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Literature summary for 4.2.1.84 extracted from

  • Gumataotao, N.; Kuhn, M.L.; Hajnas, N.; Holz, R.C.
    Identification of an active site-bound nitrile hydratase intermediate through single turnover stopped-flow spectroscopy (2013), J. Biol. Chem., 288, 15532-15536.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Rhodococcus equi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information single turnover stopped-flow experiments and multiple turnover experiments with methacrylonitrile suggest a three-step kinetic model that allows for the reversible binding of substrate, the presence of an intermediate, and the formation of product, identification of catalytic Fe3+-nitrile intermediate species, kinetics, detaiiled overview Rhodococcus equi

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ iron-type nitrile hydratase Rhodococcus equi

Organism

Organism UniProt Comment Textmining
Rhodococcus equi
-
-
-
Rhodococcus equi TG328-2
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography and ultrafiltration Rhodococcus equi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methacrylonitrile + H2O
-
Rhodococcus equi methacrylamide
-
?
methacrylonitrile + H2O
-
Rhodococcus equi TG328-2 methacrylamide
-
?

Synonyms

Synonyms Comment Organism
iron-type nitrile hydratase
-
Rhodococcus equi
NHase
-
Rhodococcus equi
ReNHase
-
Rhodococcus equi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Rhodococcus equi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Rhodococcus equi