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Literature summary extracted from

  • Chen, J.; Yu, H.; Liu, C.; Liu, J.; Shen, Z.
    Improving stability of nitrile hydratase by bridging the salt-bridges in specific thermal-sensitive regions (2012), J. Biotechnol., 164, 354-362.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.84 betaW47E site-directed mutagenesis Rhodococcus ruber
4.2.1.84 additional information transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH Pseudonocardia thermophila
4.2.1.84 additional information transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH Bacillus sp. (in: Bacteria)
4.2.1.84 additional information transfer of stabilized salt-bridge interactions from three deformation-prone thermal-sensitive regions (A1, A2 and A3 in beta-subunit) of the thermophilic NHase 1V29 from Bacillus SC-105-1 and 1UGQ from Pseudonocardia thermophila JCM3095 into industrialized mesophilic NHase-TH from Rhodococcus ruber TH. Three types of salt bridge - active center-adjacent (in A1), internal neighboring-residue-bridged (in A2) and C-terminal-residue-bridged (A3) - are constructed in NHase-TH. A C-terminal salt-bridge strategy is powerful for enzyme stability intensification through triggering global changes of the salt bridge networks, molecular dynamic simulation, overview Rhodococcus ruber

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.84 Bacillus sp. (in: Bacteria) Q7SID2 alpha-subunit
-
4.2.1.84 Bacillus sp. (in: Bacteria) Q7SID3 beta-subunit
-
4.2.1.84 Bacillus sp. (in: Bacteria) SC-105-1 Q7SID2 alpha-subunit
-
4.2.1.84 Bacillus sp. (in: Bacteria) SC-105-1 Q7SID3 beta-subunit
-
4.2.1.84 Pseudonocardia thermophila
-
-
-
4.2.1.84 Pseudonocardia thermophila JCM 3095
-
-
-
4.2.1.84 Rhodococcus ruber
-
-
-
4.2.1.84 Rhodococcus ruber TH
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.84 acrylonitrile + H2O
-
 Rhodococcus ruber acrylamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Pseudonocardia thermophila acrylamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Bacillus sp. (in: Bacteria) acrylamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Rhodococcus ruber TH acrylamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Pseudonocardia thermophila JCM 3095 acrylamide
-
 ?
4.2.1.84 acrylonitrile + H2O
-
 Bacillus sp. (in: Bacteria) SC-105-1 acrylamide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.84 NHase
-
 Rhodococcus ruber
4.2.1.84 NHase
-
 Pseudonocardia thermophila
4.2.1.84 NHase
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.84 28
-
 assay at Rhodococcus ruber
4.2.1.84 28
-
 assay at Pseudonocardia thermophila
4.2.1.84 28
-
 assay at Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.84 77
-
 identification of three hyperthermal sensitive regions in the beta-subunit of NHase-TH, referred to as region A1 (amino acids 211-231), A2 (amino acids 308-319) and A3 (amino acids 429-432) at heating stress Rhodococcus ruber

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.84 7
-
 assay at Rhodococcus ruber
4.2.1.84 7
-
 assay at Pseudonocardia thermophila
4.2.1.84 7
-
 assay at Bacillus sp. (in: Bacteria)