Results 81 to 90 of about 79,802 (211)

Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis [PDF]

open access: yes, 2009
Glyoxalase II (GloII) is a ubiquitous thioester hydrolase catalyzing the last step of the glutathione-dependent conversion of 2-oxoaldehydes to 2-hydroxycarboxylic acids.
Elia A.C.   +6 more
core   +1 more source

Synthesis of Indole Derivatives via Aryl Triazole Ring-Opening and Subsequent Cyclization

open access: yesMolecules
A metal-free two-step synthetic approach for obtaining indole derivatives from aryl triazole fragment-containing compounds has been developed. In the first step, the Dimroth equilibrium, followed by nitrogen extrusion, Wolff rearrangement, and amine ...
Aleksejs Burcevs   +4 more
doaj   +1 more source

Hydrazones as Singular Reagents in Asymmetric Organocatalysis [PDF]

open access: yes, 2016
This Minireview summarizes strategies and developments regarding the use of hydrazones as reagents in asymmetric organocatalysis, their distinct roles in nucleophile–electrophile, cycloaddition, and cyclization reactions.
Fernández Fernández, Rosario Fátima   +4 more
core   +1 more source

Biocatalytic Synthesis of Stereospecific Triketide Lactones using Polyketide Synthases [PDF]

open access: yes, 2016
Polyketide synthases are modular enzymes that create and modify large acyl chains. The domains and modules of polyketide synthases allow us to create molecules that resemble naturally occurring products by applying a biocatalytic in vitro in vivo ...
Alexander, Bradley
core   +1 more source

nucleophile

open access: yes, 2014
Citation: 'nucleophile' in the IUPAC Compendium of Chemical Terminology, 3rd ed.; International Union of Pure and Applied Chemistry; 2006. Online version 3.0.1, 2019. 10.1351/goldbook.N04249 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms.
openaire   +1 more source

Phosphazene-catalyzed desymmetrization of cyclohexadienones by dithiane addition

open access: yesBeilstein Journal of Organic Chemistry, 2017
We report a desymmetrization of cyclohexadienones by intramolecular conjugate addition of a tethered dithiane nucleophile. Mild reaction conditions allow the formation of diversely functionalized fused bicyclic lactones.
Matthew A. Horwitz   +2 more
doaj   +1 more source

Reactivity of TEMPO anion as a nucleophile and its applications for selective transformations of haloalkanes or acyl halides to aldehydes [PDF]

open access: yes, 2004
Sodium 2,2,6,6-tetramethylpiperidine-N-oxide (TEMPO−Na+), generated by reduction of TEMPO· with sodium naphthalenide in THF, reacted with alkyl halides or acyl halides to produce O-alkylated or acylated TEMPOs, which were in turn oxidized with ...
Allen   +35 more
core   +1 more source

Chiral phosphoric acid catalyzed aminative dearomatization of α-naphthols/Michael addition sequence

open access: yesNature Communications, 2019
Catalytic asymmetric dearomatization (CADA) reactions readily convert common aromatic compounds to diverse 3D chiral, polycyclic molecules. Here, the authors report an intermolecular asymmetric dearomatization of nucleophile-tethered α-naphthols ...
Zi-Lei Xia   +3 more
doaj   +1 more source

The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc-Oxy) and Acid–Base zones

open access: yesCurrent Research in Structural Biology
SGNH hydrolase-like fold proteins are serine proteases with the default Asp-His-Ser catalytic triad. Here, we show that these proteins share two unique conserved structural organizations around the active site: (1) the Nuc-Oxy Zone around the catalytic ...
Konstantin Denessiouk   +5 more
doaj   +1 more source

The High-Resolution Structures of the Neutral and the Low pH Crystals of Aminopeptidase from \u3cem\u3eAeromonas proteolytica\u3c/em\u3e [PDF]

open access: yes, 2006
The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in the active site and catalyzes the degradation of peptides. Herein we report the crystal structures of AAP at 0.95-Å resolution at neutral pH and at 1.24-Å resolution at low pH.
Bienvenue, David L.   +5 more
core   +1 more source

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