Results 1 to 10 of about 43,837 (307)

Protein Engineering for Nicotinamide Coenzyme Specificity in Oxidoreductases: Attempts and Challenges

open access: yesFrontiers in Microbiology, 2018
Oxidoreductases are ubiquitous enzymes that catalyze an extensive range of chemical reactions with great specificity, efficiency, and selectivity. Most oxidoreductases are nicotinamide cofactor-dependent enzymes with a strong preference for NADP or NAD ...
Andrea M Chánique
exaly   +3 more sources

Biotransformation of tobacco-derived Z-abienol into precursors of ambrox by newly identified Acinetobacter tjernbergiae LSC-2 [PDF]

open access: yesFrontiers in Microbiology
Z-abienol is a labdane diterpene present in tobacco leaves and is a key precursor for producing valuable aroma compounds such as ambrox. This study aimed to identify and characterize a bacterial strain that can efficiently degrade Z-abienol through ...
Gaolei Xi   +10 more
doaj   +2 more sources

The Adaptation of MCF-7 Breast Cancer Spheroids to the Chemotherapeutic Doxorubicin: The Dynamic Role of Phase I Drug Metabolizing Enzymes [PDF]

open access: yesMetabolites
Background/Objectives: Drug resistance (DR) is a major challenge in cancer therapy, contributing to approximately 90% of cancer-related deaths. While alterations in drug metabolism are known to be key drivers of DR, their role—particularly in the early ...
Daniel Crispim   +3 more
doaj   +2 more sources

A Structure-Based Approach for Detection of Thiol Oxidoreductases and Their Catalytic Redox-Active Cysteine Residues [PDF]

open access: yesPLoS Computational Biology, 2009
Cysteine (Cys) residues often play critical roles in proteins, for example, in the formation of structural disulfide bonds, metal binding, targeting proteins to the membranes, and various catalytic functions.
Stefano M Marino, Vadim N Gladyshev
exaly   +2 more sources

The Role of Oxidoreductases in Determining the Function of the Neisserial Lipid A Phosphoethanolamine Transferase Required for Resistance to Polymyxin [PDF]

open access: yesPLoS ONE, 2014
The decoration of the lipid A headgroups of the lipooligosaccharide (LOS) by the LOS phosphoethanolamine (PEA) transferase (LptA) in Neisseria spp. is central for resistance to polymyxin.
Jhuma Ganguly   +2 more
exaly   +2 more sources

Change in Cofactor Specificity of Oxidoreductases by Adaptive Evolution of an Escherichia coli NADPH-Auxotrophic Strain

open access: yesmBio, 2021
The nicotinamide cofactor specificity of enzymes plays a key role in regulating metabolic processes and attaining cellular homeostasis. Multiple studies have used enzyme engineering tools or a directed evolution approach to switch the cofactor preference
Madeleine Bouzon   +12 more
doaj   +1 more source

Fungal Treatment for the Valorization of Technical Soda Lignin

open access: yesJournal of Fungi, 2021
Technical lignins produced as a by-product in biorefinery processes represent a potential source of renewable carbon. In consideration of the possibilities of the industrial transformation of this substrate into various valuable bio-based molecules, the ...
Mariane Daou   +12 more
doaj   +1 more source

Laccases: Versatile Biocatalysts for the Synthesis of Heterocyclic Cores

open access: yesMolecules, 2021
Laccases are multicopper oxidases that have shown a great potential in various biotechnological and green chemistry processes mainly due to their high relative non-specific oxidation of phenols, arylamines and some inorganic metals, and their high redox ...
Ana Catarina Sousa   +2 more
doaj   +1 more source

Current Challenges for Biological Treatment of Pharmaceutical-Based Contaminants with Oxidoreductase Enzymes: Immobilization Processes, Real Aqueous Matrices and Hybrid Techniques

open access: yesBiomolecules, 2022
The worldwide access to pharmaceuticals and their continuous release into the environment have raised a serious global concern. Pharmaceuticals remain active even at low concentrations, therefore their occurrence in waterbodies may lead to successive ...
Helena Sá   +3 more
doaj   +1 more source

Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates

open access: yesJournal of Fungi, 2021
A dye-decolorizing peroxidase (DyP) from Irpex lacteus was cloned and heterologously expressed as inclusion bodies in Escherichia coli. The protein was purified in one chromatographic step after its in vitro activation.
Laura Isabel de Eugenio   +6 more
doaj   +1 more source

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