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Literature summary for 4.2.1.84 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
Search for more literature for 4.2.1.84

Protein Variants

Protein Variants Comment Organism
betaW47E site-directed mutagenesis Rhodococcus ruber
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
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)
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

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

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

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