Literature summary for 4.2.1.84 extracted from

Miyanaga, A.; Fushinobu,S.; Ito, K.; Wakagi, T.
Crystal structure of cobalt-containing nitrile hydratase (2001), Biochem. Biophys. Res. Commun., 288, 1169-1174.

Search for more literature for 4.2.1.84

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression in Escherichia coli strain HB101 from vector pUC18. The recombinant enzyme shows almost the same specific activity and other properties as the native enzyme	Pseudonocardia thermophila

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, sitting drop vapor diffusion method, 8 mg/ml protein, with a reservoir solution containing 1.4 M tri-sodium citrate, and 0.1 M HEPES-NaOH, pH 7.5, 5°C, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement and modeling	Pseudonocardia thermophila

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the enzyme shows a high tolerance against acrylamide; the enzyme shows a high tolerance against acrylamide	Pseudonocardia thermophila

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	cobalt-containing nitrile hydratase, noncorrin cobalt at the catalytic center, structure, overview. Two cysteine residues (alphaCys111 and alphaCys113) coordinated to the cobalt are posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively	Pseudonocardia thermophila
Fe2+	with cobalt substitution for iron, the enzyme activity becomes weak	Pseudonocardia thermophila
additional information	structure comparison with the Fe-type NHase, overview. In cobalt-containing nitrile hydratase, a tryptophan residue betaTrp72, which may be involved in substrate binding, replaces the tyrosine residue of iron-containing nitrile hydratase	Pseudonocardia thermophila

Organism

Organism	UniProt	Comment	Textmining
Pseudonocardia thermophila	Q7SID2	alpha-subunit	-
Pseudonocardia thermophila	Q7SID3	beta-subunit	-
Pseudonocardia thermophila JCM 3095	Q7SID2	alpha-subunit	-
Pseudonocardia thermophila JCM 3095	Q7SID3	beta-subunit	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain HB101 by heat treatment at 55°C for 30 min, ammonium sulfate precipitation, anion exchange chromatography, hydrophobic interaction chromatography, and a another differentstep of anion exchange chromatography	Pseudonocardia thermophila

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	thhe enzyme exhibits high activity	Pseudonocardia thermophila

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding	Pseudonocardia thermophila	?	-	?
additional information	the enzyme shows a preference for aromatic nitriles as substrates rather than aliphatic ones. Tryptophan residue betaTrp72 may be involved in substrate binding	Pseudonocardia thermophila JCM 3095	?	-	?

Subunits

Subunits	Comment	Organism
heterotetramer	(alphabeta)2	Pseudonocardia thermophila

Synonyms

Synonyms	Comment	Organism
Co-type NHase	-	Pseudonocardia thermophila
cobalt-containing nitrile hydratase	-	Pseudonocardia thermophila
NHase	-	Pseudonocardia thermophila

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
additional information	-	the enzyme exhibits a high optimum temperature	Pseudonocardia thermophila

General Information

General Information	Comment	Organism
additional information	the recombinant enzyme shows almost the same specific activity and other properties as the native enzyme. Structure of the active center of the recombinant enzyme, overview	Pseudonocardia thermophila

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Release 2023.1 (January 2023)