BRENDA - Enzyme Database show
show all sequences of 3.5.5.7

Cloning, overexpression, and characterization of a thermoactive nitrilase from the hyperthermophilic archaeon Pyrococcus abyssi

Mueller, P.; Egorova, K.; Vorgias, C.E.; Boutou, E.; Trauthwein, H.; Verseck, S.; Antranikian, G.; Protein Expr. Purif. 47, 672-681 (2006)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
activates at 1 mM
Pyrococcus abyssi
dithiothreitol
1 mM, 23% inhibition; activates at 1 mM
Pyrococcus abyssi
ethylene glycol
20% increase of activity at 10% ethylene glycol
Pyrococcus abyssi
L-cysteine
activates at 1 mM
Pyrococcus abyssi
Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli; expression in Escherichia coli
Pyrococcus abyssi
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
5 mM, 29% inhibition
Pyrococcus abyssi
5,5'-dithiobis(2-nitrobenzoate)
complete inhibition at 5 mM
Pyrococcus abyssi
acetone
10%, complete inhibition; complete inhibition at 10% acetone
Pyrococcus abyssi
Ag+
1 mM, complete inhibition; complete inhibition at 1 mM
Pyrococcus abyssi
Ca2+
1 mM, 20% inhibition; 75% residual activity at 5 mM
Pyrococcus abyssi
Cr3+
5 mM, 40% inhibition; 60% residual activity at 5 mM
Pyrococcus abyssi
dithiothreitol
5 mM, 50% inhibition
Pyrococcus abyssi
DTNB
5 mM, complete inhibition
Pyrococcus abyssi
ethanol
57% inhibition at 30%, complete inhibition at 50%; complete inhibition at 50% ethanol
Pyrococcus abyssi
ethylene glycol
80% inhibition at 50%; 80% inhibition at 50% ethylene glycol
Pyrococcus abyssi
Fe2+
40% residual activity at 5 mM; 5 mM, 60% inhibition
Pyrococcus abyssi
Hg2+
1 mM, complete inhibition; complete inhibition at 1 mM
Pyrococcus abyssi
iodacetamide
complete inhibition at 5 mM
Pyrococcus abyssi
iodacetate
complete inhibition at 5 mM
Pyrococcus abyssi
iodoacetamide
5 mM, complete inhibition
Pyrococcus abyssi
iodoacetate
5 mM, complete inhibition
Pyrococcus abyssi
L-Cys
5 mM, 27% inhibition
Pyrococcus abyssi
Malononitrile
concentrations above 12 mM have a strong inhibitory effect; strong inhibition at 12 mM
Pyrococcus abyssi
methanol
complete inhibition at 30%; complete inhibition at 30% methanol
Pyrococcus abyssi
additional information
EDTA and NaN3 have no influence on activity
Pyrococcus abyssi
p-chloromercuribenzoate
complete inhibition at 1 mM
Pyrococcus abyssi
p-hydroxymercuribenzoate
1 mM, complete inhibition; complete inhibition at 1 mM
Pyrococcus abyssi
PCMB
1 mM, complete inhibition
Pyrococcus abyssi
phenyl hydrazine
53% residual activity at 5 mM; 5 mM, 47% inhibition
Pyrococcus abyssi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.47
-
Malononitrile
in 20 mM potassium phosphate, pH 7.4, with 1 mM dithiothreitol, at 80°C; pH 7.4, 80°C
Pyrococcus abyssi
9.48
-
Fumaronitrile
in 20 mM potassium phosphate, pH 7.4, with 1 mM dithiothreitol, at 80°C; pH 7.4, 80°C
Pyrococcus abyssi
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
intracellular
-
Pyrococcus abyssi
5622
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29800
-
2 * 29800, gel filtration
Pyrococcus abyssi
30000
-
2 * 30000, SDS-PAGE
Pyrococcus abyssi
59800
-
gel filtration
Pyrococcus abyssi
60000
-
gel filtration; SDS-PAGE
Pyrococcus abyssi
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
no activity in Aeropyrum pernix
-
-
-
no activity in Pyrococcus furiosus
-
-
-
no activity in Pyrococcus horikoshii
-
-
-
Pyrococcus abyssi
-
-
-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
-
-
Purification (Commentary)
Commentary
Organism
; Q-Sepharose Fast Flow column chromatography and Sephadex PD-10 column gel filtration
Pyrococcus abyssi
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00595
-
recombinant enzyme from crude extract
Pyrococcus abyssi
0.1419
-
recombinant enzyme after 23.85fold purification
Pyrococcus abyssi
141.9
-
-
Pyrococcus abyssi
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fumaronitrile + H2O
-
670792
Pyrococcus abyssi
fumaric acid + NH3
-
-
-
?
fumaronitrile + H2O
preferred substrate
670792
Pyrococcus abyssi
fumaric acid + NH3
-
-
-
?
fumaronitrile + H2O
-
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
fumaric acid + NH3
-
-
-
?
fumaronitrile + H2O
preferred substrate
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
fumaric acid + NH3
-
-
-
?
malononitrile + H2O
-
670792
Pyrococcus abyssi
malonic acid + NH3
-
-
-
?
malononitrile + H2O
preferred substrate
670792
Pyrococcus abyssi
malonic acid + NH3
-
-
-
?
malononitrile + H2O
-
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
malonic acid + NH3
-
-
-
?
malononitrile + H2O
preferred substrate
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
malonic acid + NH3
-
-
-
?
additional information
compounds with a nitrile group bound to an aromatic ring or amino acid are not hydrolyzed by recombinant nitrilase
670792
Pyrococcus abyssi
?
-
-
-
-
additional information
compounds with a nitrile group bound to an aromatic ring or amino acid are not hydrolyzed by recombinant nitrilase
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 30000, SDS-PAGE
Pyrococcus abyssi
homodimer
2 * 29800, gel filtration; 2 * 30000, SDS-PAGE
Pyrococcus abyssi
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Pyrococcus abyssi
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
90
-
Pyrococcus abyssi
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
90
the recombinant enzyme is highly thermostable with a half-life of 25 h at 70°C, 9 h at 80°C, and 6 h at 90°C
Pyrococcus abyssi
70
-
25 h, recombinant enzyme loses about 50% of maximal activity
Pyrococcus abyssi
80
-
half-life: 9 h
Pyrococcus abyssi
90
-
half-life: 6 h
Pyrococcus abyssi
113
-
Tm-value: 112.7°C
Pyrococcus abyssi
120
-
irreversible denaturation after heating to 120°C
Pyrococcus abyssi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
-
Pyrococcus abyssi
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
8
-
Pyrococcus abyssi
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Pyrococcus abyssi
isoelectric focusing
-
5.3
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
activates at 1 mM
Pyrococcus abyssi
dithiothreitol
1 mM, 23% inhibition; activates at 1 mM
Pyrococcus abyssi
ethylene glycol
20% increase of activity at 10% ethylene glycol
Pyrococcus abyssi
L-cysteine
activates at 1 mM
Pyrococcus abyssi
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli; expression in Escherichia coli
Pyrococcus abyssi
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
5 mM, 29% inhibition
Pyrococcus abyssi
5,5'-dithiobis(2-nitrobenzoate)
complete inhibition at 5 mM
Pyrococcus abyssi
acetone
10%, complete inhibition; complete inhibition at 10% acetone
Pyrococcus abyssi
Ag+
1 mM, complete inhibition; complete inhibition at 1 mM
Pyrococcus abyssi
Ca2+
1 mM, 20% inhibition; 75% residual activity at 5 mM
Pyrococcus abyssi
Cr3+
5 mM, 40% inhibition; 60% residual activity at 5 mM
Pyrococcus abyssi
dithiothreitol
5 mM, 50% inhibition
Pyrococcus abyssi
DTNB
5 mM, complete inhibition
Pyrococcus abyssi
ethanol
57% inhibition at 30%, complete inhibition at 50%; complete inhibition at 50% ethanol
Pyrococcus abyssi
ethylene glycol
80% inhibition at 50%; 80% inhibition at 50% ethylene glycol
Pyrococcus abyssi
Fe2+
40% residual activity at 5 mM; 5 mM, 60% inhibition
Pyrococcus abyssi
Hg2+
1 mM, complete inhibition; complete inhibition at 1 mM
Pyrococcus abyssi
iodacetamide
complete inhibition at 5 mM
Pyrococcus abyssi
iodacetate
complete inhibition at 5 mM
Pyrococcus abyssi
iodoacetamide
5 mM, complete inhibition
Pyrococcus abyssi
iodoacetate
5 mM, complete inhibition
Pyrococcus abyssi
L-Cys
5 mM, 27% inhibition
Pyrococcus abyssi
Malononitrile
concentrations above 12 mM have a strong inhibitory effect; strong inhibition at 12 mM
Pyrococcus abyssi
methanol
complete inhibition at 30%; complete inhibition at 30% methanol
Pyrococcus abyssi
additional information
EDTA and NaN3 have no influence on activity
Pyrococcus abyssi
p-chloromercuribenzoate
complete inhibition at 1 mM
Pyrococcus abyssi
p-hydroxymercuribenzoate
1 mM, complete inhibition; complete inhibition at 1 mM
Pyrococcus abyssi
PCMB
1 mM, complete inhibition
Pyrococcus abyssi
phenyl hydrazine
53% residual activity at 5 mM; 5 mM, 47% inhibition
Pyrococcus abyssi
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.47
-
Malononitrile
in 20 mM potassium phosphate, pH 7.4, with 1 mM dithiothreitol, at 80°C; pH 7.4, 80°C
Pyrococcus abyssi
9.48
-
Fumaronitrile
in 20 mM potassium phosphate, pH 7.4, with 1 mM dithiothreitol, at 80°C; pH 7.4, 80°C
Pyrococcus abyssi
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
intracellular
-
Pyrococcus abyssi
5622
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29800
-
2 * 29800, gel filtration
Pyrococcus abyssi
30000
-
2 * 30000, SDS-PAGE
Pyrococcus abyssi
59800
-
gel filtration
Pyrococcus abyssi
60000
-
gel filtration; SDS-PAGE
Pyrococcus abyssi
Purification (Commentary) (protein specific)
Commentary
Organism
; Q-Sepharose Fast Flow column chromatography and Sephadex PD-10 column gel filtration
Pyrococcus abyssi
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00595
-
recombinant enzyme from crude extract
Pyrococcus abyssi
0.1419
-
recombinant enzyme after 23.85fold purification
Pyrococcus abyssi
141.9
-
-
Pyrococcus abyssi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fumaronitrile + H2O
-
670792
Pyrococcus abyssi
fumaric acid + NH3
-
-
-
?
fumaronitrile + H2O
preferred substrate
670792
Pyrococcus abyssi
fumaric acid + NH3
-
-
-
?
fumaronitrile + H2O
-
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
fumaric acid + NH3
-
-
-
?
fumaronitrile + H2O
preferred substrate
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
fumaric acid + NH3
-
-
-
?
malononitrile + H2O
-
670792
Pyrococcus abyssi
malonic acid + NH3
-
-
-
?
malononitrile + H2O
preferred substrate
670792
Pyrococcus abyssi
malonic acid + NH3
-
-
-
?
malononitrile + H2O
-
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
malonic acid + NH3
-
-
-
?
malononitrile + H2O
preferred substrate
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
malonic acid + NH3
-
-
-
?
additional information
compounds with a nitrile group bound to an aromatic ring or amino acid are not hydrolyzed by recombinant nitrilase
670792
Pyrococcus abyssi
?
-
-
-
-
additional information
compounds with a nitrile group bound to an aromatic ring or amino acid are not hydrolyzed by recombinant nitrilase
670792
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 30000, SDS-PAGE
Pyrococcus abyssi
homodimer
2 * 29800, gel filtration; 2 * 30000, SDS-PAGE
Pyrococcus abyssi
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
80
-
-
Pyrococcus abyssi
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
90
-
Pyrococcus abyssi
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
90
the recombinant enzyme is highly thermostable with a half-life of 25 h at 70°C, 9 h at 80°C, and 6 h at 90°C
Pyrococcus abyssi
70
-
25 h, recombinant enzyme loses about 50% of maximal activity
Pyrococcus abyssi
80
-
half-life: 9 h
Pyrococcus abyssi
90
-
half-life: 6 h
Pyrococcus abyssi
113
-
Tm-value: 112.7°C
Pyrococcus abyssi
120
-
irreversible denaturation after heating to 120°C
Pyrococcus abyssi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
-
Pyrococcus abyssi
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
8
-
Pyrococcus abyssi
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Pyrococcus abyssi
isoelectric focusing
-
5.3
Other publictions for EC 3.5.5.7
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)
733526
Fang
Enzymatic degradation of aliph ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous BX2
Biores. Technol.
185
28-34
2015
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733919
Yusuf
Cloning and functional charact ...
Fusarium proliferatum, Fusarium proliferatum AUF-2
Funct. Integr. Genomics
15
413-424
2015
1
-
1
-
-
-
12
1
-
6
1
-
-
2
-
-
1
-
-
-
-
-
22
1
1
1
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
12
-
1
-
6
1
-
-
-
-
1
-
-
-
-
22
1
1
1
-
-
1
-
-
-
-
-
-
-
-
-
734577
Zhang
Structural insights into enzym ...
Synechocystis sp.
J. Struct. Biol.
188
93-101
2014
-
-
1
1
25
-
-
18
-
-
-
-
-
1
-
-
1
-
-
-
18
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
-
1
-
1
25
-
-
-
-
18
-
-
-
-
-
-
-
1
-
-
18
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
18
18
735340
Wang
A novel nitrilase from Rhodoba ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides LHS-305
World J. Microbiol. Biotechnol.
30
245-252
2014
-
-
1
-
-
-
9
1
-
-
2
-
-
2
-
-
1
-
-
-
-
-
19
1
1
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
9
-
1
-
-
2
-
-
-
-
1
-
-
-
-
19
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
710984
Bayer
A nitrilase from a metagenomic ...
uncultured bacterium
Appl. Microbiol. Biotechnol.
89
91-98
2011
-
-
1
-
-
-
4
1
-
-
2
-
-
2
-
-
1
-
-
-
-
-
13
1
1
-
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
1
-
-
2
-
-
-
-
1
-
-
-
-
13
1
1
-
1
-
1
1
-
-
-
-
-
-
1
1
718661
He
A high-throughput screening st ...
Alcaligenes sp., Alcaligenes sp. ECU0401, Rhodococcus erythropolis, Rhodococcus erythropolis CGMCC 1.2362
Appl. Microbiol. Biotechnol.
89
817-823
2011
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
2
-
12
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
12
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
695831
Kim
Identification and characteriz ...
Pseudomonas fluorescens, Pseudomonas fluorescens Pf-5
Appl. Microbiol. Biotechnol.
83
273-283
2009
-
-
1
-
-
-
6
7
-
-
2
-
-
5
-
-
-
-
-
-
2
-
13
1
1
-
5
7
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
6
-
7
-
-
2
-
-
-
-
-
-
-
2
-
13
1
1
-
5
7
1
-
-
1
-
-
-
-
-
-
699065
Nigam
Nitrilase-catalysed conversion ...
Streptomyces sp.
J. Biosci.
34
21-26
2009
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712260
Thuku
Microbial nitrilases: Versatil ...
Acidovorax facilis, Acidovorax facilis 72W, Acinetobacter sp., Acinetobacter sp. AK226, Comamonas testosteroni, Pseudomonas sp., Pseudomonas sp. S1, Pyrococcus abyssi, Rhodococcus rhodochrous, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Synechocystis sp.
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29
8
7
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7
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712870
Sharma
-
In silico analysis of amino ac ...
Bradyrhizobium sp., Bradyrhizobium sp. ORS278, Methylibium petroleiphilum, Pseudomonas syringae pv. syringae, Rhodococcus rhodochrous, Rhodococcus rhodochrous J1, Rhodococcus rhodochrous K22, Synechococcus elongatus
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2009
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6
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685014
Yeom
A determinant residue of subst ...
Rhodococcus rhodochrous
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2008
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1
1
16
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31
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32
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25
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32
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13
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9
1
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32
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695708
Luo
Gene cloning, overexpression, ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous tg1-A6
Appl. Biochem. Biotechnol.
160
393-400
2008
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1
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10
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1
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-
1
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687941
Khandelwal
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Optimization of nitrilase prod ...
Streptomyces sp., Streptomyces sp. MTCC 7546
J. Chem. Technol. Biotechnol.
82
646-651
2007
2
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20
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1
1
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1
1
1
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670463
Bergeron
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Nitrilase-catalyzed desymmetri ...
Pseudomonas fluorescens
Org. Proc. Res. Dev.
10
661-665
2006
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1
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670792
Mueller
Cloning, overexpression, and c ...
no activity in Aeropyrum pernix, no activity in Pyrococcus furiosus, no activity in Pyrococcus horikoshii, Pyrococcus abyssi, Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Protein Expr. Purif.
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672-681
2006
4
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1
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24
2
1
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4
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6
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1
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3
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2
1
1
6
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1
1
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4
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1
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24
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2
1
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4
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1
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3
-
10
2
1
1
6
-
1
1
-
1
-
-
-
-
-
-
685425
Holtze
Transformation of the herbicid ...
Pseudomonas fluorescens 11387, Pseudomonas fluorescens, Pseudomonas putida 11388, Pseudomonas putida, Rhizobium sp. 11401, Rhizobium sp.
Biodegradation
17
503-510
2006
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6
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686545
Mukherjee
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Exploring the synthetic applic ...
Synechocystis sp.
Eur. J. Org. Chem.
23
5238-5242
2006
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1
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1
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8
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670922
Hann
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Regioselective biocatalytic hy ...
Acidovorax facilis, Acidovorax facilis 72W
Tetrahedron
60
577-581
2004
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8
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2
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654298
Chauhan
Purification, cloning, sequenc ...
Acidovorax facilis, Acidovorax facilis 72W
Appl. Microbiol. Biotechnol.
61
118-122
2003
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1
1
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1
1
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2
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655310
Brenner
Catalysis in the nitrilase sup ...
Arabidopsis thaliana, Rhodococcus rhodochrous
Curr. Opin. Struct. Biol.
12
775-782
2002
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655149
Dias
Enzymatic degradation of nitri ...
Meyerozyma guilliermondii, Meyerozyma guilliermondii UFMG-Y65
Can. J. Microbiol.
46
525-531
2000
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2
1
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20
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26
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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
20
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26
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1
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1
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1
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209747
Dhillon
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Transformation of aliphatic an ...
Pseudomonas sp., Pseudomonas sp. S1
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811-815
1999
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1
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1
1
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1
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6
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1
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1
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15
1
1
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1
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32507
Levy-Schil
Aliphatic nitrilase from a soi ...
Comamonas testosteroni
Gene
161
15-20
1995
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1
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5
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1
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6
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32505
Kobayashi
Primary structure of an alipha ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous K22
Biochemistry
31
9000-9007
1992
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2
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1
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6
1
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32506
Kobayashi
Purification and characterizat ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous K22
J. Bacteriol.
172
4807-4815
1990
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3
2
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3
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1
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1
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63
2
1
1
7
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1
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2
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3
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2
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1
3
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1
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1
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63
2
1
1
7
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1
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2
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