BRENDA - Enzyme Database
show all sequences of 3.5.5.5

Gene cloning, expression, and characterization of a nitrilase from Alcaligenes faecalis ZJUTB10

Liu, Z.Q.; Dong, L.Z.; Cheng, F.; Xue, Y.P.; Wang, Y.S.; Ding, J.N.; Zheng, Y.G.; Shen, Y.C.; J. Agric. Food Chem. 59, 11560-11570 (2011)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
nitrilases are important industrial enzymes that convert nitriles directly into the corresponding carboxylic acids
Alcaligenes faecalis
Cloned(Commentary)
Cloned (Commentary)
Organism
DNA and amino acid sequence determination and analysis, sequence comparison, cloning and expression as His-tagged protein in Escherichia coli strains JM109 and BL21(DE3)
Alcaligenes faecalis
Engineering
Protein Variants
Commentary
Organism
C163G
site-directed mutagenesis
Alcaligenes faecalis
E47Q
site-directed mutagenesis
Alcaligenes faecalis
K129I
site-directed mutagenesis
Alcaligenes faecalis
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
94% inhibition at 5 mM
Alcaligenes faecalis
Ba2+
8% inhibition at 5 mM
Alcaligenes faecalis
Co2+
80% inhibition at 5 mM
Alcaligenes faecalis
Cu2+
84% inhibition at 5 mM
Alcaligenes faecalis
Fe2+
17% inhibition at 5 mM
Alcaligenes faecalis
Fe3+
19% inhibition at 5 mM
Alcaligenes faecalis
Hg2+
complete inhibition at 5 mM
Alcaligenes faecalis
Li+
11% inhibition at 5 mM
Alcaligenes faecalis
Mn2+
22% inhibition at 5 mM
Alcaligenes faecalis
Ni2+
83% inhibition at 5 mM
Alcaligenes faecalis
Zn2+
36% inhibition at 5 mM
Alcaligenes faecalis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.74
-
mandelonitrile
pH 7.5, 40°C
Alcaligenes faecalis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
stimulates hydrolytic activity to 122%
Alcaligenes faecalis
additional information
no effects by Ca2+ and EDTA at 5 mM
Alcaligenes faecalis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44200
-
x * 44200, recombinant enzyme, SDS-PAGE
Alcaligenes faecalis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
mandelonitrile + 2 H2O
Alcaligenes faecalis
-
mandelate + NH3
-
-
?
mandelonitrile + 2 H2O
Alcaligenes faecalis ZJUTB10
-
mandelate + NH3
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Alcaligenes faecalis
-
-
-
Alcaligenes faecalis ZJUTB10
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Alcaligenes faecalis
Reaction
Reaction
Commentary
Organism
Reaction ID
4-chlorophenylacetonitrile + 2 H2O = 4-chlorophenylacetate + NH3
reaction mechanism, overview
Alcaligenes faecalis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(R,S)-mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis
(R)-mandelic acid + NH3
the enantiomeric excess against (R)-mandelic acid is over 99%
-
-
?
(R,S)-mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
(R)-mandelic acid + NH3
the enantiomeric excess against (R)-mandelic acid is over 99%
-
-
?
2-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
2-methoxyphenylacetic acid + NH3
-
-
-
?
2-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
2-methoxyphenylacetic acid + NH3
-
-
-
?
3-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
3-methoxyphenylacetic acid + NH3
-
-
-
?
4-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
4-methoxyphenylacetic acid + NH3
-
-
-
?
mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis
mandelate + NH3
-
-
-
?
mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
mandelate + NH3
-
-
-
?
additional information
though the enzyme exhibits activity toward both classes of aromatic and arylacetonitriles, the nitrilase shows higher activity toward the arylacetonitriles, substrate specificity and substrate docking study, overview. No activity toward aminobutytonitrile, 2,2-dimethylcyclopropyl cyanide, and 2-amino-2,3-dimethylbutanenitrile, very low activity toward 4-aminobenzonitrile and iminodiacetonitrile, overview
719629
Alcaligenes faecalis
?
-
-
-
-
additional information
though the enzyme exhibits activity toward both classes of aromatic and arylacetonitriles, the nitrilase shows higher activity toward the arylacetonitriles, substrate specificity and substrate docking study, overview. No activity toward aminobutytonitrile, 2,2-dimethylcyclopropyl cyanide, and 2-amino-2,3-dimethylbutanenitrile, very low activity toward 4-aminobenzonitrile and iminodiacetonitrile, overview
719629
Alcaligenes faecalis ZJUTB10
?
-
-
-
-
phenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
phenylacetic acid + NH3
-
-
-
?
phenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
phenylacetic acid + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 44200, recombinant enzyme, SDS-PAGE
Alcaligenes faecalis
More
homology modeling and docking, three-dimensional homology model of nitrilase, overview
Alcaligenes faecalis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
-
Alcaligenes faecalis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
65
activity range, inactive above
Alcaligenes faecalis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
35
65
purified recombinant enzyme, labile at higher temperature, half-life of 57 min at 40°C, 42 min at 45°C, and 20 min at 55°C, respectively. The activity decreases markedly above 55°C
Alcaligenes faecalis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
-
Alcaligenes faecalis
Application (protein specific)
Application
Commentary
Organism
synthesis
nitrilases are important industrial enzymes that convert nitriles directly into the corresponding carboxylic acids
Alcaligenes faecalis
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, sequence comparison, cloning and expression as His-tagged protein in Escherichia coli strains JM109 and BL21(DE3)
Alcaligenes faecalis
Engineering (protein specific)
Protein Variants
Commentary
Organism
C163G
site-directed mutagenesis
Alcaligenes faecalis
E47Q
site-directed mutagenesis
Alcaligenes faecalis
K129I
site-directed mutagenesis
Alcaligenes faecalis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
94% inhibition at 5 mM
Alcaligenes faecalis
Ba2+
8% inhibition at 5 mM
Alcaligenes faecalis
Co2+
80% inhibition at 5 mM
Alcaligenes faecalis
Cu2+
84% inhibition at 5 mM
Alcaligenes faecalis
Fe2+
17% inhibition at 5 mM
Alcaligenes faecalis
Fe3+
19% inhibition at 5 mM
Alcaligenes faecalis
Hg2+
complete inhibition at 5 mM
Alcaligenes faecalis
Li+
11% inhibition at 5 mM
Alcaligenes faecalis
Mn2+
22% inhibition at 5 mM
Alcaligenes faecalis
Ni2+
83% inhibition at 5 mM
Alcaligenes faecalis
Zn2+
36% inhibition at 5 mM
Alcaligenes faecalis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.74
-
mandelonitrile
pH 7.5, 40°C
Alcaligenes faecalis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
stimulates hydrolytic activity to 122%
Alcaligenes faecalis
additional information
no effects by Ca2+ and EDTA at 5 mM
Alcaligenes faecalis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44200
-
x * 44200, recombinant enzyme, SDS-PAGE
Alcaligenes faecalis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
mandelonitrile + 2 H2O
Alcaligenes faecalis
-
mandelate + NH3
-
-
?
mandelonitrile + 2 H2O
Alcaligenes faecalis ZJUTB10
-
mandelate + NH3
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Alcaligenes faecalis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(R,S)-mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis
(R)-mandelic acid + NH3
the enantiomeric excess against (R)-mandelic acid is over 99%
-
-
?
(R,S)-mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
(R)-mandelic acid + NH3
the enantiomeric excess against (R)-mandelic acid is over 99%
-
-
?
2-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
2-methoxyphenylacetic acid + NH3
-
-
-
?
2-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
2-methoxyphenylacetic acid + NH3
-
-
-
?
3-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
3-methoxyphenylacetic acid + NH3
-
-
-
?
4-methoxyphenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
4-methoxyphenylacetic acid + NH3
-
-
-
?
mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis
mandelate + NH3
-
-
-
?
mandelonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
mandelate + NH3
-
-
-
?
additional information
though the enzyme exhibits activity toward both classes of aromatic and arylacetonitriles, the nitrilase shows higher activity toward the arylacetonitriles, substrate specificity and substrate docking study, overview. No activity toward aminobutytonitrile, 2,2-dimethylcyclopropyl cyanide, and 2-amino-2,3-dimethylbutanenitrile, very low activity toward 4-aminobenzonitrile and iminodiacetonitrile, overview
719629
Alcaligenes faecalis
?
-
-
-
-
additional information
though the enzyme exhibits activity toward both classes of aromatic and arylacetonitriles, the nitrilase shows higher activity toward the arylacetonitriles, substrate specificity and substrate docking study, overview. No activity toward aminobutytonitrile, 2,2-dimethylcyclopropyl cyanide, and 2-amino-2,3-dimethylbutanenitrile, very low activity toward 4-aminobenzonitrile and iminodiacetonitrile, overview
719629
Alcaligenes faecalis ZJUTB10
?
-
-
-
-
phenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis
phenylacetic acid + NH3
-
-
-
?
phenylacetonitrile + 2 H2O
-
719629
Alcaligenes faecalis ZJUTB10
phenylacetic acid + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 44200, recombinant enzyme, SDS-PAGE
Alcaligenes faecalis
More
homology modeling and docking, three-dimensional homology model of nitrilase, overview
Alcaligenes faecalis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
-
-
Alcaligenes faecalis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
65
activity range, inactive above
Alcaligenes faecalis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
35
65
purified recombinant enzyme, labile at higher temperature, half-life of 57 min at 40°C, 42 min at 45°C, and 20 min at 55°C, respectively. The activity decreases markedly above 55°C
Alcaligenes faecalis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
-
Alcaligenes faecalis
General Information
General Information
Commentary
Organism
evolution
strain ZJUTB10 nitrilase belongs to the family of arylacetonitrilases
Alcaligenes faecalis
General Information (protein specific)
General Information
Commentary
Organism
evolution
strain ZJUTB10 nitrilase belongs to the family of arylacetonitrilases
Alcaligenes faecalis
Other publictions for EC 3.5.5.5
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
Synonyms
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)
733193
Sosedov
Improvement of the amides form ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
Appl. Microbiol. Biotechnol.
99
2623-2635
2015
-
-
1
-
1
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733558
Sun
Cloning, purification and eval ...
Luminiphilus syltensis, Luminiphilus syltensis NOR5-1B
Biotechnol. Lett.
37
1655-1661
2015
-
-
1
-
-
-
-
1
-
-
1
-
-
4
-
-
1
-
-
-
-
-
41
1
2
1
1
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
41
1
1
1
1
-
1
-
-
-
-
-
-
-
-
-
733546
Bhatia
Purification and characterizat ...
Alcaligenes sp., Alcaligenes sp. MTCC 10675
Biotechnol. Appl. Biochem.
61
459-465
2014
-
-
-
-
-
1
10
1
-
1
2
-
-
3
-
-
1
-
-
-
-
-
8
1
2
1
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
10
-
1
-
1
2
-
-
-
-
1
-
-
-
-
8
1
1
-
1
1
1
-
-
-
-
-
-
-
-
-
718648
Baum
Conversion of sterically deman ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
Appl. Environ. Microbiol.
78
48-57
2012
-
1
1
-
11
-
-
1
-
-
-
2
-
10
-
-
-
-
-
-
-
-
14
-
1
1
-
-
-
2
-
-
-
-
-
-
-
1
1
-
-
11
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
14
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
718670
Petrickova
Purification and characterizat ...
Aspergillus niger, Aspergillus niger CBS 513.88, Neurospora crassa, Neurospora crassa OR74A
Appl. Microbiol. Biotechnol.
93
1553-1561
2012
-
-
2
-
-
-
-
6
-
-
-
6
-
7
-
-
2
-
-
-
-
-
24
-
-
2
-
8
-
2
-
9
-
-
-
-
-
-
3
-
-
-
-
-
-
-
9
-
-
-
6
-
-
-
3
-
-
-
-
24
-
3
-
12
-
3
-
14
-
-
1
1
-
-
-
734496
Petrickova
-
Influence of point mutations n ...
Aspergillus niger, Aspergillus niger CBS 513.88, Neurospora crassa, Neurospora crassa DSM 1257
J. Mol. Catal. B
77
74-80
2012
-
-
2
-
4
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
8
-
4
-
-
-
-
2
4
-
-
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
2
4
-
-
-
-
-
-
-
-
719297
Detzel
-
Autodisplay of nitrilase from ...
Alcaligenes faecalis, Alcaligenes faecalis ATCC 8750
ChemCatChem
3
719-725
2011
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
719629
Liu
Gene cloning, expression, and ...
Alcaligenes faecalis, Alcaligenes faecalis ZJUTB10
J. Agric. Food Chem.
59
11560-11570
2011
-
1
1
-
3
-
11
1
-
2
1
2
-
2
-
-
1
1
-
-
-
-
12
2
-
1
1
1
-
1
-
-
-
-
-
-
-
1
1
-
-
3
-
-
11
-
1
-
2
1
2
-
-
-
1
-
-
-
-
12
2
1
1
1
-
1
-
-
-
-
1
1
-
-
-
710940
Sosedov
Construction and application o ...
Pseudomonas fluorescens
Appl. Environ. Microbiol.
76
3668-3674
2010
-
-
-
-
14
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712643
He
Biocatalytic synthesis of (R)- ...
Alcaligenes faecalis
J. Ind. Microbiol. Biotechnol.
37
741-750
2010
-
-
-
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
710930
Kiziak
Identification of amino acid r ...
Pseudomonas fluorescens
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1
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8
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Thuku
Microbial nitrilases: Versatil ...
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1
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6
1
1
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1
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713073
Howden
Pseudomonas syringae pv. syrin ...
no activity in no activity in Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. syringae, Pseudomonas syringae pv. syringae B728a
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4
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Synthesis of enantiomerically ...
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1
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2
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1
1
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684655
Rustler
Simultaneous expression of an ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
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87-97
2008
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1
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1
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2
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1
1
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687882
Zhu
A new nitrilase from Bradyrhiz ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum USDA 110
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327-333
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1
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3
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24
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1
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26
1
1
1
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1
1
1
1
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1
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1
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3
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1
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26
1
1
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1
1
1
1
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694107
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enantioselective nitrilase fro ...
Pseudomonas putida, Pseudomonas putida MTCC 5110
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2008
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1
1
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1
2
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2
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1
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10
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2
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1
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1
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1
1
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1
2
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1
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10
-
2
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1
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1
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700670
Agerbirk
Sinapis phylogeny and evolutio ...
Sinapis alba
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3
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701254
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Characterisation of the substr ...
Exophiala oligosperma, Exophiala oligosperma R1
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1
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2
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12
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1
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12
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689852
Kiziak
Influence of different carboxy ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
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385-396
2007
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1
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1
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10
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1
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4
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1
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1
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4
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Banerjee
Purification and characterizat ...
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7
3
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2
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3
2
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1
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1
2
18
2
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1
2
3
4
1
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4
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7
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3
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2
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3
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1
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1
2
18
2
1
2
3
4
1
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4
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718003
Mateo
-
Stabilisation of oxygen-labile ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
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2006
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1
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2
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1
1
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718410
Mateo
-
Synthesis of enantiomerically ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
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320-323
2006
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2
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1
1
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670163
Kiziak
Nitrilase from Pseudomonas flu ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
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2
15
1
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1
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1
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1
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1
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1
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1
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2
15
1
1
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1
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1
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652959
Layh
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Characterization and partial p ...
Pseudomonas fluorescens
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Occurrence of a novel nitrilas ...
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20
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1
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1
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20
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1
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Nagasawa
A novel nitrilase, arylacetoni ...
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1
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33
1
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2
1
3
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1
1
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3
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27
-
13
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5
1
1
-
-
1
-
-
1
4
33
1
2
1
3
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1
1
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-
-
-
-
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-