Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.5.5.5: Arylacetonitrilase

This is an abbreviated version!
For detailed information about Arylacetonitrilase, go to the full flat file.

Word Map on EC 3.5.5.5

Reaction

4-Chlorophenylacetonitrile
+ 2 H2O =
4-chlorophenylacetate
 +
NH3

Synonyms

Arylacetonitrilase, arylacetonitrile-hydrolyzing nitrilase, arylacetonitrile-specific nitrilase, blr3397, enantioselective arylacetonitrilase, GPnor51, NIT, NitA, NitAd, NitAk2, NitAn, NitMp, NitP, nitrilase, nitrilase PpL19, Nitrilase, arylaceto-, NitTv

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.5 In nitriles
                3.5.5.5 Arylacetonitrilase

Engineering

Engineering on EC 3.5.5.5 - Arylacetonitrilase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C163G
-
site-directed mutagenesis
E47Q
-
site-directed mutagenesis
K129I
-
site-directed mutagenesis
C163G
-
site-directed mutagenesis
-
E47Q
-
site-directed mutagenesis
-
K129I
-
site-directed mutagenesis
-
H165N
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
W163A
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
H165N
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
-
W163A
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
-
H170N
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
W168A
the mutant forms significantly increases amounts of mandelamide and 2-phenylpropionamide and demonstrates an almost complete inversion of enantioselectivity for the conversion of (R,S)-2-phenylpropionitrile (from R- to S-selectivity)
H170N
-
the mutant exhibits a decreased activity for (R,S)-2-phenylpropionitrile compared to the wild type enzyme
-
W168A
-
the mutant forms significantly increases amounts of mandelamide and 2-phenylpropionamide and demonstrates an almost complete inversion of enantioselectivity for the conversion of (R,S)-2-phenylpropionitrile (from R- to S-selectivity)
-
A114F
-
inactive
A116C
-
the mutant shows activity similar to the wild type enzyme
A116F
-
the mutant shows about 50% of wild type activity
A165E
mutant with very low activities toward (R,S)-mandelonitrile and substrate (R,S)-2-phenylpropionitrile
A165F
A165G
the mutant forms 4.3% amide and thus produces significantly more amide than the wild type enzyme with the substrate (R,S)-2-phenylpropionitrile
A165H
the mutant enzyme shows a significantly increased relative activity for mandelonitrile (compared to (R,S)-2-phenylpropionitrile)
A165R
mutant with very low activities toward (R,S)-mandelonitrile and substrate (R,S)-2-phenylpropionitrile
A165W
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids
A165Y
the mutant enzyme converts racemic mandelonitrile and (R,S)-2-phenylpropionitrile to increased amounts of the R enantiomers of the corresponding acids
C163A
-
the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid
C163N
-
the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates
C163N/A165R
-
the mutant demonstrates increased amide formation capacity in comparison to the mutants carrying only single mutations
C163N/W110I
-
the mutant enzyme forms about 100fold more 2-phenylpropionamide (in relation to the total amount of (R,S)-2-phenylpropionitrile converted) than the wild type, although the relative activity of this mutant for the conversion (R,S)-2-phenylpropionitrile to 2-phenylpropionic acid is only 4% of that observed for the wild type
C163Q
-
the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates
C163S
-
the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid
C164A
the mutant is devoid of nitrilase activity with the substrate (R,S)-2-phenylpropionitrile
E137A
-
the mutant demonstrates less than 1% of the wild type activity but is still enzymatically competent to convert mandelonitrile to mandelic acid and mandeloamide
G109F
-
inactive
I117F
-
the mutant shows about 50% of wild type activity
L111F
-
the mutant shows about 50% of wild type activity
L113F
-
the mutant shows activity similar to the wild type enzyme
Tyr54C
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Tyr54P
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Tyr54V
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
W110F
-
the mutant shows activity similar to the wild type enzyme
W188K
the mutant enzyme produces almost exclusively phenylglycine amide from (R,S)-phenylglycinonitrile. In comparison to the wild type, there is an increase in the ee-value of the formed (S)-phenylglycine amide
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
Y54A
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54F
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54H
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
Y54L
-
mutant with significantly reduced activity compared to the wild type enzyme
Y54M
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
A165F
-
decreased degree of amide formation compared to the wild type enzyme and forms about 3% phenylglycine amide from (R,S)-phenylglycinonitrile. In contrast to the wild-type enzyme, the variant almost exclusively forms (R)-phenylglycine. This point mutation results in an almost complete stereoinversion of the reaction
-
E137A
-
the mutant demonstrates less than 1% of the wild type activity but is still enzymatically competent to convert mandelonitrile to mandelic acid and mandeloamide
-
W188K
-
the mutant enzyme produces almost exclusively phenylglycine amide from (R,S)-phenylglycinonitrile. In comparison to the wild type, there is an increase in the ee-value of the formed (S)-phenylglycine amide
-
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
-
Y54A
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
-
Y54F
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
-
Y54H
-
the mutant shows wild type activity but forms significantly decreased relative amounts of atrolactamide from 2-hydroxy-2-phenylpropionitrile
-
Y54I
-
inactive
-
Y54K
-
inactive
-
A136Y
-
mutant enzyme shows reversed selectivity and preferentially produces (R)-mandelic acid with an enantiomeric excess values of 66.7%
A136Y/I168Y
-
mutant enzyme produces (R)-mandelic acid with an enantiomeric excess value of 89.7%, an R-enantioselectivity higher than that obtained with the single mutations A136Y and I168Y
A136Y/I168Y/M113G
-
mutant enzyme with R-selectivity, 90.9% enantiomeric excess
I168Y
-
mutant enzyme shows reversed selectivity and preferentially produces (R)-mandelic acid with an enantiomeric excess values of 74.3%
M113C
-
mutation enhances the S-enantioselectivity of the enzyme toward mandelonitrile
M113G/A136Y/I168Y
-
R-selectivity toward mandelonitrile with 90.1% enantiomeric excess
M113L/R128H
-
S-selectivity toward mandelonitrile with 91.1% enantiomeric excess
M113Q
-
mutation enhances the S-enantioselectivity of the enzyme toward mandelonitrile
R128E
-
mutant displays no activity toward mandelonitrile
R128H
-
mutation enhances the S-enantioselectivity of the enzyme toward mandelonitrile
R128K
-
mutant demonstrates low enantioselectivity (44.9% enantiomeric excess) as compared with the wild-type enzyme (52.7% enantiomeric excess)
A136Y
-
mutant enzyme shows reversed selectivity and preferentially produces (R)-mandelic acid with an enantiomeric excess values of 66.7%
-
I168Y
-
mutant enzyme shows reversed selectivity and preferentially produces (R)-mandelic acid with an enantiomeric excess values of 74.3%
-
M113Q
-
mutation enhances the S-enantioselectivity of the enzyme toward mandelonitrile
-
R128H
-
mutation enhances the S-enantioselectivity of the enzyme toward mandelonitrile
-
R128K
-
mutant demonstrates low enantioselectivity (44.9% enantiomeric excess) as compared with the wild-type enzyme (52.7% enantiomeric excess)
-
additional information