BRENDA - Enzyme Database show
show all sequences of 3.5.5.5

Purification and characterization of arylacetonitrile-specific nitrilase of Alcaligenes sp. MTCC 10675

Bhatia, S.; Mehta, P.; Bhatia, R.; Bhalla, T.; Biotechnol. Appl. Biochem. 61, 459-465 (2014)

Data extracted from this reference:

General Stability
General Stability
Organism
in citrate buffer, the activity of the enzyme increases with the increase in the pH (4.0-5.5), whereas in borate and carbonate buffers very little activity is observed
Alcaligenes sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
about 50% inhibition at 1 mM
Alcaligenes sp.
Cd2+
about 50% inhibition at 1 mM
Alcaligenes sp.
Co2+
77% inhibition at 1 mM
Alcaligenes sp.
Cs+
about 50% inhibition at 1 mM
Alcaligenes sp.
Cu2+
87% inhibition at 1 mM
Alcaligenes sp.
dithiothreitol
about 50% inhibition at 1 mM
Alcaligenes sp.
Hg2+
98% inhibition at 1 mM
Alcaligenes sp.
Mg2+
91% inhibition at 1 mM
Alcaligenes sp.
Mn2+
about 50% inhibition at 1 mM
Alcaligenes sp.
additional information
EDTA shows very little effect on arylacetonitrilase activity
Alcaligenes sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
13
-
mandelonitrile
at pH 6.5 and 30°C
Alcaligenes sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
Zn2+, Na+, and K+ show very little effect on arylacetonitrilase activity
Alcaligenes sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
8 * 60000, SDS-PAGE
Alcaligenes sp.
520000
-
gel filtration
Alcaligenes sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Alcaligenes sp.
L7RY40
-
-
Alcaligenes sp. MTCC 10675
L7RY40
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Sephacryl S-300 gel filtration
Alcaligenes sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diphenylacetonitrile + H2O
-
733546
Alcaligenes sp.
diphenylacetic acid + NH3
-
-
-
?
diphenylacetonitrile + H2O
-
733546
Alcaligenes sp. MTCC 10675
diphenylacetic acid + NH3
-
-
-
?
mandelonitrile + H2O
-
733546
Alcaligenes sp.
mandelic acid + NH3
-
-
-
?
mandelonitrile + H2O
-
733546
Alcaligenes sp. MTCC 10675
mandelic acid + NH3
-
-
-
?
additional information
the purified enzyme has very little activity against heterocyclic and aliphatic nitriles like 2-cyanopyridine and 4-cyanopyridine, and no activity is recorded against aromatic nitriles like benzonitrile, 4-hydroxynitrile, and tolunitrile
733546
Alcaligenes sp.
?
-
-
-
-
additional information
the purified enzyme has very little activity against heterocyclic and aliphatic nitriles like 2-cyanopyridine and 4-cyanopyridine, and no activity is recorded against aromatic nitriles like benzonitrile, 4-hydroxynitrile, and tolunitrile
733546
Alcaligenes sp. MTCC 10675
?
-
-
-
-
phenylacetonitrile + H2O
best substrate
733546
Alcaligenes sp.
phenylacetic acid + NH3
-
-
-
?
phenylacetonitrile + H2O
best substrate
733546
Alcaligenes sp. MTCC 10675
phenylacetic acid + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
homooctamer
8 * 60000, SDS-PAGE
Alcaligenes sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
-
Alcaligenes sp.
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
15
55
exposure of the enzyme at 15, 25, and 35°C for 5 h causes 8%, 15%, and 28% decrease in arylacetonitrilase activity, respectively. A further increase in the temperature to 45 and 55°C results in 58% and 90% decrease in activity, respectively. The half-life of this enzyme at 15, 25, 35, 45, 50, and 55°C is 31 h, 16 h, 9 h, 4 h 30 min, 3 h 20 min, and 2 h 40 min, respectively
Alcaligenes sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
26
-
mandelonitrile
at pH 6.5 and 50°C
Alcaligenes sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Alcaligenes sp.
General Stability (protein specific)
General Stability
Organism
in citrate buffer, the activity of the enzyme increases with the increase in the pH (4.0-5.5), whereas in borate and carbonate buffers very little activity is observed
Alcaligenes sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
about 50% inhibition at 1 mM
Alcaligenes sp.
Cd2+
about 50% inhibition at 1 mM
Alcaligenes sp.
Co2+
77% inhibition at 1 mM
Alcaligenes sp.
Cs+
about 50% inhibition at 1 mM
Alcaligenes sp.
Cu2+
87% inhibition at 1 mM
Alcaligenes sp.
dithiothreitol
about 50% inhibition at 1 mM
Alcaligenes sp.
Hg2+
98% inhibition at 1 mM
Alcaligenes sp.
Mg2+
91% inhibition at 1 mM
Alcaligenes sp.
Mn2+
about 50% inhibition at 1 mM
Alcaligenes sp.
additional information
EDTA shows very little effect on arylacetonitrilase activity
Alcaligenes sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
13
-
mandelonitrile
at pH 6.5 and 30°C
Alcaligenes sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
Zn2+, Na+, and K+ show very little effect on arylacetonitrilase activity
Alcaligenes sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
8 * 60000, SDS-PAGE
Alcaligenes sp.
520000
-
gel filtration
Alcaligenes sp.
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Sephacryl S-300 gel filtration
Alcaligenes sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diphenylacetonitrile + H2O
-
733546
Alcaligenes sp.
diphenylacetic acid + NH3
-
-
-
?
diphenylacetonitrile + H2O
-
733546
Alcaligenes sp. MTCC 10675
diphenylacetic acid + NH3
-
-
-
?
mandelonitrile + H2O
-
733546
Alcaligenes sp.
mandelic acid + NH3
-
-
-
?
mandelonitrile + H2O
-
733546
Alcaligenes sp. MTCC 10675
mandelic acid + NH3
-
-
-
?
additional information
the purified enzyme has very little activity against heterocyclic and aliphatic nitriles like 2-cyanopyridine and 4-cyanopyridine, and no activity is recorded against aromatic nitriles like benzonitrile, 4-hydroxynitrile, and tolunitrile
733546
Alcaligenes sp.
?
-
-
-
-
additional information
the purified enzyme has very little activity against heterocyclic and aliphatic nitriles like 2-cyanopyridine and 4-cyanopyridine, and no activity is recorded against aromatic nitriles like benzonitrile, 4-hydroxynitrile, and tolunitrile
733546
Alcaligenes sp. MTCC 10675
?
-
-
-
-
phenylacetonitrile + H2O
best substrate
733546
Alcaligenes sp.
phenylacetic acid + NH3
-
-
-
?
phenylacetonitrile + H2O
best substrate
733546
Alcaligenes sp. MTCC 10675
phenylacetic acid + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homooctamer
8 * 60000, SDS-PAGE
Alcaligenes sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
-
Alcaligenes sp.
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
15
55
exposure of the enzyme at 15, 25, and 35°C for 5 h causes 8%, 15%, and 28% decrease in arylacetonitrilase activity, respectively. A further increase in the temperature to 45 and 55°C results in 58% and 90% decrease in activity, respectively. The half-life of this enzyme at 15, 25, 35, 45, 50, and 55°C is 31 h, 16 h, 9 h, 4 h 30 min, 3 h 20 min, and 2 h 40 min, respectively
Alcaligenes sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
26
-
mandelonitrile
at pH 6.5 and 50°C
Alcaligenes sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Alcaligenes sp.
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
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
-
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1
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1
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-
-
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
1
1
1
-
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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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
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1
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8
1
1
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1
1
1
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1
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10
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1
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1
2
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1
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-
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
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-
-
2
-
-
-
-
-
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-
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
-
-
-
-
-
-
-
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8
-
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2
4
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2
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4
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-
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
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-
-
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1
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-
-
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
-
-
-
-
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-
-
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2
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14
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2
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-
-
-
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-
-
-
-
-
-
-
712643
He
Biocatalytic synthesis of (R)- ...
Alcaligenes faecalis
J. Ind. Microbiol. Biotechnol.
37
741-750
2010
-
-
-
-
-
-
-
-
-
-
-
4
-
2
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5
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4
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5
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
710930
Kiziak
Identification of amino acid r ...
Pseudomonas fluorescens
Appl. Environ. Microbiol.
75
5592-5599
2009
-
-
1
-
8
-
-
-
-
-
-
-
-
5
-
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-
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2
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1
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8
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2
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712260
Thuku
Microbial nitrilases: Versatil ...
Alcaligenes faecalis, Alcaligenes faecalis ATCC 8750
J. Appl. Microbiol.
106
703-727
2009
-
-
-
-
-
-
-
-
-
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2
-
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4
-
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6
1
1
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1
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2
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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
Mol. Plant Pathol.
10
857-865
2009
-
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-
-
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10
-
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4
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4
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-
-
717051
Sosedov
-
Synthesis of enantiomerically ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
Adv. Synth. Catal.
351
1531 - 1538
2009
-
-
1
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-
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-
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5
-
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2
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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
Appl. Microbiol. Biotechnol.
80
87-97
2008
-
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1
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13
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2
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1
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
J. Biotechnol.
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327-333
2008
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24
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26
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694107
Banerjee
enantioselective nitrilase fro ...
Pseudomonas putida, Pseudomonas putida MTCC 5110
Mol. Biotechnol.
41
35-41
2008
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10
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700670
Agerbirk
Sinapis phylogeny and evolutio ...
Sinapis alba
Phytochemistry
69
2937-2949
2008
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3
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701254
Rustler
Characterisation of the substr ...
Exophiala oligosperma, Exophiala oligosperma R1
Stud. Mycol.
61
165-174
2008
1
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12
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689852
Kiziak
Influence of different carboxy ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
Protein Eng. Des. Sel.
20
385-396
2007
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10
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4
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667345
Banerjee
Purification and characterizat ...
Pseudomonas putida
Arch. Microbiol.
184
407-418
2006
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7
3
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2
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18
2
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1
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7
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3
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1
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2
18
2
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4
1
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4
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718003
Mateo
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Stabilisation of oxygen-labile ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
J. Mol. Catal. B
38
154-157
2006
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1
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718410
Mateo
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Synthesis of enantiomerically ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
Tetrahedron Asymmetry
17
320-323
2006
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1
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670163
Kiziak
Nitrilase from Pseudomonas flu ...
Pseudomonas fluorescens, Pseudomonas fluorescens EBC191
Microbiology
151
3639-3648
2005
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10
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15
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15
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652959
Layh
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Characterization and partial p ...
Pseudomonas fluorescens
J. Mol. Catal. B
5
467-474
1998
2
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2
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32502
Mauger
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Occurrence of a novel nitrilas ...
Alcaligenes faecalis, Alcaligenes faecalis JM3
Arch. Microbiol.
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1-6
1990
2
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20
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32503
Nagasawa
A novel nitrilase, arylacetoni ...
Alcaligenes faecalis, Alcaligenes faecalis JM3
Eur. J. Biochem.
194
765-772
1990
3
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13
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1
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5
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33
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27
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13
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5
1
1
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4
33
1
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1
3
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1
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