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Literature summary for 4.2.1.84 extracted from

  • Hopmann, K.H.; Himo, F.
    On the role of tyrosine as catalytic base in nitrile hydratase (2008), Eur. J. Inorg. Chem., 2008, 3452-3459.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamics Rhodococcus erythropolis
additional information
-
additional information thermodynamics Pseudonocardia thermophila

Metals/Ions

Metals/Ions Comment Organism Structure
Co3+ the enzyme belongs to the CoIII-NHase group of enzymes, octahedrally coordinated metal ion with two deprotonated backbone amides as ligands as well as three cysteine residues, two of which are posttranslationally oxidized to cysteine-sulfenic and cysteine-sulfinic acids Pseudonocardia thermophila
Fe3+ the enzyme belongs to the FeIII-NHase group of enzymes, octahedrally coordinated metal ion with two deprotonated backbone amides as ligands as well as three cysteine residues, two of which are posttranslationally oxidized to cysteine-sulfenic and cysteine-sulfinic acids Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
an aliphatic amide Rhodococcus erythropolis
-
a nitrile + H2O
-
?
an aliphatic amide Pseudonocardia thermophila
-
a nitrile + H2O
-
?
an aliphatic amide Rhodococcus erythropolis N-771
-
a nitrile + H2O
-
?
an aliphatic amide Pseudonocardia thermophila JCM 3095
-
a nitrile + H2O
-
?

Organism

Organism UniProt Comment Textmining
Pseudonocardia thermophila
-
-
-
Pseudonocardia thermophila JCM 3095
-
-
-
Rhodococcus erythropolis
-
-
-
Rhodococcus erythropolis N-771
-
-
-

Reaction

Reaction Comment Organism Reaction ID
an aliphatic amide = a nitrile + H2O first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview Rhodococcus erythropolis
an aliphatic amide = a nitrile + H2O reaction mechanism, first-shell mechanism of CoIII-NHase involving Tyr68 as catalytic base, deprotonated Tyr68 is proposed to abstract a proton from the nucleophilic water molecule, thus activating it for attack on the metal-bound substrate, modelling, detailed overview Pseudonocardia thermophila

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an aliphatic amide
-
Rhodococcus erythropolis a nitrile + H2O
-
?
an aliphatic amide
-
Pseudonocardia thermophila a nitrile + H2O
-
?
an aliphatic amide ligand exchange reactions, overview Rhodococcus erythropolis a nitrile + H2O
-
?
an aliphatic amide ligand exchange reactions, overview Pseudonocardia thermophila a nitrile + H2O
-
?
an aliphatic amide
-
Rhodococcus erythropolis N-771 a nitrile + H2O
-
?
an aliphatic amide ligand exchange reactions, overview Rhodococcus erythropolis N-771 a nitrile + H2O
-
?
an aliphatic amide
-
Pseudonocardia thermophila JCM 3095 a nitrile + H2O
-
?
an aliphatic amide ligand exchange reactions, overview Pseudonocardia thermophila JCM 3095 a nitrile + H2O
-
?

Synonyms

Synonyms Comment Organism
CoIII-NHase
-
Rhodococcus erythropolis
CoIII-NHase
-
Pseudonocardia thermophila