Results 21 to 30 of about 10,401,391 (311)

Insights on catalytic mechanism of CeO2 as multiple nanozymes

open access: yesNano Reseach, 2022
CeO2 with the reversible Ce3+/Ce4+ redox pair exhibits multiple enzyme-like catalytic performance, which has been recognized as a promising nanozyme with potentials for disease diagnosis and treatments.
Yuan-Yuan Ma   +3 more
semanticscholar   +1 more source

Family characteristics, phylogenetic reconstruction, and potential applications of the plant BAHD acyltransferase family

open access: yesFrontiers in Plant Science, 2023
The BAHD acyltransferase family is a class of proteins in plants that can acylate a variety of primary and specialized secondary metabolites. The typically acylated products have greatly improved stability, lipid solubility, and bioavailability and thus ...
Donghuan Xu   +5 more
doaj   +1 more source

The Catalytic Mechanisms of Binuclear Metallohydrolases [PDF]

open access: yesChemical Reviews, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Mitic, Natasa   +5 more
openaire   +6 more sources

Molecular Insight into the Acryloyl-CoA Hydration by AcuH for Acrylate Detoxification in Dimethylsulfoniopropionate-Catabolizing Bacteria

open access: yesFrontiers in Microbiology, 2017
Microbial cleavage of dimethylsulfoniopropionate (DMSP) producing dimethyl sulfide (DMS) and acrylate is an important step in global sulfur cycling. Acrylate is toxic for cells, and thus should be metabolized effectively for detoxification. There are two
Hai-Yan Cao   +9 more
doaj   +1 more source

Structural and Mechanistic Insights Into Dimethylsulfoxide Formation Through Dimethylsulfide Oxidation

open access: yesFrontiers in Microbiology, 2021
Dimethylsulfide (DMS) and dimethylsulfoxide (DMSO) are widespread in marine environment, and are important participants in the global sulfur cycle. Microbiol oxidation of DMS to DMSO represents a major sink of DMS in marine surface waters.
Xiu-Juan Wang   +17 more
doaj   +1 more source

The catalytic mechanism of galactose mutarotase [PDF]

open access: yesProtein Science, 2003
AbstractGalactose mutarotase catalyzes the first step in normal galactose metabolism by catalyzing the conversion of β‐d‐galactose to α‐d‐galactose. The structure of the enzyme from Lactococcus lactis was recently solved in this laboratory and shown to be topologically similar to domain 5 of β‐galactosidase. From this initial X‐ray analysis, four amino
James B, Thoden   +3 more
openaire   +2 more sources

Glycoside Hydrolase Family 48 Cellulase: A Key Player in Cellulolytic Bacteria for Lignocellulose Biorefinery

open access: yesFermentation, 2023
Cellulases from glycoside hydrolase family 48 (GH48) are critical components of natural lignocellulose-degrading systems. GH48 cellulases are broadly distributed in cellulolytic microorganisms.
Cai You   +3 more
doaj   +1 more source

The catalytic mechanism of sulfoxide synthases

open access: yesCurrent Opinion in Chemical Biology, 2020
Sulfoxide synthases are non-heme iron enzymes that catalyze oxidative carbonsulfur bond formation in the biosynthesis of thiohistidines such as ergothioneine and ovothiol. The catalytic mechanism of these enzymes has been studied by protein crystallography, steady-state kinetics, non-natural amino acid incorporation and computational modeling.
Anja R. Stampfli, Florian P. Seebeck
openaire   +4 more sources

UDP-Glycosyltransferases in Edible Fungi: Function, Structure, and Catalytic Mechanism

open access: yesFermentation, 2023
UDP-glycosyltransferases (UGTs) are the most studied glycosyltransferases, and belong to large GT1 family performing the key roles in antibiotic synthesis, the development of bacterial glycosyltransferase inhibitors, and in animal inflammation.
Yumeng Yang   +6 more
doaj   +1 more source

Catalytic mechanism of thioltransferase

open access: yesJournal of Biological Chemistry, 1991
To evaluate potential catalytic mechanism for thioltransferase thiol-disulfide exchange reactions, seven pig liver mutants were constructed by site-directed mutagenesis. All the expressed enzymes, including wild-type and mutants with the exception of the inactive mutant, ETT-C22S, were variably inhibited by iodoacetamide, and similar results were ...
Y F, Yang, W W, Wells
openaire   +2 more sources

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