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

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Published: 3 June 2025

Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Sheppard, Christal A., Elizabeth E. Trimmer, and Rowena G. Matthews. "Purification and Properties of NADH-Dependent 5,10-Methylenetetrahydrofolate Reductase (MetF) fromEscherichia coli." Journal of Bacteriology 181, no. 3 (1999): 718–25. http://dx.doi.org/10.1128/jb.181.3.718-725.1999.

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ABSTRACT A K-12 strain of Escherichia coli that overproduces methylenetetrahydrofolate reductase (MetF) has been constructed, and the enzyme has been purified to apparent homogeneity. A plasmid specifying MetF with six histidine residues added to the C terminus has been used to purify histidine-tagged MetF to homogeneity in a single step by affinity chromatography on nickel-agarose, yielding a preparation with specific activity comparable to that of the unmodified enzyme. The native protein comprises four identical 33-kDa subunits, each of which contains a molecule of noncovalently bound flavi

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12

Yang, Xianqin, and Kesen Ma. "Characterization of a Thioredoxin-Thioredoxin Reductase System from the Hyperthermophilic Bacterium Thermotoga maritima." Journal of Bacteriology 192, no. 5 (2010): 1370–76. http://dx.doi.org/10.1128/jb.01035-09.

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ABSTRACT A thioredoxin reductase and a thioredoxin were purified to homogeneity from a cell extract of Thermotoga maritima. The thioredoxin reductase was a homodimeric flavin adenine dinucleotide (FAD)-containing protein with a subunit of 37 kDa estimated using SDS-PAGE, which was identified to be TM0869. The amino acid sequence of the enzyme showed high identities and similarities to those of typical bacterial thioredoxin reductases. Although the purified T. maritima thioredoxin reductase could not use thioredoxin from Spirulina as an electron acceptor, it used thioredoxin that was purified f

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13

FIORAVANTI, C. F., and K. P. VANDOCK. "Transhydrogenase and the anaerobic mitochondrial metabolism of adult Hymenolepis diminuta." Parasitology 137, no. 3 (2009): 395–410. http://dx.doi.org/10.1017/s0031182009990904.

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SUMMARYThe adult cestode, Hymenolepis diminuta, is essentially anaerobic energetically. Carbohydrate dissimilation results in acetate, lactate and succinate accumulation with succinate being the major end product. Succinate accumulation results from the anaerobic, mitochondrial, ‘malic’ enzyme-dependent utilization of malate coupled to ATP generation via the electron transport-linked fumarate reductase. A lesser peroxide-forming oxidase is apparent, however, fumarate reduction to succinate predominates even in air. The H. diminuta matrix-localized ‘malic’ enzyme is NADP-specific whereas the in

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14

Chohan, Shahid N., and Les Copeland. "Acetoacetyl Coenzyme A Reductase and Polyhydroxybutyrate Synthesis in Rhizobium(Cicer) sp. Strain CC 1192." Applied and Environmental Microbiology 64, no. 8 (1998): 2859–63. http://dx.doi.org/10.1128/aem.64.8.2859-2863.1998.

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ABSTRACT Biochemical controls that regulate the biosynthesis of poly-3-hydroxybutyrate (PHB) were investigated in Rhizobium(Cicer) sp. strain CC 1192. This species is of interest for studying PHB synthesis because the polymer accumulates to a large extent in free-living cells but not in bacteroids during nitrogen-fixing symbiosis with chickpea (Cicer arietinumL.) plants. Evidence is presented that indicates that CC 1192 cells retain the enzymic capacity to synthesize PHB when they differentiate from the free-living state to the bacteroid state. This evidence includes the incorporation by CC 11

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15

Wang, Mingxuan, Jing Li, Wenjie Cong та Jianguo Zhang. "NADPH–Cytochrome P450 Reductase Mediates the Fatty Acid Desaturation of ω3 and ω6 Desaturases from Mortierella alpina". Current Issues in Molecular Biology 44, № 5 (2022): 1828–37. http://dx.doi.org/10.3390/cimb44050125.

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Fatty acid desaturases play an important role in maintaining the appropriate structure and function of biological membranes. The biochemical characterization of integral membrane desaturases, particularly ω3 and ω6 desaturases, has been limited by technical difficulties relating to the acquisition of large quantities of purified proteins, and by the fact that functional activities of these proteins were only tested in an NADH-initiated reaction system. The main aim of this study was to reconstitute an NADPH-dependent reaction system in vitro and investigate the kinetic properties of Mortierell

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16

Benveniste, I., B. Gabriac, and F. Durst. "Purification and characterization of the NADPH-cytochrome P-450 (cytochrome c) reductase from higher-plant microsomal fraction." Biochemical Journal 235, no. 2 (1986): 365–73. http://dx.doi.org/10.1042/bj2350365.

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NADPH-cytochrome P-450 (cytochrome c) reductase (EC 1.6.2.4) was solubilized by detergent from microsomal fraction of wounded Jerusalem-artichoke (Helianthus tuberosus L.) tubers and purified to electrophoretic homogeneity. The purification was achieved by two anion-exchange columns and by affinity chromatography on 2′,5′-bisphosphoadenosine-Sepharose 4B. An Mr value of 82,000 was obtained by SDS/polyacrylamide-gel electrophoresis. The purified enzyme exhibited typical flavoprotein redox spectra and contained equimolar quantities of FAD and FMN. The purified enzyme followed Michaelis-Menten ki

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17

Kleczkowski, L. A., D. D. Randall, and D. G. Blevins. "Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase." Biochemical Journal 239, no. 3 (1986): 653–59. http://dx.doi.org/10.1042/bj2390653.

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A novel reductase displaying high specificity for glyoxylate and NADPH was purified 3343-fold from spinach leaves. The enzyme was found to be an oligomer of about 125 kDa, composed of four equal subunits of 33 kDa each. A Km for glyoxylate was about 14-fold lower with NADPH than with NADH (0.085 and 1.10 mM respectively), but the maximal activity, 210 mumol/min per mg of protein, was similar with either cofactor. Km values for NADPH and NADH were 3 and 150 microM respectively. Optimal rates with either NADPH or NADH were found in the pH range 6.5-7.4. The enzyme also showed some reactivity tow

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18

Franklin, Edward, Seamus Browne, Jerrard Hayes та ін. "Activation of biliverdin-IXα reductase by inorganic phosphate and related anions". Biochemical Journal 405, № 1 (2007): 61–67. http://dx.doi.org/10.1042/bj20061651.

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The effect of pH on the initial-rate kinetic behaviour of BVR-A (biliverdin-IXα reductase) exhibits an alkaline optimum with NADPH as cofactor, but a neutral optimum with NADH as cofactor. This has been described as dual cofactor and dual pH dependent behaviour; however, no mechanism has been described to explain this phenomenon. We present evidence that the apparent peak of activity observed at neutral pH with phosphate buffer and NADH as cofactor is an anion-dependent activation, where inorganic phosphate apparently mimics the role played by the 2′-phosphate of NADPH in stabilizing the inter

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19

Nishizawa, Akito, Ayaka Harada, Miki Senda, et al. "Complete pyridine-nucleotide-specific conversion of an NADH-dependent ferredoxin reductase." Biochemical Journal 462, no. 2 (2014): 257–65. http://dx.doi.org/10.1042/bj20140384.

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An NADH-specific ferredoxin reductase component, BphA4 of biphenyl dioxygenase BphA from Acidovorax sp. strain KKS102, was changed to an NADPH-dependent form using a method combining structure-based systematic mutations and site-directed random mutagenesis.

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20

Ahmed ABASS, Hend. "ALDOSE REDUCTASE ENZYME'S CLINICAL AND THERMODYNAMIC CHARACTERISTICS IN THE SERUM OF IRAQI DIABETIC PATIENTS." MINAR International Journal of Applied Sciences and Technology 05, no. 04 (2023): 17–28. http://dx.doi.org/10.47832/2717-8234.17.2.

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A superfamily of aldo-keto reductases includes the monomeric NADPH-dependent cytosolic enzyme aldose reductase (AR). When hyperglycemia, increased glucose levels stimulate the AR, which activates the polyol pathway and results in glucose metabolism, the dangerous aldehydes created by reactive oxygen species (ROS) into innocuous alcohols. NADPH is a crucial cofactor in the formation of glutathione (GSH), a crucial antioxidant, and its consumption lowers GSH levels. The main causes problems of diabetes are osmotic stress brought on by the buildup of excess AR and oxidative stress brought on by a

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21

Hoang, Tung T., and Herbert P. Schweizer. "Characterization of Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI): a Target for the Antimicrobial Triclosan and Its Role in Acylated Homoserine Lactone Synthesis." Journal of Bacteriology 181, no. 17 (1999): 5489–97. http://dx.doi.org/10.1128/jb.181.17.5489-5497.1999.

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ABSTRACT The Pseudomonas aeruginosa fabI structural gene, encoding enoyl-acyl carrier protein (ACP) reductase, was cloned and sequenced. Nucleotide sequence analysis revealed that fabIis probably the last gene in a transcriptional unit that includes a gene encoding an ATP-binding protein of an ABC transporter of unknown function. The FabI protein was similar in size and primary sequence to other bacterial enoyl-ACP reductases, and it contained signature motifs for the FAD-dependent pyridine nucleotide reductase and glucose/ribitol dehydrogenase families, respectively. The chromosomal fabIgene

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22

Forlani, Giuseppe, Giuseppe Sabbioni, and Milosz Ruszkowski. "Functional Characterization of Saccharomyces cerevisiae P5C Reductase, the Enzyme at the Converging Point of Proline and Arginine Metabolism." Microorganisms 10, no. 10 (2022): 2077. http://dx.doi.org/10.3390/microorganisms10102077.

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The enzyme that, in Saccharomyces cerevisiae, catalyzes the last step in both proline synthesis and arginine catabolism, d1-pyrroline-5-carboxylate (P5C) reductase, was purified to near homogeneity and characterized thoroughly. Retention patterns upon gel permeation chromatography were consistent with a homodecameric composition of the holomer. High lability of the purified preparations and stabilization by reducing compounds suggested susceptibility to reactive-oxygen-species-mediated damage. Both NADH and NADPH were used as the electron donor, the latter resulting in a 3-fold higher Vmax. Ho

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23

Hertzberger, Rosanne, Jos Arents, Henk L. Dekker, et al. "H2O2Production in Species of the Lactobacillus acidophilus Group: a Central Role for a Novel NADH-Dependent Flavin Reductase." Applied and Environmental Microbiology 80, no. 7 (2014): 2229–39. http://dx.doi.org/10.1128/aem.04272-13.

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ABSTRACTHydrogen peroxide production is a well-known trait of many bacterial species associated with the human body. In the presence of oxygen, the probiotic lactic acid bacteriumLactobacillus johnsoniiNCC 533 excretes up to 1 mM H2O2, inducing growth stagnation and cell death. Disruption of genes commonly assumed to be involved in H2O2production (e.g., pyruvate oxidase, NADH oxidase, and lactate oxidase) did not affect this. Here we describe the purification of a novel NADH-dependent flavin reductase encoded by two highly similar genes (LJ_0548andLJ_0549) that are conserved in lactobacilli be

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24

Mondal, S., C. Nagao, and K. Muzuguchi. "Comparative analysis of putative NADPH- and NADH-dependent ketopantoate reductase." Acta Crystallographica Section A Foundations of Crystallography 64, a1 (2008): C228. http://dx.doi.org/10.1107/s0108767308092672.

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25

LEADBEATER, Claire, Lisa MCIVER, Dominic J. CAMPOPIANO, et al. "Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase." Biochemical Journal 352, no. 2 (2000): 257–66. http://dx.doi.org/10.1042/bj3520257.

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The structure of the Escherichia coli flavodoxin NADP+ oxidoreductase (FLDR) places three arginines (R144, R174 and R184) in the proposed NADPH-binding site. Mutant enzymes produced by site-directed mutagenesis, in which each arginine was replaced by neutral alanine, were characterized. All mutants exhibited decreased NADPH-dependent cytochrome c reductase activity (R144A, 241.6min-1; R174A, 132.1min-1; R184A, 305.5min-1 versus wild type, 338.9min-1) and increased Km for NADPH (R144A, 5.3µM; R174A, 20.2µM; R184A, 54.4µM versus wild type, 3.9µM). The kcat value for NADH-dependent cytochrome c r

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Opperman, Diederik Johannes, Lizelle Ann Piater, and Esta van Heerden. "A Novel Chromate Reductase from Thermus scotoductus SA-01 Related to Old Yellow Enzyme." Journal of Bacteriology 190, no. 8 (2008): 3076–82. http://dx.doi.org/10.1128/jb.01766-07.

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ABSTRACT Bacteria can reduce toxic and carcinogenic Cr(VI) to insoluble and less toxic Cr(III). Thermus scotoductus SA-01, a South African gold mine isolate, has been shown to be able to reduce a variety of metals, including Cr(VI). Here we report the purification to homogeneity and characterization of a novel chromate reductase. The oxidoreductase is a homodimeric protein, with a monomer molecular mass of approximately 36 kDa, containing a noncovalently bound flavin mononucleotide cofactor. The chromate reductase is optimally active at a pH of 6.3 and at 65°C and requires Ca2+ or Mg2+ for act

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27

Shabdar, Sherwin, Bukuru Anaclet, Ana Garcia Castineiras, et al. "Structural and Kinetic Characterization of Hyperthermophilic NADH-Dependent Persulfide Reductase from Archaeoglobus fulgidus." Archaea 2021 (March 9, 2021): 1–9. http://dx.doi.org/10.1155/2021/8817136.

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NADH-dependent persulfide reductase (Npsr) has been proposed to facilitate dissimilatory sulfur respiration by reducing persulfide or sulfane sulfur-containing substrates to H2S. The presence of this gene in the sulfate and thiosulfate-reducing Archaeoglobus fulgidus DSM 4304 and other hyperthermophilic Archaeoglobales appears anomalous, as A. fulgidus is unable to respire S0 and grow in the presence of elemental sulfur. To assess the role of Npsr in the sulfur metabolism of A. fulgidus DSM 4304, the Npsr from A. fulgidus was characterized. AfNpsr is specific for persulfide and polysulfide as

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Raedts, John, Marco A. J. Siemerink, Mark Levisson, John van der Oost, and Servé W. M. Kengen. "Molecular Characterization of an NADPH-Dependent Acetoin Reductase/2,3-Butanediol Dehydrogenase fromClostridium beijerinckiiNCIMB 8052." Applied and Environmental Microbiology 80, no. 6 (2014): 2011–20. http://dx.doi.org/10.1128/aem.04007-13.

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ABSTRACTAcetoin reductase is an important enzyme for the fermentative production of 2,3-butanediol, a chemical compound with a very broad industrial use. Here, we report on the discovery and characterization of an acetoin reductase fromClostridium beijerinckiiNCIMB 8052. Anin silicoscreen of theC. beijerinckiigenome revealed eight potential acetoin reductases. One of them (CBEI_1464) showed substantial acetoin reductase activity after expression inEscherichia coli. The purified enzyme (C. beijerinckiiacetoin reductase [Cb-ACR]) was found to exist predominantly as a homodimer. In addition to ac

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29

Lee, Jung-Kul, Sang-Yong Kim, Yeon-Woo Ryu, Jin-Ho Seo, and Jung-Hoe Kim. "Purification and Characterization of a Novel Erythrose Reductase from Candida magnoliae." Applied and Environmental Microbiology 69, no. 7 (2003): 3710–18. http://dx.doi.org/10.1128/aem.69.7.3710-3718.2003.

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ABSTRACT Erythritol biosynthesis is catalyzed by erythrose reductase, which converts erythrose to erythritol. Erythrose reductase, however, has never been characterized in terms of amino acid sequence and kinetics. In this study, NAD(P)H-dependent erythrose reductase was purified to homogeneity from Candida magnoliae KFCC 11023 by ion exchange, gel filtration, affinity chromatography, and preparative electrophoresis. The molecular weights of erythrose reductase determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography were 38,800 and 79,000, resp

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30

Tauber, AI, J. Wright, FK Higson, SA Edelman, and DJ Waxman. "Purification and characterization of the human neutrophil NADH- cytochrome b5 reductase." Blood 66, no. 3 (1985): 673–78. http://dx.doi.org/10.1182/blood.v66.3.673.673.

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Abstract NADH-cytochrome b5 reductase is the predominant NADH-diaphorase found in the human neutrophil (Blood 62:152, 1983). Although this reductase segregates with the light membranes of nitrogen-cavitated neutrophils separated on Percoll gradients (which include the plasma membrane markers alkaline phosphatase and NADPH-oxidase), it is approximately 95% excluded from plasma membrane-enriched phagocytic vacuoles. The reductase constitutes approximately 5% of the light membrane fraction FAD-flavoprotein (14.8 +/- 5.5 pmol/mg protein) and was found in equimolar concentration with a high potenti

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Tauber, AI, J. Wright, FK Higson, SA Edelman, and DJ Waxman. "Purification and characterization of the human neutrophil NADH- cytochrome b5 reductase." Blood 66, no. 3 (1985): 673–78. http://dx.doi.org/10.1182/blood.v66.3.673.bloodjournal663673.

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NADH-cytochrome b5 reductase is the predominant NADH-diaphorase found in the human neutrophil (Blood 62:152, 1983). Although this reductase segregates with the light membranes of nitrogen-cavitated neutrophils separated on Percoll gradients (which include the plasma membrane markers alkaline phosphatase and NADPH-oxidase), it is approximately 95% excluded from plasma membrane-enriched phagocytic vacuoles. The reductase constitutes approximately 5% of the light membrane fraction FAD-flavoprotein (14.8 +/- 5.5 pmol/mg protein) and was found in equimolar concentration with a high potential b cyto

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32

Dème, D., J. Doussiere, V. De Sandro, C. Dupuy, J. Pommier, and A. Virion. "The Ca2+/NADPH-dependent H2O2 generator in thyroid plasma membrane: inhibition by diphenyleneiodonium." Biochemical Journal 301, no. 1 (1994): 75–81. http://dx.doi.org/10.1042/bj3010075.

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The thyroid plasma membrane contains a Ca(2+)-regulated NADPH-dependent H2O2-generating system which provides H2O2 for the peroxidase-catalysed biosynthesis of thyroid hormones. The electron transfer from NADPH to O2 catalysed by this system was studied by using diphenyleneiodonium (DPI), an inhibitor of flavo- and haemo-proteins. The prosthetic group of the H2O2 generator was removed by incubation with 5 mM CHAPS at 40 degrees C, and an active holoenzyme was reconstituted with FAD, but not with FMN. The H2O2-generating system also had an intrinsic Ca(2+)-dependent NADPH:ferricyanide reductase

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Case, Christopher L., Jason R. Rodriguez, and Biswarup Mukhopadhyay. "Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii." Microbiology 155, no. 1 (2009): 69–79. http://dx.doi.org/10.1099/mic.0.024265-0.

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Methanocaldococcus jannaschii, a deeply rooted hyperthermophilic anaerobic methanarchaeon from a deep-sea hydrothermal vent, carries an NADH oxidase (Nox) homologue (MJ0649). According to the characteristics described here, MJ0649 represents an unusual member within group 3 of the flavin-dependent disulfide reductase (FDR) family. This FDR group comprises Nox, NADH peroxidases (Npx) and coenzyme A disulfide reductases (CoADRs); each carries a Cys residue that forms Cys-sulfenic acid during catalysis. A sequence analysis identified MJ0649 as a CoADR homologue. However, recombinant MJ0649 (rMJNo

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Buey, Rubén M., David Fernández-Justel, José M. de Pereda, et al. "Ferredoxin-linked flavoenzyme defines a family of pyridine nucleotide-independent thioredoxin reductases." Proceedings of the National Academy of Sciences 115, no. 51 (2018): 12967–72. http://dx.doi.org/10.1073/pnas.1812781115.

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Ferredoxin-dependent thioredoxin reductase was identified 35 y ago in the fermentative bacterium Clostridium pasteurianum [Hammel KE, Cornwell KL, Buchanan BB (1983) Proc Natl Acad Sci USA 80:3681–3685]. The enzyme, a flavoprotein, was strictly dependent on ferredoxin as reductant and was inactive with either NADPH or NADH. This early work has not been further pursued. We have recently reinvestigated the problem and confirmed that the enzyme, here designated ferredoxin-dependent flavin thioredoxin reductase (FFTR), is a flavoprotein. The enzyme differs from ferredoxin−thioredoxin reductase (FT

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MAYR, Peter, and Bernd NIDETZKY. "Catalytic reaction profile for NADH-dependent reduction of aromatic aldehydes by xylose reductase from Candida tenuis." Biochemical Journal 366, no. 3 (2002): 889–99. http://dx.doi.org/10.1042/bj20020080.

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Kinetic substituent effects have been used to examine the catalytic reaction profile of xylose reductase from the yeast Candida tenuis, a representative aldo/keto reductase of primary carbohydrate metabolism. Michaelis—Menten parameters (kcat and Km) for NADH-dependent enzymic aldehyde reductions have been determined using a homologous series of benzaldehyde derivatives in which substituents in meta and para positions were employed to systematically perturb the properties of the reactive carbonyl group. Kinetic isotope effects (KIEs) on kcat and kcat/Km for enzymic reactions with meta-substitu

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Kleczkowski, L. A., D. D. Randall, and G. E. Edwards. "Oxalate as a potent and selective inhibitor of spinach (Spinacia oleracea) leaf NADPH-dependent hydroxypyruvate reductase." Biochemical Journal 276, no. 1 (1991): 125–27. http://dx.doi.org/10.1042/bj2760125.

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Purified spinach (Spinacia oleracea) NADPH-preferring hydroxypyruvate reductase (HPR-2) was potently and selectively inhibited by oxalate, an end product of metabolism in plants. Both hydroxypyruvate- and glyoxylate-dependent rates of the HPR-2 enzyme were affected. Oxalate acted as an uncompetitive inhibitor of the enzyme, with Ki values of 7 and 36 microM for the NADPH/hydroxypyruvate and NADPH/glyoxylate pairs of reactants respectively. Oxalate, at millimolar levels, caused less than 10% inhibition of purified spinach NADH-preferring HPR (HPR-1) and had no effect on purified spinach NADPH-p

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Nguyen, Giang Thu, Shinae Kim, Hyeonseok Jin, et al. "Crystal Structure of NADPH-Dependent Methylglyoxal Reductase Gre2 from Candida Albicans." Crystals 9, no. 9 (2019): 471. http://dx.doi.org/10.3390/cryst9090471.

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Gre2 is a key enzyme in the methylglyoxal detoxification pathway; it uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde. This enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily whose members catalyze this type of reaction with a broad range of substrates. To elucidate the structural features, we determined the crystal structures of the NADPH-dependent methylglyoxal reductase Gre2 from Candida albicans (CaGre2) for both the apo-form and NADPH-complexed form at resolutions of 2.8 and 3.02 Å, respectively. The CaGre2 structur

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Blaise, Mickaël, Niël Van Wyk, Françoise Banères-Roquet, Yann Guérardel та Laurent Kremer. "Binding of NADP+ triggers an open-to-closed transition in a mycobacterial FabG β-ketoacyl-ACP reductase". Biochemical Journal 474, № 6 (2017): 907–21. http://dx.doi.org/10.1042/bcj20161052.

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The ketoacyl-acyl carrier protein (ACP) reductase FabG catalyzes the NADPH/NADH dependent reduction of β-ketoacyl-ACP substrates to β-hydroxyacyl-ACP products, the first reductive step in the fatty acid biosynthesis elongation cycle. FabG proteins are ubiquitous in bacteria and are part of the type II fatty acid synthase system. Mining the Mycobacterium smegmatis genome uncovered several putative FabG-like proteins. Among them, we identified M. smegmatis MSMEG_6753 whose gene was found adjacent to MSMEG_6754, encoding a recently characterized enoyl-CoA dehydratase, and to MSMEG_6755, encoding

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Katsyv, Alexander, Surbhi Jain, Mirko Basen, and Volker Müller. "Electron carriers involved in autotrophic and heterotrophic acetogenesis in the thermophilic bacterium Thermoanaerobacter kivui." Extremophiles 25, no. 5-6 (2021): 513–26. http://dx.doi.org/10.1007/s00792-021-01247-8.

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AbstractThermoanaerobacter kivui is an acetogenic model organism that reduces CO2 with electrons derived from H2 or CO, or from organic substrates in the Wood–Ljugdahl pathway (WLP). For the calculation of ATP yields, it is necessary to know the electron carriers involved in coupling of the oxidative and reductive parts of metabolism. Analyses of key catabolic oxidoreductases in cell-free extract (CFE) or with purified enzymes revealed the physiological electron carriers involved. The glyceraldehyde-3-phosphate dehydrogenase (GA3P-DH) assayed in CFE was NAD+-specific, NADP+ was used with less

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Wendroth, S., та H. U. Seitz. "Characterization and localization of progesterone 5α-reductase from cell cultures of foxglove (Digitalis lanata EHRH)". Biochemical Journal 266, № 1 (1990): 41–46. http://dx.doi.org/10.1042/bj2660041.

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Progesterone 5 alpha-reductase, which catalyses the reduction of progesterone to 5 alpha-pregnane-3,20-dione, was isolated and characterized from cell cultures of Digitalis lanata (foxglove). Optimum enzyme activity was observed at pH 7.0, and the enzyme had an apparent Km value of 30 microM for its substrate progesterone. The enzyme needs NADPH as reductant, which could not be replaced by NADH. For NADPH, the apparent Km value is 130 microM. The optimum temperature was 40 degrees C; at temperatures below 45 degrees C, the product 5 alpha-pregnane-3,20-dione was reduced by a second reaction to

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Bertsova, Y. V., M. V. Serebryakova, V. A. Anashkin, A. A. Baykov, and A. V. Bogachev. "A REDOX-REGULATED, HETERODIMERIC NADH:CINNAMATE REDUCTASE IN Vibrio ruber." Биохимия 89, no. 2 (2024): 261–78. http://dx.doi.org/10.31857/s0320972524020053ncwtx.

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Genes of putative reductases of α,β-unsaturated carboxylic acids are abundant among anaerobic and facultatively anaerobic microorganisms, yet substrate specificity has been experimentally verified for few encoded proteins. Here, we co-produced in Escherichia coli a heterodimeric protein of the facultatively anaerobic marine bacterium Vibrio ruber (GenBank SJN56019 and SJN56021; annotated as NADPH azoreductase and urocanate reductase, respectively) with Vibrio cholerae flavin transferase. The isolated protein (named Crd) consists of the sjn56021-encoded subunit CrdB (NADH:flavin, FAD binding 2,

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Kaufmann, Franz, and Derek R. Lovley. "Isolation and Characterization of a Soluble NADPH-Dependent Fe(III) Reductase from Geobacter sulfurreducens." Journal of Bacteriology 183, no. 15 (2001): 4468–76. http://dx.doi.org/10.1128/jb.183.15.4468-4476.2001.

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ABSTRACT NADPH is an intermediate in the oxidation of organic compounds coupled to Fe(III) reduction in Geobacter species, but Fe(III) reduction with NADPH as the electron donor has not been studied in these organisms. Crude extracts of Geobacter sulfurreducens catalyzed the NADPH-dependent reduction of Fe(III)-nitrilotriacetic acid (NTA). The responsible enzyme, which was recovered in the soluble protein fraction, was purified to apparent homogeneity in a four-step procedure. Its specific activity for Fe(III) reduction was 65 μmol · min−1 · mg−1. The soluble Fe(III) reductase was specific for

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Mohazzab, K. M., and M. S. Wolin. "Sites of superoxide anion production detected by lucigenin in calf pulmonary artery smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 267, no. 6 (1994): L815—L822. http://dx.doi.org/10.1152/ajplung.1994.267.6.l815.

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Sources of superoxide anion (O2-.) production in calf pulmonary artery smooth muscle homogenate and subcellular fractions were examined in this study by measurement of the chemiluminescence produced by the reaction of O2-. with 50 microM lucigenin, because recent evidence suggests that endogenously produced reactive O2 species appear to mediate certain vascular responses. In the homogenate fraction, an NADH (0.1 mM)-dependent oxidoreductase activity was the major detected source of chemiluminescence. NADPH (0.1 mM) produced only 3% of the O2-. observed with NADH. Quantitation of certain other

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de, las Heras Alejandro Muñoz, Diogo J. Portugal-Nunes, Nathasha Rizza, Anders G. Sandström, and Marie F. Gorwa-Grauslund. "Anaerobic poly-3-d-hydroxybutyrate production from xylose in recombinant Saccharomyces cerevisiae using a NADH-dependent acetoacetyl-CoA reductase." Microbial Cell Factories 15, no. 1 (2016): 197. https://doi.org/10.1186/s12934-016-0598-0.

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<strong>Background: </strong>Poly-3-d-hydroxybutyrate (PHB) that is a promising precursor for bioplastic with similar physical properties as polypropylene, is naturally produced by several bacterial species. The bacterial pathway is comprised of the three enzymes β-ketothiolase, acetoacetyl-CoA reductase (AAR) and PHB synthase, which all together convert acetyl-CoA into PHB. Heterologous expression of the pathway genes from <i>Cupriavidus necator</i> has enabled PHB production in the yeast <i>Saccharomyces cerevisiae</i> from glucose as well as from xylose, after introduction of the fungal xyl

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Smith, M. A., A. R. Cross, O. T. G. Jones, W. T. Griffiths, S. Stymne та K. Stobart. "Electron-transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine Δ12-desaturase (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons". Biochemical Journal 272, № 1 (1990): 23–29. http://dx.doi.org/10.1042/bj2720023.

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The major cytochrome in microsomal membrane preparations from developing seeds of safflower (Carthamus tinctorius, var High Linoleate), has a reduced-minus-oxidized difference spectrum characteristic of a b-type cytochrome, and was identified from its midpoint-potential (E'7.2) value as cytochrome b5. Cytochromes P-450 and P-420 were also present. The cytochrome b5 content of microsomal preparations from a number of oilseed species was found to be in the order of 200-300 pmol/mg of protein. The cytochrome b5 was reduced in the membrane preparations by NADH, demonstrating the presence of an NAD

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Chamizo-Ampudia, Alejandro, Aurora Galvan, Emilio Fernandez, and Angel Llamas. "The Chlamydomonas reinhardtii Molybdenum Cofactor Enzyme crARC Has a Zn-Dependent Activity and Protein Partners Similar to Those of Its Human Homologue." Eukaryotic Cell 10, no. 10 (2011): 1270–82. http://dx.doi.org/10.1128/ec.05096-11.

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ABSTRACT The ARC (amidoxime reducing component) proteins are molybdenum cofactor (Moco) enzymes named hmARC1 and hmARC2 (human ARCs [hmARCs]) in humans and YcbX in Escherichia coli. They catalyze the reduction of a broad range of N-hydroxylated compounds (NHC) using reducing power supplied by other proteins. Some NHC are prodrugs or toxic compounds. YcbX contains a ferredoxin (Fd) domain and requires the NADPH flavin reductase CysJ to reduce NHC. In contrast, hmARCs lack the Fd domain and require a human cytochrome b5 (hCyt b5 ) and a human NADH Cyt b5 reductase (hCyt b5- R) to reduce NHC. The

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Takahashi, T., T. Yamaguchi, M. Shitashige, T. Okamoto, and T. Kishi. "Reduction of ubiquinone in membrane lipids by rat liver cytosol and its involvement in the cellular defence system against lipid peroxidation." Biochemical Journal 309, no. 3 (1995): 883–90. http://dx.doi.org/10.1042/bj3090883.

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Rat liver homogenates reduced ubiquinone (UQ)-10 to ubiquinol (UQH2)-10 in the presence of NADPH rather than NADH. This NADPH-dependent UQ reductase (NADPH-UQ reductase) activity that was not inhibited by antimycin A and rotenone, was located mainly in the cytosol fraction and its activity accounted for 68% of that of the homogenates. Furthermore, the NADPH-UQ reductase from rat liver cytosol efficiently reduced both UQ-10 incorporated into egg yolk lecithin liposomes, and native UQ-9 residing in rat microsomes, to the respective UQH2 form in the presence of NADPH. The gross redox ratios of UQ

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Neeli, Rajasekhar, Muna Sabri, Kirsty J. McLean, et al. "Trp359 regulates flavin thermodynamics and coenzyme selectivity in Mycobacterium tuberculosis FprA." Biochemical Journal 411, no. 3 (2008): 563–70. http://dx.doi.org/10.1042/bj20071298.

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Mtb (Mycobacterium tuberculosis) FprA (flavoprotein reductase A) is an NAD(P)H-dependent FAD-binding reductase that is structurally related to mammalian adrenodoxin reductase, and which supports the catalytic function of Mtb cytochrome P450s. Trp359, proximal to the FAD, was investigated in light of its potential role in controlling coenzyme interactions, as observed for similarly located aromatic residues in diflavin reductases. Phylogenetic analysis indicated that a tryptophan residue corresponding to Trp359 is conserved across FprA-type enzymes and in adrenodoxin reductases. W359A/H mutants

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Mouro, Adriane, Angela A. dos Santos, Denis D. Agnolo, et al. "Combining Xylose Reductase from Spathaspora arborariae with Xylitol Dehydrogenase from Spathaspora passalidarum to Promote Xylose Consumption and Fermentation into Xylitol by Saccharomyces cerevisiae." Fermentation 6, no. 3 (2020): 72. http://dx.doi.org/10.3390/fermentation6030072.

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In recent years, many novel xylose-fermenting yeasts belonging to the new genus Spathaspora have been isolated from the gut of wood-feeding insects and/or wood-decaying substrates. We have cloned and expressed, in Saccharomyces cerevisiae, a Spathaspora arborariae xylose reductase gene (SaXYL1) that accepts both NADH and NADPH as co-substrates, as well as a Spathaspora passalidarum NADPH-dependent xylose reductase (SpXYL1.1 gene) and the SpXYL2.2 gene encoding for a NAD+-dependent xylitol dehydrogenase. These enzymes were co-expressed in a S. cerevisiae strain over-expressing the native XKS1 g

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Lee, Jung-Kul, Bong-Seong Koo, and Sang-Yong Kim. "Cloning and Characterization of the xyl1 Gene, Encoding an NADH-Preferring Xylose Reductase from Candida parapsilosis, and Its Functional Expression in Candida tropicalis." Applied and Environmental Microbiology 69, no. 10 (2003): 6179–88. http://dx.doi.org/10.1128/aem.69.10.6179-6188.2003.

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ABSTRACT Xylose reductase (XR) is a key enzyme in d-xylose metabolism, catalyzing the reduction of d-xylose to xylitol. An NADH-preferring XR was purified to homogeneity from Candida parapsilosis KFCC-10875, and the xyl1 gene encoding a 324-amino-acid polypeptide with a molecular mass of 36,629 Da was subsequently isolated using internal amino acid sequences and 5′ and 3′ rapid amplification of cDNA ends. The C. parapsilosis XR showed high catalytic efficiency (k cat/Km = 1.46 s−1 mM−1) for d-xylose and showed unusual coenzyme specificity, with greater catalytic efficiency with NADH (k cat/Km

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