Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.84 extracted from

  • Nojiri, M.; Yohda, M.; Odaka, M.; Matsushita, Y.; Tsujimura, M.; Yoshida, T.; Dohmae, N.; Takio, K.; Endo, I.
    Functional expression of nitrile hydratase in Escherichia coli: requirement of a nitrile hydratase activator and post-translational modification of a ligand cysteine (1999), J. Biochem., 125, 696-704.
    View publication on PubMed
Search for more literature for 4.2.1.84

Activating Compound

Activating Compound Comment Organism Structure
light restores activity inhibited by NO Rhodococcus sp.
potassium hexacyanoferrate oxidizing agent that activates the Co-substituted enzyme by oxidizing the Co2+ atom and/or modification of a alphaCys-112 to cysteine-sulfinic acid Rhodococcus sp.

Application

Application Comment Organism
synthesis useful for acrylamide production Rhodococcus sp.

Cloned(Commentary)

Cloned (Comment) Organism
Co-substituted NHase produced in Escherichia coli grown in Co supplemented medium Rhodococcus sp.
expression in Escherichia coli Rhodococcus sp.

Inhibitors

Inhibitors Comment Organism Structure
NO reversible inhibition, for recombinant enzyme Rhodococcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ incorporated instead of Fe into the catalytic site with initial weak activity that increases when an oxidizing agent is added Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information alphaCys112 is modified to a cysteine-sulfinic acid in both recombinant and native enzymes Rhodococcus sp.

Purification (Commentary)

Purification (Comment) Organism
chromatography on butyl-toyopearl Rhodococcus sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
97
-
 purified co-substituted enzyme Rhodococcus sp.