1
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13
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2
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3
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4
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1
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208981
Heymann
The active site of an inducibl ...
Delftia acidovorans
Int. J. Pept. Protein Res.
11
59-64
1978
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1
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3
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208982
Hsu
Rat brain aryl acylamidase: mu ...
Rattus norvegicus
Life Sci.
20
857-866
1977
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4
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2
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1
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1
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2
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208983
Fujimoto
Serotonin-sensitive aryl acyla ...
Electrophorus electricus, Sus scrofa
FEBS Lett.
71
121-123
1976
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2
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2
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1
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3
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208984
Paul
Rat brain de-acetylating activ ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
70
207-211
1976
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7
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1
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7
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1
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208985
Hoagland
-
Hydrolysis of 3',4'-dichloropr ...
Taraxacum officinale
Phytochemistry
14
383-386
1975
-
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9
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1
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1
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10
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1
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9
1
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1
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10
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1
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3
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1
1
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208986
Hoagland
The purification and propertie ...
Glycine max
Can. J. Biochem.
52
903-910
1974
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8
1
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1
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1
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1
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1
1
1
13
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1
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1
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1
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8
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1
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1
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1
1
1
13
-
1
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1
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1
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-
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208987
Fujimoto
Serotonin-sensitive aryl acyla ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
61
72-74
1974
-
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2
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2
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2
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2
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208988
Engelhardt
Purification and properties of ...
Lysinibacillus sphaericus
Appl. Microbiol.
26
709-718
1973
-
-
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1
10
4
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1
1
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2
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1
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1
5
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3
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1
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10
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4
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1
1
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1
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1
5
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3
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