Results 31 to 40 of about 142,240 (109)

Purification and characterization of nadph-linked aldehyde reductase from pig brain

, 1973
NADPH-linked aldehyde reductase was purified 750- fold with an 18% yield from pig brain. The enzyme was shown to catalyze both the reduction of aromatic and aliphatic aldehydes and the oxidation of aromatic and aliphatic alcohols.
Susa, John Baptist
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The binding mode of NADPH, NADPH-analogues, and NADPH fragments of the flavoenzyme glutathione reductase

, 1988
The binding of the substrate NADPH as well as a number of fragments and derivatives of NADPH to glutathione reductase from human erythrocytes has been investigated by using X-ray crystallography.
Pai, E., Schulz, G., Karplus, P.
core   +1 more source

Hydroxymethylglutaryl coA reductase (NADPH) in the latex of Hevea brasiliensis

, 1982
The activity of hydroxymethylglutaryl CoA reductase (NADPH) (EC 1.1.1.34) was studied in the latex of regularly tapped mature trees of Hevea brasiliensis.
Abdullah B. Sipat, Sipat, Abdullah B.
core   +1 more source

Inhibition of Leishmania infantum trypanothione reductase by NADPH, its natural substrate

, 2012
Trypanothione reductase is a flavoprotein that catalyzes the β-NADPH-linked reduction of trypanothione (N1,N8-bis (glutathionyl)spermidine), a glutathione analog unique to trypanosomatid parasites [1].
GIORGI, ALESSANDRA, G. Colotti, ILARI, ANDREA, SCHININA', Maria Eugenia, BAIOCCO, PAOLA, FIORILLO, ANNARITA, MALATESTA, FRANCESCO, LANTELLA, ANTONELLA   +7 more
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NADPH-Driven Organohalide Reduction by a Nonrespiratory Reductive Dehalogenase

, 2018
Reductive dehalogenases are corrinoid and iron–sulfur cluster-dependent enzymes that mostly act as the terminal oxidoreductases in the bacterial organohalide respiration process.
Fraser A. Collins (5388674), David Leys (1328622), Karl Fisher (1740823), Samantha Gaytan Mondragon (5388671), Stephen E. J. Rigby (110349), Karl A. P. Payne (4796952)   +5 more
core   +1 more source

Disruption of the Saccharomyces Cerevlsiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole

, 1989
Strains of Saccharomyces cerevisiae deleted in the NADPH-cytochrome P450 reductase gene by transplacement are 200-fold more sensitive to ketoconazole, an inhibitor of the cytochrome P450 lanosterol 14α-demethylase.
Sutter, Thomas R., Loper, John C.
core   +1 more source

Electron Leakage from the Mitochondrial NADPH-Adrenodoxin Reductase-Adrenodoxin-P450scc (Cholesterol Side Chain Cleavage) System

, 1993
In electron (e-) transfer systems some e- may "leak" reducing O2 to superoxide radical. This study examined the sites and kinetics of e- leakage from the mitochondrial P450scc system.
Weiner, L., Sklan, D., Hanukoglu, I., Rapoport, R.   +3 more
core   +1 more source

Roles of NADPH-P450 reductase in the O-Deethylation of 7-Ethoxycoumarin by recombinant human cytochrome P450 1B1 variants in Escherichia coli

, 2000
Four human cytochrome P450 1B1 (CYP1B1) allelic variants were purified from membranes of Escherichia coli in which respective CYP1B1 cDNAs and human NADPH-P450 reductase cDNA have been introduced.
Gillam, Elizabeth M. J., Shimada, Tsutomu, Guengerich, F. Peter, Inoue, Kiyoshi, Tsumura, Fujiko   +4 more
core   +1 more source

Hepatocyte Hyperproliferation upon Liver-Specific Co-disruption of Thioredoxin-1, Thioredoxin Reductase-1, and Glutathione Reductase

, 2017
Energetic nutrients are oxidized to sustain high intracellular NADPH/NADP(+) ratios. NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively ...
Jean A. Kundert, Colin G. Miller, Prigge, Justin R., Schmidt, Edward E., Arne Holmgren, Miller, Colin G., Elias S.J. Arnér, Ogata, Fernando, Orlicky, David J., Sebastin S. Martin, Gustafsson, Tomas N., Alix E. Herr, Edward E. Schmidt, Martin, Sebastin S., Colin T. Shearn, Coppo, Lucia, Justin R. Prigge, Matthew P. Taylor, David J. Orlicky, Mattsson, Åse, Herr, Alix E., Arnér, Elias S. J., Åse Mattsson, Tomas N. Gustafsson, Kundert, Jean A., Fernando Ogata, Bruschwein, Michael D., Michael D. Bruschwein, Taylor, Matthew P., Julia Lytchier, Lytchier, Julia, Lucia Coppo, Gustafsson, Tomas N.,, Holmgren, Arne, Shearn, Colin T., Martin, SS, Ogata, F, Bruschwein, MD, Prigge, JR, Kundert, JA, Orlicky, DJ, Coppo, L,, Lytchier, J, Shearn, CT, Miller, CG   +44 more
core   +1 more source

On the geometry of leukocyte NADPH‐oxidase, a membrane flavoenzyme Inferences from the structure of glutathione reductase

, 1983
Using the structure of glutathione reductase as a model, we suggest the following topography for leukocyte NADPH-oxidase: The binding sites of NADPH and O2 are separated from each other by the flavin ring and are thus exposed to opposite sides of the ...
Untucht-Grau, R., Georg E. Schulz, Schulz, G., R.Heiner Schirmer, Renate Untucht-Grau, Schirmer, R.   +5 more
core   +1 more source