Relevant bibliographies by topics / NADPH/NADH-dependent reductase

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Academic literature on the topic 'NADPH/NADH-dependent reductase'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "NADPH/NADH-dependent reductase"

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Kleczkowski, L. A., and D. D. Randall. "Purification and characterization of a novel NADPH(NADH)-dependent hydroxypyruvate reductase from spinach leaves. Comparison of immunological properties of leaf hydroxypyruvate reductases." Biochemical Journal 250, no. 1 (1988): 145–52. http://dx.doi.org/10.1042/bj2500145.

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A novel hydroxypyruvate reductase preferring NADPH to NADH as a cofactor was purified over 1500-fold from spinach leaf extracts. The enzyme was an oligomer of about 70 kDa, composed of two subunits of 38 kDa each. The Km for hydroxypyruvate (with NADPH) was about 0.8 mM in the pH range 5.5-6.5, and 0.3 mM at pH 8.2. The Vmax. was highest in the pH range 5.5-6.5 and decreased by about 65% at pH 8.2. Above pH 6.0, the enzyme was prone to a strong substrate inhibition by hydroxypyruvate. The reductase could use glyoxylate as an alternative substrate, with rates up to one-quarter of those with hyd
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Garavaglia, Patricia Andrea, Marc Laverrière, Joaquín J. B. Cannata, and Gabriela Andrea García. "Putative Role of the Aldo-Keto Reductase from Trypanosoma cruzi in Benznidazole Metabolism." Antimicrobial Agents and Chemotherapy 60, no. 5 (2016): 2664–70. http://dx.doi.org/10.1128/aac.02185-15.

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ABSTRACTBenznidazole (Bz), the drug used for treatment of Chagas' disease (caused by the protozoanTrypanosoma cruzi), is activated by a parasitic NADH-dependent type I nitroreductase (NTR I). However, several studies have shown that other enzymes are involved. The aim of this study was to evaluate whether the aldo-keto reductase fromT. cruzi(TcAKR), a NADPH-dependent oxido-reductase previously described by our group, uses Bz as the substrate. We demonstrated that both recombinant and nativeTcAKR enzymes reduce Bz by using NADPH, but not NADH, as a cofactor.TcAKR-overexpressing epimastigotes sh
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Yeom, Jinki, Che Ok Jeon, Eugene L. Madsen, and Woojun Park. "Ferredoxin-NADP+ Reductase from Pseudomonas putida Functions as a Ferric Reductase." Journal of Bacteriology 191, no. 5 (2008): 1472–79. http://dx.doi.org/10.1128/jb.01473-08.

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ABSTRACT Pseudomonas putida harbors two ferredoxin-NADP+ reductases (Fprs) on its chromosome, and their functions remain largely unknown. Ferric reductase is structurally contained within the Fpr superfamily. Interestingly, ferric reductase is not annotated on the chromosome of P. putida. In an effort to elucidate the function of the Fpr as a ferric reductase, we used a variety of biochemical and physiological methods using the wild-type and mutant strains. In both the ferric reductase and flavin reductase assays, FprA and FprB preferentially used NADPH and NADH as electron donors, respectivel
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ENTRALA, E., C. MASCARO, and J. BARRETT. "Anti-oxidant enzymes in Cryptosporidium parvum oocysts." Parasitology 114, no. 1 (1997): 13–17. http://dx.doi.org/10.1017/s0031182096008037.

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Oocysts of Cryptosporidium parvum showed relatively low levels of SOD activity. The SOD which had a pI of 4.8 and an approximate molecular weight of 35 kDa appeared to be iron dependent. Catalase, glutathione transferase, glutathione reductase and glutathione peroxidase activity could not be detected, nor could trypanothione reductase. No NADH or NADPH oxidase activity could be detected, nor could peroxidase activity be demonstrated using o-dianisidine, guaiacol, NADPH or NADH as co-substrates. However, an NADPH-dependent H2O2 scavenging system was detected in the insoluble fraction.
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PETSCHACHER, Barbara, Stefan LEITGEB, Kathryn L. KAVANAGH, David K. WILSON, and Bernd NIDETZKY. "The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography." Biochemical Journal 385, no. 1 (2004): 75–83. http://dx.doi.org/10.1042/bj20040363.

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CtXR (xylose reductase from the yeast Candida tenuis; AKR2B5) can utilize NADPH or NADH as co-substrate for the reduction of D-xylose into xylitol, NADPH being preferred approx. 33-fold. X-ray structures of CtXR bound to NADP+ and NAD+ have revealed two different protein conformations capable of accommodating the presence or absence of the coenzyme 2′-phosphate group. Here we have used site-directed mutagenesis to replace interactions specific to the enzyme–NADP+ complex with the aim of engineering the co-substrate-dependent conformational switch towards improved NADH selectivity. Purified sin
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Argyrou, Argyrides, Matthew W. Vetting, and John S. Blanchard. "Characterization of a New Member of the Flavoprotein Disulfide Reductase Family of Enzymes fromMycobacterium tuberculosis." Journal of Biological Chemistry 279, no. 50 (2004): 52694–702. http://dx.doi.org/10.1074/jbc.m410704200.

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ThelpdA(Rv3303c) gene fromMycobacterium tuberculosisencoding a new member of the flavoprotein disulfide reductases was expressed inEscherichia coli, and the recombinant LpdA protein was purified to homogeneity. LpdA is a homotetramer and co-purifies with one molecule of tightly but noncovalently bound FAD and NADP+per monomer. Although annotated as a probable lipoamide dehydrogenase inM. tuberculosis, LpdA cannot catalyze reduction of lipoyl substrates, because it lacks one of two cysteine residues involved in dithiol-disulfide interchange with lipoyl substrates and a His-Glu pair involved in
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LÓPEZ-HUERTAS, Eduardo, Francisco J. CORPAS, Luisa M. SANDALIO, and Luis A. DEL RÍO. "Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation." Biochemical Journal 337, no. 3 (1999): 531–36. http://dx.doi.org/10.1042/bj3370531.

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The production of superoxide radicals (O2-•) and the activities of ferricyanide reductase and cytochrome c reductase were investigated in peroxisomal membranes from pea (Pisum sativum L.) leaves using NADH and NADPH as electron donors. The generation of O2-• by peroxisomal membranes was also assayed in native polyacrylamide gels using an in situ staining method with NitroBlue Tetrazolium (NBT). When peroxisomal membranes were assayed under native conditions using NADH or NADPH as inducer, two different O2-•-dependent Formazan Blue bands were detected. Analysis by SDS/PAGE of these bands demons
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Proskurnina, E., M. Sozarukova, M. Fedorova, and M. Kiseleva. "ANALYSIS OF MICROSOMAL REDUCTASE ACTIVITY IN OVARIAN TISSUE AFTER CRYOPRESERVATION BY ENHANCED CHEMILUMINESCENCE." Russian Journal of Biological Physics and Chemisrty 7, no. 3 (2022): 434–39. http://dx.doi.org/10.29039/rusjbpc.2022.0540.

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The aim of the study was to investigate the activity of NADH-dependent cytochrome b5 reductase (CYB5R) and NADPH-dependent cytochrome P450 reductase (CYPOR) in ovarian tissues after cryopreservation by lucigenin-enhanced chemiluminescence with NADH and NADPH stimulation, respectively. The results indicate that both mitochondrial and microsomal reductase activities are preserved in cryopreserved ovarian tissues. After cryopreservation, the level of production of superoxide anion radical by mitochondria drops by 3–10 times, while the presence or absence of chemotherapy has no effect, and this pa
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Stockinger, Peter, Niels Borlinghaus, Mahima Sharma, Benjamin Aberle, Gideon James Grogan, and Bettina Nestl. "Inverting the Stereoselectivity of an NADH-Dependent Imine-Reductase Variant." ChemCatChem 13 (December 15, 2021): 5210–15. https://doi.org/10.1002/cctc.202101057.

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Abstract Imine reductases (IREDs) offer biocatalytic routes to chiral amines and have a natural preference for the NADPH cofactor. In previous work, we reported enzyme engineering of the (<em>R</em>)-selective IRED from <em>Myxococcus stipitatus </em>(NADH-IRED-<em>Ms</em>) yielding a NADH-dependent variant with high catalytic efficiency. However, no IRED with NADH specificity and (<em>S</em>)-selectivity in asymmetric reductions has yet been reported. Herein, we applied semi-rational enzyme engineering to switch the selectivity of NADH-IRED-<em>Ms. </em>The quintuple variant A241V/ H242Y/N243
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Benveniste, I., A. Lesot, M. P. Hasenfratz, and F. Durst. "Immunochemical characterization of NADPH-cytochrome P-450 reductase from Jerusalem artichoke and other higher plants." Biochemical Journal 259, no. 3 (1989): 847–53. http://dx.doi.org/10.1042/bj2590847.

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Polyclonal antibodies were prepared against NADPH-cytochrome P-450 reductase purified from Jerusalem artichoke. These antibodies inhibited efficiently the NADPH-cytochrome c reductase activity of the purified enzyme, as well as of Jerusalem artichoke microsomes. Likewise, microsomal NADPH-dependent cytochrome P-450 mono-oxygenases (cinnamate and laurate hydroxylases) were efficiently inhibited. The antibodies were only slightly inhibitory toward microsomal NADH-cytochrome c reductase activity, but lowered NADH-dependent cytochrome P-450 mono-oxygenase activities. The Jerusalem artichoke NADPH-
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Dissertations / Theses on the topic "NADPH/NADH-dependent reductase"

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Shorrock, Vicky Jane. "An NADH dependent reductase for isolated enzyme and whole cell catalysis." Thesis, University College London (University of London), 2006. http://discovery.ucl.ac.uk/1445080/.

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Isolated enzymes and whole cell biocatalysts can both be applied for the synthesis of chiral hydroxy compounds. It is hypothesized that whole cells can easily be employed for such reactions using simple technology which is robust. This is because whole cells contain all the necessary enzymes and metabolic pathways for cofactor regeneration. This also means that the enzymes and their cofactors are well-protected within their natural cell environment. In contrast, it is hypothesized that isolated enzymes require complicated and expensive purification procedures. They also require the stoichiomet
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Greenler, John McClure. "Regulation of NADH-dependent hydroxypyruvate reductase transcript abundance in cucumber seedlings." 1990. http://catalog.hathitrust.org/api/volumes/oclc/22433078.html.

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Thesis (Ph. D.)--University of Wisconsin-Madison, 1990.<br>Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
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Schwartz, Brian William. "Cloning and analysis of regulation of a cucumber gene encoding NADH-dependent hydroxypyruvate reductase." 1992. http://catalog.hathitrust.org/api/volumes/oclc/28757883.html.

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Book chapters on the topic "NADPH/NADH-dependent reductase"

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Stöhr, Christine, Stefanie Wienkoop, and Wolfram R. Ullrich. "Nitrate reductase in roots: Succinate- and NADH-dependent plasma membrane-bound forms." In Recent Advances of Plant Root Structure and Function. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-017-2858-4_14.

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Caubergs, Roland, Han Asard, and Jan A. De Greef. "b-Type Cytochromes, Light- and NADH-Dependent Oxido-Reductase Activities in Plant Plasma Membranes." In Plasma Membrane Oxidoreductases in Control of Animal and Plant Growth. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-8029-0_30.

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Arinç, Emel. "Essential Features of NADH Dependent Cytochrome b5 Reductase and Cytochrome b5 of Liver and Lung Microsomes." In Molecular Aspects of Monooxygenases and Bioactivation of Toxic Compounds. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-7284-4_9.

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"Vitamin B2 Riboflavin." In The Chemical Biology of Human Vitamins. The Royal Society of Chemistry, 2018. http://dx.doi.org/10.1039/bk9781788014649-00104.

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Riboflavin is vitamin B2. In vivo it is converted to the coenzyme forms FMN and FAD, by tandem phosphorylation and adenylation, respectively. The tricyclic isoalloxazine ring is the business end of the flavins and can undergo either two electron reduction (e.g. hydride transfer from NADH) or two single electron reductive steps (e.g. from O2) in metabolism. The ability to serve as a stepdown 2/1 electron transfer reagent puts flavin-dependent enzymes at crucial metabolic nodes in both catabolic and anabolic pathways.
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Frey, Perry A., and Adrian D. Hegeman. "Oxidoreductases." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0020.

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Oxidoreductases constitute a very large class of enzymes. They are dehydrogenases and reductases that catalyze the removal or addition of the elements of molecular hydrogen to or from substrates. Enzymatic dehydrogenation is sometimes linked to auxiliary functions such as decarboxylation, deamination, or dehydration of the substrate, as in the actions of isocitrate dehydrogenase (decarboxylation), glutamate dehydrogenase (deamination), and ribonucleotide reductase (deoxygenation). The best known oxidoreductases are the NAD-dependent dehydrogenases, and a thorough discussion of the actions of t
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Frey, Perry A., and Adrian D. Hegeman. "Complex Enzymes." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0022.

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Most enzymes discussed in the preceding chapters consist of single proteins that catalyze single biochemical reactions. Many of them contain one type of polypeptide chain, although most exist as oligomers of a polypeptide, and some consist of different polypeptides that cooperate to catalyze one reaction. Increasing attention is being focused on enzymes that catalyze more complex processes and are composed of more than one enzyme or enzymatic domain, each of which catalyzes or facilitates a specific biochemical process. These complex enzymes are the subjects of this chapter. Complex enzymes ar
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