Results 1 to 10 of about 483,724 (361)
Pteridines, 1993 During the past decade numerous advances have been made in understanding the structure, mechanism and clinical properties of dihydropteridine reductase.
Whiteley John M. +4 more
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Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle
Frontiers in Molecular Biosciences, 2023 Biliverdin Reductase B (BLVRB) is an NADPH-dependent reductase that catalyzes the reduction of multiple substrates and is therefore considered a critical cellular redox regulator.
Eunjeong Lee +6 more
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Thiol Reductases in Deinococcus Bacteria and Roles in Stress Tolerance
Antioxidants, 2022 Deinococcus species possess remarkable tolerance to extreme environmental conditions that generate oxidative damage to macromolecules. Among enzymes fulfilling key functions in metabolism regulation and stress responses, thiol reductases (TRs) harbour ...
Arjan de Groot +3 more
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Production of Long Chain Fatty Alcohols Found in Bumblebee Pheromones by Yarrowia lipolytica
Frontiers in Bioengineering and Biotechnology, 2021 Fatty alcohols (FA-OH) are aliphatic unbranched primary alcohols with a chain of four or more carbon atoms. Besides potential industrial applications, fatty alcohols have important biological functions as well. In nature, fatty alcohols are produced as a
Jaroslav Hambalko +6 more
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Biochemical Journal, 2000 The mammalian thioredoxin reductases (TrxRs) are a family of selenium-containing pyridine nucleotide-disulphide oxidoreductases with mechanistic and sequence identity, including a conserved -Cys-Val-Asn-Val-Gly-Cys- redox catalytic site, to glutathione reductases.
D, Mustacich, G, Powis
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Frontiers in Molecular Biosciences, 2023 Thioredoxin/glutathione reductase (TGR) from the platyhelminthic parasitic worms has recently been identified as a drug target for the treatment of schistosomiasis.
Madison M. Smith, Graham R. Moran
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Human Carbonyl Reductase 1 Is an S-Nitrosoglutathione Reductase [PDF]
Journal of Biological Chemistry, 2008 Human carbonyl reductase 1 (hCBR1) is an NADPH-dependent short chain dehydrogenase/reductase with broad substrate specificity and is thought to be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds including xenobiotics.
Brandon Tavshanjian +4 more
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Ketopantoyl lactone reductase is a conjugated polyketone reductase [PDF]
FEMS Microbiology Letters, 1989 Ketopantoyl lactone reductase (EC 1.1.1.168) of Saccharomyces cerevisiae was found to catalyze the reduction of a variety of natural and unnatural conjugated polyketone compounds and quinones, such as isatin, ninhydrin, camphorquinone and beta-naphthoquinone in the presence of NADPH. 5-Bromoisatin is the best substrate for the enzyme (Km = 3.1 mM; Vmax
Sakayu Shimizu +3 more
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Biomolecules, 2023 A unique cytochrome P450 (CYP) oxidoreductase (CPR) sustains activities of human microsomal CYPs. Its function requires toggling between a closed conformation enabling electron transfers from NADPH to FAD and then FMN cofactors and open conformations ...
Francisco Esteves +8 more
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Advanced NanoBiomed Research, 2021 The development of dark pro‐aggregation‐induced‐emission luminogens (pro‐AIEgens) based on the solid‐state intramolecular motion–caused quenching effect has been rarely reported in biochemical analysis.
Changhuo Xu +10 more
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