BRENDA - Enzyme Database show
show all sequences of 3.5.5.7

Structural insights into enzymatic activity and substrate specificity determination by a single amino acid in nitrilase from Synechocystis sp. PCC6803

Zhang, L.; Yin, B.; Wang, C.; Jiang, S.; Wang, H.; Yuan, Y.A.; Wei, D.; J. Struct. Biol. 188, 93-101 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Synechocystis sp.
Crystallization (Commentary)
Crystallization
Organism
vapor diffusion method, using 15% (w/v) PEG 5000MME, 1 mM dithiothreitol, 3% tascimate and 100 mM HEPES, pH 6.8
Synechocystis sp.
Engineering
Amino acid exchange
Commentary
Organism
C169A
inactive
Synechocystis sp.
E142A
inactive
Synechocystis sp.
E53A
inactive
Synechocystis sp.
K135A
inactive
Synechocystis sp.
N118A
inactive
Synechocystis sp.
W146A
inactive
Synechocystis sp.
W146C
inactive
Synechocystis sp.
W146D
inactive
Synechocystis sp.
W146E
inactive
Synechocystis sp.
W146F
the mutant shows reduced activity compared to the wild type enzyme
Synechocystis sp.
W146G
inactive
Synechocystis sp.
W146H
the mutant shows reduced activity compared to the wild type enzyme
Synechocystis sp.
W146I
inactive
Synechocystis sp.
W146K
inactive
Synechocystis sp.
W146L
inactive
Synechocystis sp.
W146M
inactive
Synechocystis sp.
W146N
inactive
Synechocystis sp.
W146P
inactive
Synechocystis sp.
W146Q
inactive
Synechocystis sp.
W146R
inactive
Synechocystis sp.
W146S
inactive
Synechocystis sp.
W146T
inactive
Synechocystis sp.
W146V
inactive
Synechocystis sp.
W146Y
the mutant shows reduced activity compared to the wild type enzyme
Synechocystis sp.
Y59A
inactive
Synechocystis sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.98
-
Benzonitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
1.13
-
2-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
1.21
-
Benzonitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.26
-
2-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.26
-
Benzonitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.3
-
2-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.33
-
Benzonitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.47
-
2-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
3.16
-
3-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
3.2
-
3-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
3.94
-
3-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
4.41
-
3-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
7.95
-
2-butenenitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
9.01
-
Fumaronitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
9.16
-
2-butenenitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
10.77
-
Fumaronitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
11.06
-
Fumaronitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
11.45
-
Fumaronitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechocystis sp.
Q55949
-
-
Purification (Commentary)
Commentary
Organism
Ni2+ affinity column chromatography and Superdex 75 gel filtration
Synechocystis sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.05
-
mutant enzyme W146F, with 2-butenenitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
0.29
-
wild type enzyme, with 2-butenenitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
0.68
-
wild type enzyme, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
0.97
-
wild type enzyme, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1
-
mutant enzyme W146F, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.18
-
mutant enzyme W146Y, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.47
-
mutant enzyme W146H, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.57
-
mutant enzyme W146Y, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.6
-
mutant enzyme W146F, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.69
-
mutant enzyme W146Y, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.82
-
mutant enzyme W146H, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.85
-
mutant enzyme W146F, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.95
-
mutant enzyme W146H, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
2.7
-
wild type enzyme, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
2.72
-
mutant enzyme W146H, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
2.93
-
mutant enzyme W146F, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
3.08
-
mutant enzyme W146Y, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
3.2
-
wild type enzyme, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-butenenitrile + H2O
worst substrate
734577
Synechocystis sp.
2-butenic acid + NH3
-
-
-
?
2-cyanopyridine + H2O
second best substrate
734577
Synechocystis sp.
?
-
-
-
?
3-cyanopyridine + H2O
-
734577
Synechocystis sp.
?
-
-
-
?
benzonitrile + H2O
-
734577
Synechocystis sp.
benzoate + NH3
-
-
-
?
fumaronitrile + H2O
best substrate
734577
Synechocystis sp.
fumarate + NH3
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.03
-
2-butenenitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.19
-
2-butenenitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.45
-
3-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.65
-
Benzonitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.67
-
Benzonitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.79
-
Benzonitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.98
-
Benzonitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.07
-
3-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.13
-
3-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
1.21
-
3-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.8
-
2-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.81
-
2-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.95
-
2-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
2.05
-
2-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
7.42
-
Fumaronitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
8.75
-
Fumaronitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
9.22
-
Fumaronitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
15.13
-
Fumaronitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Synechocystis sp.
Crystallization (Commentary) (protein specific)
Crystallization
Organism
vapor diffusion method, using 15% (w/v) PEG 5000MME, 1 mM dithiothreitol, 3% tascimate and 100 mM HEPES, pH 6.8
Synechocystis sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C169A
inactive
Synechocystis sp.
E142A
inactive
Synechocystis sp.
E53A
inactive
Synechocystis sp.
K135A
inactive
Synechocystis sp.
N118A
inactive
Synechocystis sp.
W146A
inactive
Synechocystis sp.
W146C
inactive
Synechocystis sp.
W146D
inactive
Synechocystis sp.
W146E
inactive
Synechocystis sp.
W146F
the mutant shows reduced activity compared to the wild type enzyme
Synechocystis sp.
W146G
inactive
Synechocystis sp.
W146H
the mutant shows reduced activity compared to the wild type enzyme
Synechocystis sp.
W146I
inactive
Synechocystis sp.
W146K
inactive
Synechocystis sp.
W146L
inactive
Synechocystis sp.
W146M
inactive
Synechocystis sp.
W146N
inactive
Synechocystis sp.
W146P
inactive
Synechocystis sp.
W146Q
inactive
Synechocystis sp.
W146R
inactive
Synechocystis sp.
W146S
inactive
Synechocystis sp.
W146T
inactive
Synechocystis sp.
W146V
inactive
Synechocystis sp.
W146Y
the mutant shows reduced activity compared to the wild type enzyme
Synechocystis sp.
Y59A
inactive
Synechocystis sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.98
-
Benzonitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
1.13
-
2-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
1.21
-
Benzonitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.26
-
2-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.26
-
Benzonitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.3
-
2-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.33
-
Benzonitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.47
-
2-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
3.16
-
3-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
3.2
-
3-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
3.94
-
3-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
4.41
-
3-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
7.95
-
2-butenenitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
9.01
-
Fumaronitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
9.16
-
2-butenenitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
10.77
-
Fumaronitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
11.06
-
Fumaronitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
11.45
-
Fumaronitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
Purification (Commentary) (protein specific)
Commentary
Organism
Ni2+ affinity column chromatography and Superdex 75 gel filtration
Synechocystis sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.05
-
mutant enzyme W146F, with 2-butenenitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
0.29
-
wild type enzyme, with 2-butenenitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
0.68
-
wild type enzyme, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
0.97
-
wild type enzyme, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1
-
mutant enzyme W146F, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.18
-
mutant enzyme W146Y, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.47
-
mutant enzyme W146H, with benzonitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.57
-
mutant enzyme W146Y, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.6
-
mutant enzyme W146F, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.69
-
mutant enzyme W146Y, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.82
-
mutant enzyme W146H, with 3-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.85
-
mutant enzyme W146F, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
1.95
-
mutant enzyme W146H, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
2.7
-
wild type enzyme, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
2.72
-
mutant enzyme W146H, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
2.93
-
mutant enzyme W146F, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
3.08
-
mutant enzyme W146Y, with 2-cyanopyridine as substrate, at pH 7.0 and 30°C
Synechocystis sp.
3.2
-
wild type enzyme, with fumaronitrile as substrate, at pH 7.0 and 30°C
Synechocystis sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-butenenitrile + H2O
worst substrate
734577
Synechocystis sp.
2-butenic acid + NH3
-
-
-
?
2-cyanopyridine + H2O
second best substrate
734577
Synechocystis sp.
?
-
-
-
?
3-cyanopyridine + H2O
-
734577
Synechocystis sp.
?
-
-
-
?
benzonitrile + H2O
-
734577
Synechocystis sp.
benzoate + NH3
-
-
-
?
fumaronitrile + H2O
best substrate
734577
Synechocystis sp.
fumarate + NH3
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.03
-
2-butenenitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.19
-
2-butenenitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.45
-
3-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.65
-
Benzonitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.67
-
Benzonitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.79
-
Benzonitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.98
-
Benzonitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.07
-
3-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.13
-
3-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
1.21
-
3-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.8
-
2-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.81
-
2-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.95
-
2-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
2.05
-
2-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
7.42
-
Fumaronitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
8.75
-
Fumaronitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
9.22
-
Fumaronitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
15.13
-
Fumaronitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00328
-
2-butenenitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.0239
-
2-butenenitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.141
-
3-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.243
-
3-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.307
-
3-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
0.357
-
3-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.531
-
Benzonitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.537
-
Benzonitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.689
-
Fumaronitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.737
-
Benzonitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
0.764
-
Fumaronitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.806
-
Benzonitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.834
-
Fumaronitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.224
-
2-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.392
-
2-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.548
-
2-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.679
-
Fumaronitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.814
-
2-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00328
-
2-butenenitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.0239
-
2-butenenitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.141
-
3-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.243
-
3-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.307
-
3-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
0.357
-
3-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.531
-
Benzonitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.537
-
Benzonitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
0.689
-
Fumaronitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.737
-
Benzonitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
0.764
-
Fumaronitrile
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
0.806
-
Benzonitrile
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
0.834
-
Fumaronitrile
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.224
-
2-Cyanopyridine
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.392
-
2-Cyanopyridine
mutant enzyme W146H, at pH 7.0 and 30°C
Synechocystis sp.
1.548
-
2-Cyanopyridine
mutant enzyme W146F, at pH 7.0 and 30°C
Synechocystis sp.
1.679
-
Fumaronitrile
wild type enzyme, at pH 7.0 and 30°C
Synechocystis sp.
1.814
-
2-Cyanopyridine
mutant enzyme W146Y, at pH 7.0 and 30°C
Synechocystis sp.
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
-
-
-
-
-
-
-
-
-
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2
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8
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-
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
-
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2
-
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1
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-
-
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22
1
1
1
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-
1
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1
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1
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12
-
1
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6
1
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1
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-
-
22
1
1
1
-
-
1
-
-
-
-
-
-
-
-
-
734577
Zhang
Structural insights into enzym ...
Synechocystis sp.
J. Struct. Biol.
188
93-101
2014
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-
1
1
25
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-
18
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1
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1
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18
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5
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18
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1
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1
25
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18
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1
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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
-
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9
1
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2
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2
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1
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19
1
1
1
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1
1
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1
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-
-
-
-
9
-
1
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2
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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
-
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1
-
-
-
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13
1
1
-
1
-
1
1
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-
-
-
-
-
-
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
-
-
-
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-
-
-
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5
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2
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12
-
2
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2
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-
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-
-
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-
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-
-
-
-
-
-
-
-
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.
J. Appl. Microbiol.
106
703-727
2009
1
2
-
-
3
-
-
-
-
-
14
-
-
22
-
-
-
-
-
-
-
-
29
8
7
-
-
-
7
-
-
-
-
-
-
1
2
-
-
-
3
-
-
-
-
-
-
-
14
-
-
-
-
-
-
-
-
-
29
8
7
-
-
-
7
-
-
-
-
-
-
-
-
-
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
J. Proteomics Bioinform.
2
185-192
2009
-
-
-
-
-
-
-
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6
-
-
27
-
-
-
-
-
-
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-
-
-
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-
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6
-
-
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-
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-
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6
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
685014
Yeom
A determinant residue of subst ...
Rhodococcus rhodochrous
Biochem. J.
415
401-407
2008
-
-
1
1
16
-
-
31
-
-
1
-
1
2
-
-
1
1
-
-
13
-
9
1
-
-
-
32
-
-
-
-
-
-
-
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1
-
1
25
-
-
-
-
32
-
-
1
-
1
-
-
1
-
-
13
-
9
1
-
-
-
32
-
-
-
-
-
-
-
-
-
-
695708
Luo
Gene cloning, overexpression, ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous tg1-A6
Appl. Biochem. Biotechnol.
160
393-400
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
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10
-
1
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-
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1
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-
-
-
-
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-
1
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
10
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
687941
Khandelwal
-
Optimization of nitrilase prod ...
Streptomyces sp., Streptomyces sp. MTCC 7546
J. Chem. Technol. Biotechnol.
82
646-651
2007
2
-
-
-
-
-
-
-
-
-
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2
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20
-
1
1
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1
1
1
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2
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-
-
-
-
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-
-
-
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-
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-
-
-
-
-
20
-
1
1
-
-
1
1
1
-
-
-
-
-
-
-
670463
Bergeron
-
Nitrilase-catalyzed desymmetri ...
Pseudomonas fluorescens
Org. Proc. Res. Dev.
10
661-665
2006
-
1
-
-
-
-
-
-
-
-
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1
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1
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-
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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.
47
672-681
2006
4
-
1
-
-
-
24
2
1
-
4
-
-
6
-
-
1
-
-
-
3
-
10
2
1
1
6
-
1
1
-
-
-
1
-
4
-
1
-
-
-
-
-
24
-
2
1
-
4
-
-
-
-
1
-
-
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
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
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6
-
-
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-
-
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-
-
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-
-
-
-
-
-
-
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-
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-
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-
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-
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6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
686545
Mukherjee
-
Exploring the synthetic applic ...
Synechocystis sp.
Eur. J. Org. Chem.
23
5238-5242
2006
-
-
1
-
-
-
-
-
-
-
-
-
-
1
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-
1
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-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670922
Hann
-
Regioselective biocatalytic hy ...
Acidovorax facilis, Acidovorax facilis 72W
Tetrahedron
60
577-581
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654298
Chauhan
Purification, cloning, sequenc ...
Acidovorax facilis, Acidovorax facilis 72W
Appl. Microbiol. Biotechnol.
61
118-122
2003
-
1
1
-
-
-
-
-
-
-
-
-
-
10
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655310
Brenner
Catalysis in the nitrilase sup ...
Arabidopsis thaliana, Rhodococcus rhodochrous
Curr. Opin. Struct. Biol.
12
775-782
2002
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
2
-
-
-
-
3
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
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-
-
-
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-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655149
Dias
Enzymatic degradation of nitri ...
Meyerozyma guilliermondii, Meyerozyma guilliermondii UFMG-Y65
Can. J. Microbiol.
46
525-531
2000
-
2
1
-
-
-
1
-
1
-
-
-
-
2
-
-
-
-
-
1
20
-
26
-
1
-
1
-
1
-
-
-
-
-
1
-
2
1
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
1
20
-
26
-
1
-
1
-
1
-
-
-
-
-
-
-
-
-
209747
Dhillon
-
Transformation of aliphatic an ...
Pseudomonas sp., Pseudomonas sp. S1
Can. J. Microbiol.
45
811-815
1999
-
-
-
-
-
-
-
6
-
-
1
-
-
3
-
-
1
1
-
-
1
-
15
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
1
-
-
-
-
1
-
-
1
-
15
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
32507
Levy-Schil
Aliphatic nitrilase from a soi ...
Comamonas testosteroni
Gene
161
15-20
1995
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
1
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
32505
Kobayashi
Primary structure of an alipha ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous K22
Biochemistry
31
9000-9007
1992
-
-
1
-
2
-
-
-
-
-
1
-
-
10
-
-
1
-
-
-
-
-
6
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
6
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
32506
Kobayashi
Purification and characterizat ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous K22
J. Bacteriol.
172
4807-4815
1990
-
-
-
-
-
-
3
2
-
1
3
-
-
6
-
-
1
-
-
-
1
-
63
2
1
1
7
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
3
-
2
-
1
3
-
-
-
-
1
-
-
1
-
63
2
1
1
7
-
1
-
2
-
-
-
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