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

BRENDA support

Literature summary for 4.2.1.84 extracted from

  • Murakami, T.; Nojiri, M.; Nakayama, H.; Odaka, M.; Yohda, M.; Dohmae, N.; Takio, K.; Nagamune, T.; Endo, I.
    Post-translational modification is essential for catalytic activity of nitrile hydratase (2000), Protein Sci., 9, 1024-1030.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis useful for acrylamide production Rhodococcus sp.
synthesis industrial production of nicotinamide Rhodococcus sp.

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rhodococcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ non-heme ferric iron in the catalytic center Rhodococcus sp.
Fe2+ 0.01 mM ferric citrate increases the enzyme activity Rhodococcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000
-
x * 23000, alpha + x * 23000, beta Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Rhodococcus sp.
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information two cysteine ligands, alphaCys112 and alphaCys114, are oxidized to a cysteine sulfinic acid and a cysteine sulfenic acid, respectively. Cysteine sulfinic acid in 112 is responsible for the catalytic activity. First metalloprotein having posttranslationally modified cysteine ligands Rhodococcus sp.

Purification (Commentary)

Purification (Comment) Organism
anion exchange chromatography and gel filtration, recombinant enzyme Rhodococcus sp.

Reaction

Reaction Comment Organism Reaction ID
an aliphatic amide = a nitrile + H2O the iron-type enzyme is photoreactive, it loses the catalytic activity through aerobic incubation in the dark and recovers it by light irradiation Rhodococcus sp.

Subunits

Subunits Comment Organism
? x * 23000, alpha + x * 23000, beta Rhodococcus sp.