Literature summary for 4.2.1.84 extracted from

Raczynska, J.E.; Vorgias, C.E.; Antranikian, G.; Rypniewski, W.
Crystallographic analysis of a thermoactive nitrilase (2011), J. Struct. Biol., 173, 294-302.

Search for more literature for 4.2.1.84

Cloned(Commentary)

Cloned (Comment)	Organism
gene nit-30, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain Bl21(DE3)	Pyrococcus abyssi

Crystallization (Commentary)

Crystallization (Comment)	Organism
PaNit without ligands, and with an acetate ion bound in the active site, or with a bromide ion in the active site, by hanging drop vapour diffusion method from 35% PEG 550MME, 0.2 M MgCl2 or Mg(CH3COOH)2 and 0.2 M Tris-HCl, pH 7.5, X-ray diffraction structure determination and analysis at 1.57-1.83 A resolution	Pyrococcus abyssi

Metals/Ions

Metals/Ions	Comment	Organism	Structure
acetate	the acetate ion binds close to Mg2+, and it interacts with two coordinating water molecules	Pyrococcus abyssi
Mg2+	Mg2+ bound in chain B interacts with five water molecules and Asn49B	Pyrococcus abyssi
additional information	specific binding of the carboxylate group, as well as a more general electrostatic preference for negatively charged ligands revealed by binding of the Br- ions, overview	Pyrococcus abyssi

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Pyrococcus abyssi	the thermoactive nitrilase from Pyrococcus abyssi hydrolyses small aliphatic nitriles like fumaro- and malononitril, docking calculations for fumaro- and malononitriles, modelling, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus abyssi	-	gene nit-30	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant Nit from Escherichia coli strain Bl21(DE3) by ammonium sulfate fractionation and anion exchange chromatography	Pyrococcus abyssi

Reaction

Reaction	Comment	Organism	Reaction ID
an aliphatic amide = a nitrile + H2O	role of residues in the active site and enzymatic reaction mechanism. Cys146 acts as the nucleophile, Glu42 as the general base, Lys113/Glu42 as the general acid, WatA as the hydrolytic water and Nf_Lys113 and N_Phe147 form the oxyanion hole, hydrogen bonding network in the active site of Nit structure, overview	Pyrococcus abyssi	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the thermoactive nitrilase from Pyrococcus abyssi hydrolyses small aliphatic nitriles like fumaro- and malononitril, docking calculations for fumaro- and malononitriles, modelling, overview	Pyrococcus abyssi	?	-	?

Synonyms

Synonyms	Comment	Organism
nitrilase	-	Pyrococcus abyssi
PaNit	-	Pyrococcus abyssi

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Release 2023.1 (January 2023)