3.5.5.7: Aliphatic nitrilase
This is an abbreviated version!
For detailed information about Aliphatic nitrilase, go to the full flat file.
Word Map on EC 3.5.5.7
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3.5.5.7
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rhodococcus
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enantioselectivity
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erythropolis
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synthesis
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dinitriles
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acetamide
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rhodochrous
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industry
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mononitriles
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microbacterium
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arylaliphatic
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nitrile-degrading
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environmental protection
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biotechnology
- 3.5.5.7
- rhodococcus
-
enantioselectivity
- erythropolis
- synthesis
-
dinitriles
- acetamide
- rhodochrous
- industry
-
mononitriles
- microbacterium
-
arylaliphatic
-
nitrile-degrading
- environmental protection
- biotechnology
Reaction
Synonyms
BjNIT3397, cyanoalanine hydratase/nitrilase, More, NIT, NIT1, Nit4, NitA, nitC1, nitC2, NitPf5, nitrilase, nitrile hydratase/amidase, PaCNit, REH16
ECTree
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Engineering
Engineering on EC 3.5.5.7 - Aliphatic nitrilase
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F168V/L201N
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the mutant shows increased activity and specificity compared to the wild type enzyme
L201Q
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the mutant shows increased activity and specificity compared to the wild type enzyme
F168V/L201N
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the mutant shows increased activity and specificity compared to the wild type enzyme
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L201Q
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the mutant shows increased activity and specificity compared to the wild type enzyme
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Y141A
the mutant enzyme is still active and converted the aliphatic (valeronitrile) and the aromatic substrate (2-phenylpropionitrile) with similar relative activities as the wild-type enzyme
Y141W
the mutant enzyme converts valeronitrile with a much higher relative activity than 2-phenylpropionitrile
Y141A
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the mutant enzyme is still active and converted the aliphatic (valeronitrile) and the aromatic substrate (2-phenylpropionitrile) with similar relative activities as the wild-type enzyme
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Y141W
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the mutant enzyme converts valeronitrile with a much higher relative activity than 2-phenylpropionitrile
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C170A
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mutant enzymes Cys170Ala and Cys170Ser show no catalytic activity
C170S
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mutant enzymes Cys170Ala and Cys170Ser show no catalytic activity
K9A
L79A
R129A
Y142A
Y142F
Y142I
Y142L
Y142S
Y175A
C170A
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mutant enzymes Cys170Ala and Cys170Ser show no catalytic activity
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C170S
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mutant enzymes Cys170Ala and Cys170Ser show no catalytic activity
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W146F
the mutant shows reduced activity compared to the wild type enzyme
W146H
the mutant shows reduced activity compared to the wild type enzyme
W146Y
the mutant shows reduced activity compared to the wild type enzyme
additional information
mutant exhibits slightly higher kcat/Km values for aromatic nitriles and shows no activity toward aliphatic nitriles
Y142F
mutant shows slightly lower kcat/Km values compared to the wild type enzyme
mutant exhibits slightly higher kcat/Km values for aromatic nitriles and shows no activity toward aliphatic nitriles
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mutants containing charged amino acids such as aspartate, glutamate, arginine and asparagine at position 142 display no activity towards any nitrile, possibly owing to the disruption of hydrophobic interactions with substrates
additional information
mutants containing charged amino acids such as aspartate, glutamate, arginine and asparagine at position 142 display no activity towards any nitrile, possibly owing to the disruption of hydrophobic interactions with substrates