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Literature summary extracted from

  • Shen, J.D.; Cai, X.; Liu, Z.Q.; Zheng, Y.G.
    Nitrilase a promising biocatalyst in industrial applications for green chemistry (2021), Crit. Rev. Biotechnol., 41, 72-93.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases in the near future Rhodococcus rhodochrous
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Acidovorax facilis
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Acinetobacter sp. AK226
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Alcaligenes faecalis
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Alcaligenes sp. ECU0401
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Paenarthrobacter nitroguajacolicus
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Arthrobacter sp. J1
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Bacillus subtilis
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Aeribacillus pallidus
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Bradyrhizobium japonicum
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Brevibacterium sp. R312
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Comamonas testosteroni
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Halomonas sp. IIIMB2797
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Halomonas nitrilica
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Hoeflea phototrophica
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Klebsiella pneumoniae
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Roseibium aggregatum
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Meyerozyma guilliermondii
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Nocardia sp.
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Rhodococcus rhodochrous
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Nocardia globerula
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Pannonibacter carbonis
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Pyrococcus abyssi
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Pseudomonas aeruginosa
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Pseudomonas fluorescens
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Pseudomonas putida
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Rhodococcus erythropolis
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Rhodococcus sp. NDB1165
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Streptomyces sp. MTCC 7546
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Aspergillus niger
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Fusarium solani
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Fusarium oxysporum f. sp. melonis
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Arabidopsis thaliana
3.5.5.1 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Arabis alpina
3.5.5.7 industry nitrilase is a promising biocatalyst in industrial production of various pharmaceuticals and fine chemicals. The combination of gene engineering, enzyme engineering, protein modification, as well as process engineering would be an efficient strategy for significant improvement of the catalytic properties of nitrilases and broadening the range of industrial applications for nitrilases Rhodococcus rhodochrous

Protein Variants

EC Number Protein Variants Comment Organism
3.5.5.1 F168V/L201N/S192F mutant enzyme shows 2.4fold improvement in kcat/Km Acidovorax facilis
3.5.5.1 F168V/T201N/S192F/M191T/F192S mutant enzyme shows 136% improvement in specific activity Acidovorax facilis
3.5.5.1 T201F/Q339K/Q343K mutant enzyme showes about 14fold longer half-life at 45°C Acidovorax facilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.5.1 31000
-
-
 Pannonibacter carbonis
3.5.5.1 45000
-
-
 Rhodococcus rhodochrous
3.5.5.1 60000
-
-
 Pyrococcus abyssi
3.5.5.1 74000
-
-
 Klebsiella pneumoniae
3.5.5.1 80000
-
 dimer Rhodococcus rhodochrous
3.5.5.1 130000
-
-
 Pseudomonas fluorescens
3.5.5.1 138000
-
-
 Pseudomonas fluorescens
3.5.5.1 175000
-
-
 Alcaligenes faecalis
3.5.5.1 340000
-
-
 Bradyrhizobium japonicum
3.5.5.1 376000
-
-
 Alcaligenes sp. ECU0401
3.5.5.1 410000
-
 decamer Rhodococcus rhodochrous
3.5.5.1 412000
-
-
 Pseudomonas putida
3.5.5.1 450000
-
-
 Arabidopsis thaliana
3.5.5.1 455000
-
-
 Bradyrhizobium japonicum
3.5.5.1 460000
-
-
 Alcaligenes faecalis
3.5.5.1 550000
-
-
 Fusarium oxysporum f. sp. melonis
3.5.5.1 550000
-
-
 Fusarium solani
3.5.5.1 560000
-
-
 Nocardia sp.
3.5.5.1 560000
-
-
 Rhodococcus rhodochrous
3.5.5.1 570000
-
-
 Acidovorax facilis
3.5.5.1 580000
-
 dodecamer Rhodococcus rhodochrous
3.5.5.1 580000
-
-
 Acinetobacter sp. AK226
3.5.5.1 580000
-
-
 Fusarium solani
3.5.5.1 600000
-
-
 Aeribacillus pallidus
3.5.5.1 650000
-
-
 Aspergillus niger
3.5.5.7 650000
-
-
 Rhodococcus rhodochrous

Organism

EC Number Organism UniProt Comment Textmining
3.5.5.1 Acidovorax facilis
-
-
-
3.5.5.1 Acidovorax facilis ATCC 55746
-
-
-
3.5.5.1 Acinetobacter sp. AK226 P33036
-
-
3.5.5.1 Aeribacillus pallidus
-
-
-
3.5.5.1 Aeribacillus pallidus Dac521
-
-
-
3.5.5.1 Aeribacillus pallidus RAPc8
-
-
-
3.5.5.1 Alcaligenes faecalis
-
-
-
3.5.5.1 Alcaligenes faecalis P20960
-
-
3.5.5.1 Alcaligenes faecalis G8CXY5
-
-
3.5.5.1 Alcaligenes faecalis ATCC 8750
-
-
-
3.5.5.1 Alcaligenes faecalis JM3 P20960
-
-
3.5.5.1 Alcaligenes faecalis MTCC 10757
-
-
-
3.5.5.1 Alcaligenes faecalis ZJUTB10 G8CXY5
-
-
3.5.5.1 Alcaligenes sp. ECU0401 C5IIS9
-
-
3.5.5.1 Arabidopsis thaliana
-
-
-
3.5.5.1 Arabis alpina
-
-
-
3.5.5.1 Arthrobacter sp. J1
-
-
-
3.5.5.1 Aspergillus niger
-
-
-
3.5.5.1 Aspergillus niger K10
-
-
-
3.5.5.1 Bacillus subtilis
-
-
-
3.5.5.1 Bacillus subtilis ZJB-063
-
-
-
3.5.5.1 Bradyrhizobium japonicum
-
-
-
3.5.5.1 Bradyrhizobium japonicum Q89GE3
-
-
3.5.5.1 Bradyrhizobium japonicum USDA110
-
-
-
3.5.5.1 Bradyrhizobium japonicum USDA110 Q89GE3
-
-
3.5.5.1 Brevibacterium sp. R312
-
-
-
3.5.5.1 Comamonas testosteroni
-
-
-
3.5.5.1 Fusarium oxysporum f. sp. melonis
-
-
-
3.5.5.1 Fusarium solani
-
-
-
3.5.5.1 Fusarium solani IMI196840
-
-
-
3.5.5.1 Fusarium solani O1
-
-
-
3.5.5.1 Halomonas nitrilica
-
 sp. nov.
-
3.5.5.1 Halomonas sp. IIIMB2797
-
-
-
3.5.5.1 Hoeflea phototrophica
-
-
-
3.5.5.1 Hoeflea phototrophica DFL-43
-
-
-
3.5.5.1 Klebsiella pneumoniae
-
 subsp. Ozaenae
-
3.5.5.1 Meyerozyma guilliermondii
-
-
-
3.5.5.1 Meyerozyma guilliermondii LM2
-
-
-
3.5.5.1 Nocardia globerula H9NN54
-
-
3.5.5.1 Nocardia globerula NHB-2 H9NN54
-
-
3.5.5.1 Nocardia sp.
-
-
-
3.5.5.1 Paenarthrobacter nitroguajacolicus
-
-
-
3.5.5.1 Paenarthrobacter nitroguajacolicus ZJUTB06-99
-
-
-
3.5.5.1 Pannonibacter carbonis
-
-
-
3.5.5.1 Pannonibacter carbonis Q4.6
-
-
-
3.5.5.1 Pseudomonas aeruginosa
-
-
-
3.5.5.1 Pseudomonas aeruginosa 10145
-
-
-
3.5.5.1 Pseudomonas fluorescens
-
-
-
3.5.5.1 Pseudomonas fluorescens DSM 7155
-
-
-
3.5.5.1 Pseudomonas fluorescens Pf-5
-
-
-
3.5.5.1 Pseudomonas putida
-
-
-
3.5.5.1 Pyrococcus abyssi Q9UYV8
-
-
3.5.5.1 Rhodococcus erythropolis
-
-
-
3.5.5.1 Rhodococcus erythropolis ZJB-0910
-
-
-
3.5.5.1 Rhodococcus rhodochrous
-
-
-
3.5.5.1 Rhodococcus rhodochrous J1
-
-
-
3.5.5.1 Rhodococcus rhodochrous NCIMB 11216
-
-
-
3.5.5.1 Rhodococcus rhodochrous PA-34
-
-
-
3.5.5.1 Rhodococcus sp. NDB1165
-
-
-
3.5.5.1 Roseibium aggregatum
-
-
-
3.5.5.1 Roseibium aggregatum DSM 13394
-
-
-
3.5.5.1 Streptomyces sp. MTCC 7546
-
-
-
3.5.5.7 Rhodococcus rhodochrous Q02068
-
-
3.5.5.7 Rhodococcus rhodochrous K22 Q02068
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.5.1 3-cyanopyridine + 2 H2O
-
 Rhodococcus rhodochrous nicotinic acid + NH3
-
 ?
3.5.5.1 3-cyanopyridine + 2 H2O
-
 Rhodococcus rhodochrous J1 nicotinic acid + NH3
-
 ?
3.5.5.1 3-cyanopyridine + 2 H2O
-
 Rhodococcus rhodochrous NCIMB 11216 nicotinic acid + NH3
-
 ?
3.5.5.1 3-cyanopyridine + 2 H2O
-
 Rhodococcus rhodochrous PA-34 nicotinic acid + NH3
-
 ?
3.5.5.1 benzonitrile + 2 H2O
-
 Arthrobacter sp. J1 benzoate + NH3
-
 ?
3.5.5.1 benzoylacetonitrile + 2 H2O
-
 Hoeflea phototrophica benzoylacetate + NH3
-
 ?
3.5.5.1 benzoylacetonitrile + 2 H2O
-
 Hoeflea phototrophica DFL-43 benzoylacetate + NH3
-
 ?
3.5.5.1 bromoxynil + 2 H2O
-
 Klebsiella pneumoniae 3,5-dibromo-4-hydroxybenzoic acid + NH3
-
 ?
3.5.5.1 cyclohexanecarbonitrile + 2 H2O
-
 Meyerozyma guilliermondii cyclohexanecarboxylic acid + NH3
-
 ?
3.5.5.1 cyclohexanecarbonitrile + 2 H2O
-
 Meyerozyma guilliermondii LM2 cyclohexanecarboxylic acid + NH3
-
 ?
3.5.5.1 iminiodiacetonitrile + 2 H2O
-
 Roseibium aggregatum iminodiacetic acid + NH3
-
 ?
3.5.5.1 iminiodiacetonitrile + 2 H2O
-
 Roseibium aggregatum DSM 13394 iminodiacetic acid + NH3
-
 ?
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Rhodococcus rhodochrous ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic nitriles Acidovorax facilis ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, aromatic, heterocyclic nitriles Acinetobacter sp. AK226 ?
-
-
3.5.5.1 additional information preferred substrate: monosubstituted phenylacetonitriles Alcaligenes faecalis ?
-
-
3.5.5.1 additional information preferred substrate: substituted aliphatic nitriles, phenylacetonitriles Alcaligenes faecalis ?
-
-
3.5.5.1 additional information preferred substrates: arylacetonitriles Alcaligenes faecalis ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, heterocyclic and aromatic nitriles Alcaligenes faecalis ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Alcaligenes sp. ECU0401 ?
-
-
3.5.5.1 additional information preferred substrates: phenylacetonitril Paenarthrobacter nitroguajacolicus ?
-
-
3.5.5.1 additional information preferred substrates: arylacetonitriles Bacillus subtilis ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, aromatic, and heterocyclic nitriles Aeribacillus pallidus ?
-
-
3.5.5.1 additional information preferred substrates: mandelonitrile, beta-hydroxy nitriles Bradyrhizobium japonicum ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic nitriles Comamonas testosteroni ?
-
-
3.5.5.1 additional information preferred substrates: aromatic nitriles Aeribacillus pallidus ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Nocardia sp. ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Nocardia globerula ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic dinitriles Pyrococcus abyssi ?
-
-
3.5.5.1 additional information preferred substrates: arylaminonitriles Pseudomonas aeruginosa ?
-
-
3.5.5.1 additional information preferred substrates: dinitriles Pseudomonas fluorescens ?
-
-
3.5.5.1 additional information preferred substrate: arylacetonitrile Pseudomonas putida ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic and aromatic nitriles Rhodococcus erythropolis ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic and aromatic nitriles Rhodococcus rhodochrous ?
-
-
3.5.5.1 additional information preferred substrate: aromatic nitriles, unsaturated aliphatic nitrile Rhodococcus sp. NDB1165 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic mono- and dinitriles Streptomyces sp. MTCC 7546 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Aspergillus niger ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Fusarium solani ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Fusarium oxysporum f. sp. melonis ?
-
-
3.5.5.1 additional information preferred substrate: aromatic, and heterocyclic nitriles Fusarium solani ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Arabidopsis thaliana ?
-
-
3.5.5.1 additional information preferred substrate: monosubstituted phenylacetonitriles Alcaligenes faecalis JM3 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Aspergillus niger K10 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, aromatic, and heterocyclic nitriles Aeribacillus pallidus RAPc8 ?
-
-
3.5.5.1 additional information preferred substrates: aromatic nitriles Aeribacillus pallidus RAPc8 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Rhodococcus rhodochrous J1 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic and aromatic nitriles Rhodococcus rhodochrous J1 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Fusarium solani IMI196840 ?
-
-
3.5.5.1 additional information preferred substrate: aromatic, and heterocyclic nitriles Fusarium solani IMI196840 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic, aromatic, and heterocyclic nitriles Fusarium solani O1 ?
-
-
3.5.5.1 additional information preferred substrate: aromatic, and heterocyclic nitriles Fusarium solani O1 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, aromatic, and heterocyclic nitriles Aeribacillus pallidus Dac521 ?
-
-
3.5.5.1 additional information preferred substrates: aromatic nitriles Aeribacillus pallidus Dac521 ?
-
-
3.5.5.1 additional information preferred substrates: dinitriles Pseudomonas fluorescens Pf-5 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Rhodococcus rhodochrous NCIMB 11216 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic and aromatic nitriles Rhodococcus rhodochrous NCIMB 11216 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Rhodococcus rhodochrous PA-34 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic and aromatic nitriles Rhodococcus rhodochrous PA-34 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic and aromatic nitriles Nocardia globerula NHB-2 ?
-
-
3.5.5.1 additional information preferred substrate: substituted aliphatic nitriles, phenylacetonitriles Alcaligenes faecalis ATCC 8750 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, heterocyclic and aromatic nitriles Alcaligenes faecalis ATCC 8750 ?
-
-
3.5.5.1 additional information preferred substrate: substituted aliphatic nitriles, phenylacetonitriles Alcaligenes faecalis MTCC 10757 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic, heterocyclic and aromatic nitriles Alcaligenes faecalis MTCC 10757 ?
-
-
3.5.5.1 additional information preferred substrates: arylacetonitriles Alcaligenes faecalis ZJUTB10 ?
-
-
3.5.5.1 additional information preferred substrates: mandelonitrile, beta-hydroxy nitriles Bradyrhizobium japonicum USDA110 ?
-
-
3.5.5.1 additional information preferred substrates: aliphatic nitriles Acidovorax facilis ATCC 55746 ?
-
-
3.5.5.1 additional information preferred substrates: phenylacetonitril Paenarthrobacter nitroguajacolicus ZJUTB06-99 ?
-
-
3.5.5.1 additional information preferred substrates: arylacetonitriles Bacillus subtilis ZJB-063 ?
-
-
3.5.5.1 additional information preferred substrates: arylaminonitriles Pseudomonas aeruginosa 10145 ?
-
-
3.5.5.1 additional information preferred substrates: dinitriles Pseudomonas fluorescens DSM 7155 ?
-
-
3.5.5.1 additional information preferred substrate: aliphatic and aromatic nitriles Rhodococcus erythropolis ZJB-0910 ?
-
-
3.5.5.1 o-chlorobenzyl cyanide + 2 H2O
-
 Roseibium aggregatum (o-chlorophenyl)acetid acid + NH3
-
 ?
3.5.5.1 o-chlorobenzyl cyanide + 2 H2O
-
 Roseibium aggregatum DSM 13394 (o-chlorophenyl)acetid acid + NH3
-
 ?
3.5.5.1 phenylacetonitrile + 2 H2O
-
 Halomonas nitrilica phenylacetate + NH3
-
 ?
3.5.5.1 phenylacetonitrile + 2 H2O
-
 Roseibium aggregatum phenylacetate + NH3
-
 ?
3.5.5.1 phenylacetonitrile + 2 H2O
-
 Roseibium aggregatum DSM 13394 phenylacetate + NH3
-
 ?
3.5.5.1 phenylacetonitrile + H2O
-
 Pseudomonas fluorescens phenylacetate + NH3
-
 ?
3.5.5.1 phenylacetonitrile + H2O
-
 Pseudomonas fluorescens Pf-5 phenylacetate + NH3
-
 ?
3.5.5.1 phenylacetonitrile + H2O
-
 Pseudomonas fluorescens DSM 7155 phenylacetate + NH3
-
 ?
3.5.5.1 phenylpropionitrile + 2 H2O
-
 Halomonas nitrilica phenylpropionate + NH3
-
 ?
3.5.5.1 valeronitrile + 2 H2O
-
 Halomonas sp. IIIMB2797 valeric acid + NH3
-
 ?
3.5.5.7 additional information preferred substrate: aliphatic nitriles Rhodococcus rhodochrous ?
-
-
3.5.5.7 additional information preferred substrate: aliphatic nitriles Rhodococcus rhodochrous K22 ?
-
-

Subunits

EC Number Subunits Comment Organism
3.5.5.1 ? x * 38000 Comamonas testosteroni
3.5.5.1 ? x * 40000 Hoeflea phototrophica
3.5.5.1 ? x * 37000 Roseibium aggregatum
3.5.5.1 ? 2 (or 3) * 38000 Pseudomonas fluorescens
3.5.5.1 ? 9 (or 10) * 43000 Pseudomonas putida
3.5.5.1 ? x * 38500 Aspergillus niger
3.5.5.1 ? x * 40000 Fusarium solani
3.5.5.1 decamer 10 * 40000 Rhodococcus rhodochrous
3.5.5.1 decamer 10 * 38500 Alcaligenes sp. ECU0401
3.5.5.1 decamer 10 * 34500 Bradyrhizobium japonicum
3.5.5.1 decamer 10 * 38000 Aeribacillus pallidus
3.5.5.1 dimer 2 * 40000 Rhodococcus rhodochrous
3.5.5.1 dimer 2 * 37000 Klebsiella pneumoniae
3.5.5.1 dimer 2 * 30000 Pyrococcus abyssi
3.5.5.1 dodecamer 12 * 40000 Rhodococcus rhodochrous
3.5.5.1 dodecamer 12 * 37000 Bradyrhizobium japonicum
3.5.5.1 dodecamer 12 * 45000 Nocardia sp.
3.5.5.1 dodecamer 12 * 45800 Rhodococcus rhodochrous
3.5.5.1 eicosamer 20 * 38000 Aeribacillus pallidus
3.5.5.1 hexamer 6 * 44000 Alcaligenes faecalis
3.5.5.1 hexamer 6 * 38000 Aeribacillus pallidus
3.5.5.1 monomer 1 * 31000 Pannonibacter carbonis
3.5.5.1 monomer 1 * 45000 Rhodococcus rhodochrous
3.5.5.1 octamer 8 * 38000 Aeribacillus pallidus
3.5.5.1 octamer 8 * 40000 Fusarium solani
3.5.5.1 tetradecamer 14 * 40000 Acidovorax facilis
3.5.5.1 tetradecamer 14 * 41000 Acinetobacter sp. AK226
3.5.5.1 tetradecamer 14 * 32000 Alcaligenes faecalis
3.5.5.1 tetradecamer 14 * 41000 Aeribacillus pallidus
3.5.5.1 tetradecamer 14 * 37000 Fusarium oxysporum f. sp. melonis
3.5.5.1 tetramer 4 * 33000 Pseudomonas fluorescens
3.5.5.1 tridecamer 13 * 38000 Arabidopsis thaliana
3.5.5.7 ? x * 41000 Rhodococcus rhodochrous

Synonyms

EC Number Synonyms Comment Organism
3.5.5.1 bll6402
-
 Bradyrhizobium japonicum
3.5.5.1 blr3397
-
 Bradyrhizobium japonicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.5.1 30
-
-
 Arabis alpina
3.5.5.1 30 40
-
 Arthrobacter sp. J1
3.5.5.1 30
-
-
 Comamonas testosteroni
3.5.5.1 30
-
-
 Nocardia sp.
3.5.5.1 30
-
-
 Paenarthrobacter nitroguajacolicus
3.5.5.1 30
-
-
 Rhodococcus erythropolis
3.5.5.1 30
-
-
 Rhodococcus rhodochrous
3.5.5.1 35
-
-
 Alcaligenes faecalis
3.5.5.1 35
-
-
 Arabidopsis thaliana
3.5.5.1 35
-
-
 Brevibacterium sp. R312
3.5.5.1 35
-
-
 Klebsiella pneumoniae
3.5.5.1 35
-
-
 Rhodococcus rhodochrous
3.5.5.1 40 45
-
 Alcaligenes faecalis
3.5.5.1 40
-
-
 Alcaligenes faecalis
3.5.5.1 40
-
-
 Alcaligenes sp. ECU0401
3.5.5.1 40
-
-
 Fusarium oxysporum f. sp. melonis
3.5.5.1 40
-
-
 Nocardia globerula
3.5.5.1 40
-
-
 Pseudomonas putida
3.5.5.1 45
-
-
 Alcaligenes faecalis
3.5.5.1 45
-
-
 Aspergillus niger
3.5.5.1 45
-
-
 Bradyrhizobium japonicum
3.5.5.1 45
-
-
 Fusarium solani
3.5.5.1 45
-
-
 Halomonas sp. IIIMB2797
3.5.5.1 45
-
-
 Pseudomonas fluorescens
3.5.5.1 45
-
-
 Rhodococcus rhodochrous
3.5.5.1 45
-
-
 Rhodococcus sp. NDB1165
3.5.5.1 50
-
-
 Acinetobacter sp. AK226
3.5.5.1 50
-
-
 Hoeflea phototrophica
3.5.5.1 50
-
-
 Roseibium aggregatum
3.5.5.1 55
-
-
 Pseudomonas fluorescens
3.5.5.1 60 90
-
 Pyrococcus abyssi
3.5.5.1 65
-
-
 Acidovorax facilis
3.5.5.1 65
-
-
 Aeribacillus pallidus
3.5.5.1 65
-
-
 Pannonibacter carbonis
3.5.5.7 50
-
-
 Rhodococcus rhodochrous

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.5.1 6 8
-
 Pyrococcus abyssi
3.5.5.1 6 11
-
 Fusarium oxysporum f. sp. melonis
3.5.5.1 7 8
-
 Alcaligenes faecalis
3.5.5.1 7 8
-
 Bradyrhizobium japonicum
3.5.5.1 7
-
-
 Brevibacterium sp. R312
3.5.5.1 7
-
-
 Comamonas testosteroni
3.5.5.1 7
-
-
 Halomonas sp. IIIMB2797
3.5.5.1 7 9
-
 Meyerozyma guilliermondii
3.5.5.1 7 9.5
-
 Nocardia sp.
3.5.5.1 7
-
-
 Pannonibacter carbonis
3.5.5.1 7
-
-
 Pseudomonas fluorescens
3.5.5.1 7
-
-
 Pseudomonas putida
3.5.5.1 7 8
-
 Fusarium solani
3.5.5.1 7.5
-
-
 Alcaligenes faecalis
3.5.5.1 7.5
-
-
 Paenarthrobacter nitroguajacolicus
3.5.5.1 7.5 8.5
-
 Arthrobacter sp. J1
3.5.5.1 7.5
-
-
 Nocardia globerula
3.5.5.1 7.5
-
-
 Rhodococcus erythropolis
3.5.5.1 7.5
-
-
 Rhodococcus rhodochrous
3.5.5.1 7.6
-
-
 Rhodococcus rhodochrous
3.5.5.1 7.6
-
-
 Aeribacillus pallidus
3.5.5.1 8
-
-
 Acinetobacter sp. AK226
3.5.5.1 8
-
-
 Alcaligenes faecalis
3.5.5.1 8
-
-
 Alcaligenes sp. ECU0401
3.5.5.1 8
-
-
 Roseibium aggregatum
3.5.5.1 8
-
-
 Rhodococcus rhodochrous
3.5.5.1 8
-
-
 Rhodococcus sp. NDB1165
3.5.5.1 8
-
-
 Aspergillus niger
3.5.5.1 8
-
-
 Arabis alpina
3.5.5.1 8.5
-
-
 Hoeflea phototrophica
3.5.5.1 9
-
-
 Pseudomonas fluorescens
3.5.5.1 9
-
-
 Arabidopsis thaliana
3.5.5.1 9.2
-
-
 Klebsiella pneumoniae
3.5.5.7 5.5
-
-
 Rhodococcus rhodochrous

Expression

EC Number Organism Comment Expression
3.5.5.1 Rhodococcus rhodochrous inducible by isovaleronitrile up
3.5.5.1 Alcaligenes faecalis inducible by isovaleronitrile up
3.5.5.1 Alcaligenes faecalis inducible by n-butyronitrile up
3.5.5.1 Alcaligenes faecalis inducible by acrylonitrile and benzonitrile up
3.5.5.1 Paenarthrobacter nitroguajacolicus inducible epsilon-caprolactam up
3.5.5.1 Arthrobacter sp. J1 inducible benzonitrile up
3.5.5.1 Aeribacillus pallidus inducible by benzonitrile up
3.5.5.1 Bradyrhizobium japonicum inducible by benzonitrile up
3.5.5.1 Nocardia globerula inducible by propionitrile up
3.5.5.1 Rhodococcus rhodochrous inducible by propionitrile up
3.5.5.1 Aspergillus niger inducible by 3-cyanopyridine up
3.5.5.1 Fusarium solani inducible by 2-cyanopyridine up