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
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Application
Application on EC 3.5.5.7 - Aliphatic nitrilase
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biotechnology
environmental protection
industry
synthesis
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enzyme can be recombinantly produced in high yield and at mild reaction conditions, the robust enzyme can be a suitable biocatalyst for industrial applications
biotechnology
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enzyme can be recombinantly produced in high yield and at mild reaction conditions, the robust enzyme can be a suitable biocatalyst for industrial applications
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Candida guilliermondii UFMG-Y65 might be useful for the bioremediation of environments contaminated with nitriles
environmental protection
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Candida guilliermondii UFMG-Y65 might be useful for the bioremediation of environments contaminated with nitriles
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the enzyme is engineered for the commercial production of 3-hydroxyvaleric acid
industry
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
industry
the enzyme is a potential candidate for industrial applications for biosynthesis of carboxylic acid
industry
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the enzyme is a promising biocatalyst for mild nitrile hydrolysis
industry
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under optimized conditions, using the fed-batch reaction mode, total of 1050 mM 3-cyanopyridine is hydrolyzed completely in 20.8 h with eight substrate feedings, yielding 129.2 g/l production of nicotinic acid and thus showing a potential for industrial application
industry
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the enzyme is a promising biocatalyst for mild nitrile hydrolysis
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industry
-
the enzyme is engineered for the commercial production of 3-hydroxyvaleric acid
-
industry
-
the high chemical specificity and frequent enantioselectivity of nitrilases makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation
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Candida guilliermondii UFMG-Y65 and the isolated enzyme, respectively, might be useful for the bioproduction of amides and acids
synthesis
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an efficient, scaleable synthesis of ethyl (R)-4-cyano-3-hydroxybutyrate, a potential intermediate in the synthesis of Atorvastatin (Lipitor) involves nitrilase-catalyzed desymmetrization of 3-hydroxyglutaronitrile
synthesis
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biotransformation of acrylonitrile by thermophilic nitrilase from Streptomyces sp. MTCC 7546. Enzyme converts nitriles to acids without the formation of amides. Immobilization of whole cells in agar-agar or beads allows for 25 cycles at 50°C with conversion of 71% of acrylonitrile to acid at 6 h and 100% conversion at 3 h by free cells
synthesis
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the enzyme catalyzes the hydrolysis of 3-aminopropionitrile at high substrate concentration up to 3 M, and optimal pH 7.3 and temperature 30°C. However, with the increase of substrate concentration, 3-aminopropanamide is formed, reaching 33% at the substrate concentration of 3 M. A tandem reaction strategy is developed by introducing the aspartate ammonia-lyase-catalyzed amination of fumarate, which utilizes the by-product ammonia as the amino donor in the formation of aspartic acid. Formation of 3-aminopropanamide is significantly inhibited with its amount being reduced from 33% to 3%. The tandem reaction strategy of removing the byproduct ammonia might offer a possibility of producing x02-alanine and L-aspartic acid in one process if the problem in the separation of these two products was solved
synthesis
the enzyme is a potential candidate for industrial applications for biosynthesis of carboxylic acid
synthesis
-
under optimized conditions, using the fed-batch reaction mode, total of 1050 mM 3-cyanopyridine is hydrolyzed completely in 20.8 h with eight substrate feedings, yielding 129.2 g/l production of nicotinic acid and thus showing a potential for industrial application
synthesis
-
the enzyme catalyzes the hydrolysis of 3-aminopropionitrile at high substrate concentration up to 3 M, and optimal pH 7.3 and temperature 30°C. However, with the increase of substrate concentration, 3-aminopropanamide is formed, reaching 33% at the substrate concentration of 3 M. A tandem reaction strategy is developed by introducing the aspartate ammonia-lyase-catalyzed amination of fumarate, which utilizes the by-product ammonia as the amino donor in the formation of aspartic acid. Formation of 3-aminopropanamide is significantly inhibited with its amount being reduced from 33% to 3%. The tandem reaction strategy of removing the byproduct ammonia might offer a possibility of producing x02-alanine and L-aspartic acid in one process if the problem in the separation of these two products was solved
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synthesis
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Candida guilliermondii UFMG-Y65 and the isolated enzyme, respectively, might be useful for the bioproduction of amides and acids
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