Results 1 to 10 of about 330,401 (264)
Molecules, 2021 Mitomycin has a unique chemical structure and contains densely assembled functionalities with extraordinary antitumor activity. The previously proposed mitomycin C biosynthetic pathway has caused great attention to decipher the enzymatic mechanisms for ...
Dongjin Leng +7 more
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Molecules, 2023 The mitochondrial amidoxime-reducing component (mARC) is the most recently discovered molybdoenzyme in humans after sulfite oxidase, xanthine oxidase and aldehyde oxidase. Here, the timeline of mARC’s discovery is briefly described. The story begins with
Bernd Clement, Michel A. Struwe
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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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Phytophthora capsici sterol reductase PcDHCR7 has a role in mycelium development and pathogenicity
Open Biology, 2022 The de novo biosynthesis of sterols is critical for the majority of eukaryotes; however, some organisms lack this pathway, including most oomycetes. Phytophthora spp.
Weizhen Wang +6 more
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Chromium bioremediation by Alcaligenes sp. strain newly isolated from chromite mine of Sabzevar [PDF]
Journal of Advances in Environmental Health Research, 2017 In this work, CKCr-6A strain was found to be highly resistant to some toxic heavy metals such as Cr+6, Cr+3, Cu+2, Co+2, Cd+2, Pb+2, Hg+2, U+6, tellurium, and selenite. Herein, high chromate tolerance of an isolated strain is reported with a high minimum
Mohsen Mesbahi-Nowrouzi +2 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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RIBONUCLEOTIDE REDUCTASES [PDF]
Annual Review of Biochemistry, 1998 Ribonucleotide reductases provide the building blocks for DNA replication in all living cells. Three different classes of enzymes use protein free radicals to activate the substrate. Aerobic class I enzymes generate a tyrosyl radical with an iron-oxygen center and dioxygen, class II enzymes employ adenosylcobalamin, and the anaerobic class III enzymes
A, Jordan, P, Reichard
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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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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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Chloroplast Glutathione Reductase [PDF]
Plant Physiology, 1977 Glutathione reductase (EC 1.6.4.2) activity is present in spinach (Spinacia oleracea L.) chloroplasts. The pH dependence and substrate concentration for half-maximal rate are reported and a possible role in chloroplasts is proposed.
Michail Schaedle, James A. Bassham
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