Results 21 to 30 of about 11,574 (255)
A desired product cannot be obtained at higher concentration than its equilibrium concentration when isomerases are used for biotransformation. Here, the authors engineer in vivo oxidoreductive reactions in yeast to overcome the equilibrium limitation of
Jing-Jing Liu +7 more
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Rhodopsin is formed by the condensation of opsin with a cis isomer of retinene, called neo-b. The bleaching of rhodopsin releases all-trans retinene which must be isomerized back to neo-b in order for rhodopsin to regenerate. Both retinene isomers are in equilibrium with the corresponding isomers of vitamin A, through the alcohol dehydrogenase system.
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Rare arginine codons AGA and AGG affect the heterologous expression of proteins in Eschericha coli. The tRNAs necessary for protein synthesis are scarce in E. coli strain BL21(DE3) pLysS and plentiful in strain BL21(DE3) CodonPlus −RIL.
Beatriz Aguirre-López +4 more
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Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series
About 30 years after the discovery of peptidyl-prolyl cis/trans isomerases (PPIases), research on this group of proteins has become somewhat calmer than it used to be, but it still generates lots of interest [...]
Andrzej Galat
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Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes. [PDF]
Proteins with great sequence similarity usually have similar structure, function and other physicochemical properties. But in many cases, one or more of the physicochemical or functional characteristics differ, sometimes very considerably, among these ...
Selma Díaz-Mazariegos +2 more
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Cancer stem cells (CSCs) are a great challenge in the fight against cancer because these self-renewing tumorigenic cell fractions are thought to be responsible for metastasis dissemination and cases of tumor recurrence. In comparison with non-stem cancer
Alexander Kabakov +2 more
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Vascular thiol isomerases [PDF]
AbstractThiol isomerases are multifunctional enzymes that influence protein structure via their oxidoreductase, isomerase, and chaperone activities. These enzymes localize at high concentrations in the endoplasmic reticulum of all eukaryotic cells where they serve an essential function in folding nascent proteins.
Robert, Flaumenhaft, Bruce, Furie
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Is EC class predictable from reaction mechanism?
Background We investigate the relationships between the EC (Enzyme Commission) class, the associated chemical reaction, and the reaction mechanism by building predictive models using Support Vector Machine (SVM), Random Forest (RF) and k-Nearest ...
Nath Neetika, Mitchell John BO
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A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
Bacterial disulfide isomerases shuffle incorrect disulfide bonds. Here, the authors structurally characterize the disulfide isomerase ScsC fromProteus mirabilisand identify a functionally important shape-shifting motif that allows ScsC to adopt a diverse
Emily J. Furlong +11 more
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THIOL ISOMERASES – A POSSIBLE TARGET FOR THROMBOSIS CONTROL
While there are an increasing number of antithrombotic agents with demonstrated clinical efficacy, thrombosis remains the leading cause of mortality in developed countries. Therefore, there is a need further development of therapies targeting alternative
I. V. Gribkova, M. V. Davydovskaya
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