4.2.1.84	an aliphatic amide = a nitrile + H2O	detailed reaction mechanism using large quantum-mechanical active site models, overview. The attack of Cys114-SO- on the coordinated nitrile forms a cyclic intermediate. Cys109-S-S-Cys114 disulfide formation promotes cleavage of the latter to give the amide. Active-site regeneration occurs through attack of water on the disulfide, putative cyclic intermediate structure, overview	729825	
4.2.1.84	an aliphatic amide = a nitrile + H2O	first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview	-, 697734	
4.2.1.84	an aliphatic amide = a nitrile + H2O	light	-	
4.2.1.84	an aliphatic amide = a nitrile + H2O	mechanism of action for the hydration of nitriles by NHase, overview. The cysteine-sulfenic acid ligand acts as the catalytic nucleophile. The first step in catalysis involves the direct ligation of the nitrile to the active site lowspin, trivalent metal ion. One proton transfer occurs between the alphaCys113-OH ligand and the nitrile N-atom, while the second transfer occurs between the water molecule that reforms alphaCys113-OH and the newly forming imidate N-atom	-, 729896	
4.2.1.84	an aliphatic amide = a nitrile + H2O	modeling of the catalytic mechanism of nitrile hydratase by semi-empirical quantum mechanical calculation using the enzyme crystal structure, PDB code 1IRE, overview. Active site activation is the first step of NHase catalysis, in which the Co2+ coordinated to a water molecule forms a Co-OH complex mediated by the oxidized alpha-CEA113. Then the oxygen atom in the Co-OH attacks the C atom in the -CN triple bond of acrylonitrile, forming a precursor of acrylamide, proton rearrangement happens transforming the precursor into the final product of acrylamide, under the assistance of the hydrogen atom in the -OH group of alpha-Ser112	-, 699611	
4.2.1.84	an aliphatic amide = a nitrile + H2O	monitoring of binding of substrates and their analogues to the active pocket via the NO bands	665421	
4.2.1.84	an aliphatic amide = a nitrile + H2O	N-771 and N-774 strains can be inactivated in the dark and reactivated by light	-, 648430	
4.2.1.84	an aliphatic amide = a nitrile + H2O	possible role of water and active center residues in reaction mechanism is shown	-, 675502	
4.2.1.84	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	-, 697734	
4.2.1.84	an aliphatic amide = a nitrile + H2O	reaction mechanism, overview	-, 697296	
4.2.1.84	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	716057	
4.2.1.84	an aliphatic amide = a nitrile + H2O	substrate binding occurs via breathing and flip-flop mechanisms	663896	
4.2.1.84	an aliphatic amide = a nitrile + H2O	the activity of the enzyme in intact cells increases on light irradiation and gradually decreases in the dark. For purified enzyme no differences are detected when kept in dark or light-irradiated	-, 648441	
4.2.1.84	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	648442	
4.2.1.84	an aliphatic amide = a nitrile + H2O	thermal-stable mechanism of thermophilic nitrile hydratases, molecular dynamic simulation, overview	-, 699612	
4.2.1.84	an aliphatic amide = a nitrile + H2O	water dynamics and catalytic mechanism, a water molecule bound to the metal ion directly attacks the nitrile carbon, overview. Dynamics of the active site channel, NO diffusion paths, and water molecules positions are key components in the functioning of this important industrial enzyme	696768