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Literature summary extracted from

  • Zhang, Y.; Zeng, Z.; Zeng, G.; Liu, X.; Chen, M.; Liu, L.; Liu, Z.; Xie, G.
    Enzyme-substrate binding landscapes in the process of nitrile biodegradation mediated by nitrile hydratase and amidase (2013), Appl. Biochem. Biotechnol., 170, 1614-1623.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.84 analysis of structure PDB ID 1IRE Pseudonocardia thermophila
4.2.1.84 analysis of structure PDB ID 2QDY Rhodococcus erythropolis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.84 Co2+ Co-type NHase Pseudonocardia thermophila
4.2.1.84 Fe2+ Fe-type NHase Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.84 additional information Rhodococcus erythropolis molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile ?
-
 ?
4.2.1.84 additional information Pseudonocardia thermophila molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine ?
-
 ?
4.2.1.84 additional information Pseudonocardia thermophila JCM 3095 molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine ?
-
 ?
4.2.1.84 additional information Rhodococcus erythropolis AJ270 molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.84 Pseudonocardia thermophila Q7SID2 alpha-subunit
-
4.2.1.84 Pseudonocardia thermophila JCM 3095 Q7SID2 alpha-subunit
-
4.2.1.84 Rhodococcus erythropolis P13448
-
-
4.2.1.84 Rhodococcus erythropolis AJ270 P13448
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.84 2,2-dimethylcyclopropanecarbonitrile + H2O
-
 Rhodococcus erythropolis ?
-
 ?
4.2.1.84 2-hydroxy-4-phenylbutanenitrile + H2O
-
 Rhodococcus erythropolis ?
-
 ?
4.2.1.84 3-cyanopyridine + H2O
-
 Pseudonocardia thermophila pyridine-3-carbamide
-
 ?
4.2.1.84 3-cyanopyridine + H2O
-
 Rhodococcus erythropolis pyridine-3-carbamide
-
 ?
4.2.1.84 3-cyanopyridine + H2O
-
 Pseudonocardia thermophila JCM 3095 pyridine-3-carbamide
-
 ?
4.2.1.84 3-cyanopyridine + H2O
-
 Rhodococcus erythropolis AJ270 pyridine-3-carbamide
-
 ?
4.2.1.84 4-chloro-3-hydroxybutanenitrile + H2O
-
 Rhodococcus erythropolis ?
-
 ?
4.2.1.84 acetonitrile + H2O
-
 Rhodococcus erythropolis acetamide
-
 ?
4.2.1.84 acetonitrile + H2O
-
 Rhodococcus erythropolis AJ270 acetamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Pseudonocardia thermophila ?
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Pseudonocardia thermophila JCM 3095 ?
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Rhodococcus erythropolis acrylamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Rhodococcus erythropolis AJ270 acrylamide
-
 ?
4.2.1.84 benzonitrile + H2O
-
 Pseudonocardia thermophila ?
-
 ?
4.2.1.84 benzonitrile + H2O
-
 Pseudonocardia thermophila JCM 3095 ?
-
 ?
4.2.1.84 benzonitrile + H2O
-
 Rhodococcus erythropolis benzamide
-
 ?
4.2.1.84 butyronitrile + H2O
-
 Rhodococcus erythropolis ?
-
 ?
4.2.1.84 isobutyronitrile + H2O
-
 Rhodococcus erythropolis ?
-
 ?
4.2.1.84 methacrylonitrile + H2O
-
 Pseudonocardia thermophila ?
-
 ?
4.2.1.84 methacrylonitrile + H2O
-
 Rhodococcus erythropolis methacrylamide
-
 ?
4.2.1.84 additional information substrate specificity, overview Pseudonocardia thermophila ?
-
 ?
4.2.1.84 additional information substrate specificity, overview Rhodococcus erythropolis ?
-
 ?
4.2.1.84 additional information molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile Rhodococcus erythropolis ?
-
 ?
4.2.1.84 additional information molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine Pseudonocardia thermophila ?
-
 ?
4.2.1.84 additional information substrate specificity, overview Pseudonocardia thermophila JCM 3095 ?
-
 ?
4.2.1.84 additional information molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets formed diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is 3-cyanopyridine Pseudonocardia thermophila JCM 3095 ?
-
 ?
4.2.1.84 additional information substrate specificity, overview Rhodococcus erythropolis AJ270 ?
-
 ?
4.2.1.84 additional information molecular modeling study of enzyme-substrate binding modes in the bi-enzyme pathway for degradation of nitrile to acid, specific residues within the enzyme's binding pockets form diverse contacts with the substrate, molecular docking, overview. Top substrate having favorable interactions with nitrile hydratase is benzonitrile Rhodococcus erythropolis AJ270 ?
-
 ?
4.2.1.84 propionitrile + H2O
-
 Rhodococcus erythropolis propionamide
-
 ?
4.2.1.84 tert-butylisonitrile + H2O
-
 Pseudonocardia thermophila ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.84 NHase
-
 Pseudonocardia thermophila
4.2.1.84 NHase
-
 Rhodococcus erythropolis

General Information

EC Number General Information Comment Organism
4.2.1.84 metabolism hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation Pseudonocardia thermophila
4.2.1.84 metabolism hydrolysis mediated by nitrilase, NHase, and amidase is the most common way for nitrile degradation Rhodococcus erythropolis