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Results 1 - 10 of 16 > >>
EC Number Reaction Commentary Reference
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an 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
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an aliphatic amide = a nitrile + H2O first- and second-shell reaction mechanism, a tyrosine residue acts as catalytic base, modelling, detailed overview -, 697734
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an aliphatic amide = a nitrile + H2O light -
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an 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
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an 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
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an aliphatic amide = a nitrile + H2O monitoring of binding of substrates and their analogues to the active pocket via the NO bands 665421
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an aliphatic amide = a nitrile + H2O N-771 and N-774 strains can be inactivated in the dark and reactivated by light -, 648430
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an aliphatic amide = a nitrile + H2O possible role of water and active center residues in reaction mechanism is shown -, 675502
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an 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
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84an aliphatic amide = a nitrile + H2O reaction mechanism, overview -, 697296
Results 1 - 10 of 16 > >>