Results 71 to 80 of about 6,595,197 (312)

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

open access: yesFEBS Letters, EarlyView.
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav   +2 more
wiley   +1 more source

Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01

open access: yesMarine Drugs, 2019
Chondroitinase (ChSase), a type of glycosaminoglycan (GAG) lyase, can degrade chondroitin sulfate (CS) to unsaturate oligosaccharides, with various functional activities. In this study, ChSase AC II from a newly isolated marine bacterium Arthrobacter sp.
Yangtao Fang   +7 more
doaj   +1 more source

Enzymatic production of Volatile Organosulphur Compounds for the Flavour and Fragrance Industry [PDF]

open access: yes, 2013
Volatile organosulphur compounds (VOSC) are a diverse group of chemical entities, which are among the highest impact aroma chemicals (HIACs) in the flavour and fragrance (F&F) industry.
JAMES, AGATA,BARBARA
core  

From junk to function — How weak selection in eukaryotes builds new parts and drives genomic complexity

open access: yesFEBS Letters, EarlyView.
How do genomes gain new functional parts? In eukaryotes, which tend to evolve under weak selection, much of the genome is junk. Palazzo and Qiu borrow the logic of Markov chains to show how non‐functional DNA becomes functional through the appearance of intermediate states, which arise due to epistasis, buffering, and biochemical messiness, allowing ...
Alexander F. Palazzo, Yi Qiu
wiley   +1 more source

Network reorganization of a cold-adapted β-glucosidase couples conformational flexibility to catalytic efficiency under low-temperature conditions

open access: yesFrontiers in Microbiology
IntroductionElucidating how cold-active enzymes maintain efficient catalysis under low-temperature conditions remains a significant question in enzymology.
Xian He   +20 more
doaj   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

open access: yesFEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge   +6 more
wiley   +1 more source

Improvement of Physicochemical and Enzymatic Properties of Bovine Trypsin by Non-enzymatic Glycation

open access: yesBioscience, Biotechnology, and Biochemistry, 1993
Bovine trypsin was modified with glucose through the Maillard reaction at 50°C and 65% RH for various periods (1 to 8 days). Tryptic activity against both benzoyl-L-arginine-p-nitroanilide and two protein substrates was enhanced with increases in the reaction period, and reached the maximum after a 4-day reaction. Although there were no big differences
Kato, Yasuko   +2 more
openaire   +2 more sources

Prospecting the protein design landscape

open access: yesFEBS Letters, EarlyView.
This review outlines the current state of various protein design approaches. We discuss the current possibilities enabled by recently released tools, highlight future avenues to pursue in protein design, and underscore the crucial role of key databases and resources for successful protein design workflows.
Jakob R. Riccabona   +4 more
wiley   +1 more source

Editorial: Biocatalysis and biotransformation guided by protein engineering

open access: yesFrontiers in Bioengineering and Biotechnology, 2023
Chao Li   +5 more
doaj   +1 more source

L‐aspartate oxidase provides new insights into fumarate reduction in anaerobic darkness in Synechocystis sp. PCC6803

open access: yesFEBS Letters, EarlyView.
Synechocystis strains deficient in succinate dehydrogenase (SDH) secrete more succinate than the WT under dark anaerobic conditions, supporting that SDH then primarily acts as SDH, not as a fumarate reductase. L‐aspartate oxidase (Laspo) from Synechocystis is functional under anaerobic conditions, reducing fumarate to succinate.
Kateryna Kukil   +3 more
wiley   +1 more source

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