Results 41 to 50 of about 43,844 (154)

Soluble epoxide hydrolase limits mechanical hyperalgesia during inflammation [PDF]

open access: yes, 2011
Background Cytochrome-P450 (CYP450) epoxygenases metabolise arachidonic acid (AA) into four different biologically active epoxyeicosatrienoic acid (EET) regioisomers.
Geisslinger, Gerd   +39 more
core   +3 more sources

Properties of epoxide hydrolase from the yeast Rhodotorula glutinis [PDF]

open access: yes, 2002
Epoxide hydrolases are ubiquitous enzymes that can be found in nearly all living organisms. Some of the enzymes play an important role in detoxifying xenobiotic and metabolic compounds.
Ariës-Kronenburg, N.A.E.
core  

Enantiomeric Tartaric Acid Production Using cis-Epoxysuccinate Hydrolase: History and Perspectives

open access: yesMolecules, 2019
Tartaric acid is an important chiral chemical building block with broad industrial and scientific applications. The enantioselective synthesis of l(+)- and d(−)-tartaric acids has been successfully achieved using bacteria presenting cis ...
Jinsong Xuan, Yingang Feng
doaj   +1 more source

C‐Terminal Functionalization Methods of Amino Acids, Peptides, and Proteins

open access: yesChemistry – A European Journal, EarlyView.
C‐terminal functionalization offers powerful routes to peptide and protein diversification, yet epimerization, hydrolysis, and selectivity remain key challenges. This Review surveys enzymatic, decarboxylative, and condensation strategies, highlighting advances toward chemo‐ and regioselective, protecting‐group‐free, atom‐efficient methods applicable to
Jay Hanssens   +3 more
wiley   +1 more source

The evolutionary relationship between epoxide hydrolases and dehalogenases [PDF]

open access: yes, 2022
Enzymes are well-known for being remarkably selective catalysts. They are often able to catalyse reactions for certain molecules while leaving other similar molecules completely unchanged.
Schuiten, Eva Daniëlle
core   +1 more source

MurNAc‐Based Electrophilic Inhibitors of O‐Acetylpeptidoglycan Esterase (Ape): Design, Synthesis, and Kinetic Evaluation

open access: yesChemistry – A European Journal, EarlyView.
A series of N‐acetylmuramic acid (MurNAc)‐based electrophilic inhibitors targeting Ape esterase was synthesized. Their inhibitory potency ranged from micromolar to submillimolar. The study probed binding contributions of stem peptide extension, replacing the anomeric methyl group with a benzyl, and α‐fluorination of the carbonyl to enhance ...
Dmytro Voskoboinyk, Martin E. Tanner
wiley   +1 more source

Enantioconvergent Hydrolysis of Styrene Epoxides by Newly Discovered Epoxide Hydrolases in Mung Bean

open access: yes, 2016
Two novel epoxide hydrolases were discovered in mung bean (Phaseolus radiatus L.) for the first time, either of which can catalyze enantioconvergent hydrolysis of styrene epoxides.
Xin-Yan Wu (1490878)   +4 more
core   +3 more sources

The gut microbiome and drug‐resistant epilepsy: Microbiome–antiseizure medication interactions and implications for pharmacoresistance

open access: yesEpilepsia Open, EarlyView.
Abstract Drug‐resistant epilepsy (DRE) affects approximately one‐third of patients with epilepsy and represents a major unmet clinical need. While traditional hypotheses of pharmacoresistance have focused on alterations in drug targets, efflux transporter overexpression, and intrinsic disease severity, the gut microbiome has recently emerged as a ...
Khaled Zammar   +4 more
wiley   +1 more source

Comparing the regio- and enantioselectivity of inverting versus retaining epoxide hydrolases [PDF]

open access: yes, 2016
Epoxide hydrolases (EHs) are enzymes that catalyze the ring opening of an epoxide, yielding a vicinal diol. This exciting class of enzymes is often associated with natural product and small molecule biosynthesis. One interesting class of natural products
Aliwalas, Mark A
core  

Effects of Glyphosate and Glyphosate‐Based Herbicides on the Mammalian Gut Microbiome: A Critical Review

open access: yesJournal of Applied Toxicology, EarlyView.
ABSTRACT Glyphosate has long been considered to pose negligible direct risk to mammals on the grounds that its molecular target, 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS), of the shikimate pathway, is absent from animal cells. This rationale is inaccurate as a complete toxicological argument, because the shikimate pathway is present in some ...
Robin Mesnage
wiley   +1 more source

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