Results 281 to 290 of about 502,571 (335)
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Inhibition of aldehyde reductase by aldose reductase inhibitors
Biochemical Pharmacology, 1990A broad group of structurally diverse aldose reductase inhibitors including flavonoids, carboxylic acids and hydantoins, have been examined for their ability to inhibit rat kidney aldehyde reductase (EC 1.1.1.19, EC 1.1.1.20) versus rat lens aldose reductase (EC 1.1.1.21).
Sanai Sato, Peter F. Kador
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Sulfite Reductase of Escherichia coli Is a Ferrisiderophore Reductase
Biochemical and Biophysical Research Communications, 1993A soluble ferrisiderophore reductase activity of Escherichia coli was purified to homogeneity and identified as the sulfite reductase. The pure enzyme catalyzes the reduction of ferric citrate, ferriaerobactin, ferrioxamin, ferricrocin, ferrichrome and ferrifusarinin by NADPH. Free flavins, riboflavin, FMN, FAD were absolutely required, suggesting that
Marc Fontecave +2 more
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Glutathione reductase functions as vanadate(V) reductase
Archives of Biochemistry and Biophysics, 1990The oxidation of NADPH by vanadate(V) in the presence of glutathione reductase showed typical enzymatic kinetics. The oxidation was inhibited by N-ethylmaleimide, a glutathione reductase inhibitor. Superoxide dismutase had no significant effect on the oxidation, indicating noninvolvement of the superoxide radical. The vanadate(V) reduction was found to
Naresh S. Dalal, Xianglin Shi
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Archives of Neurology, 2000
CONTEXT Increasing evidence suggests that cholesterol plays a role in the pathophysiology of Alzheimer disease (AD). For instance, an elevated serum cholesterol level has been shown to be a risk factor for AD.
B. Wolozin +4 more
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CONTEXT Increasing evidence suggests that cholesterol plays a role in the pathophysiology of Alzheimer disease (AD). For instance, an elevated serum cholesterol level has been shown to be a risk factor for AD.
B. Wolozin +4 more
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Annual Review of Biochemistry, 2006
Ribonucleotide reductases (RNRs) transform RNA building blocks to DNA building blocks by catalyzing the substitution of the 2′OH-group of a ribonucleotide with a hydrogen by a mechanism involving protein radicals. Three classes of RNRs employ different mechanisms for the generation of the protein radical. Recent structural studies of members from each
Pär, Nordlund, Peter, Reichard
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Ribonucleotide reductases (RNRs) transform RNA building blocks to DNA building blocks by catalyzing the substitution of the 2′OH-group of a ribonucleotide with a hydrogen by a mechanism involving protein radicals. Three classes of RNRs employ different mechanisms for the generation of the protein radical. Recent structural studies of members from each
Pär, Nordlund, Peter, Reichard
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Chemico-Biological Interactions, 2000
Carbonyl reductase (secondary-alcohol:NADP(+) oxidoreductase, EC 1.1. 1.184) belongs to the family of short chain dehydrogenases/reductases (SDR). Carbonyl reductases (CBRs) are NADPH-dependent, mostly monomeric, cytosolic enzymes with broad substrate specificity for many endogenous and xenobiotic carbonyl compounds.
G L, Forrest, B, Gonzalez
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Carbonyl reductase (secondary-alcohol:NADP(+) oxidoreductase, EC 1.1. 1.184) belongs to the family of short chain dehydrogenases/reductases (SDR). Carbonyl reductases (CBRs) are NADPH-dependent, mostly monomeric, cytosolic enzymes with broad substrate specificity for many endogenous and xenobiotic carbonyl compounds.
G L, Forrest, B, Gonzalez
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Proteins: Structure, Function, and Bioinformatics, 2008
AbstractThioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 Å resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues.
ANGELUCCI, Francesco +5 more
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AbstractThioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 Å resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues.
ANGELUCCI, Francesco +5 more
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Journal of Neurochemistry, 1980
AbstractHuman brain contains multiple forms of aldehyde‐reducing enzymes. One major form (AR3), as previously shown, has properties that indicate its identity with NADPH‐dependent aldehyde reductase isolated from brain and other organs of various species; i.e., low molecular weight, use of NADPH as the preferred cofactor, and sensitivity to inhibition ...
Bendicht Wermuth +2 more
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AbstractHuman brain contains multiple forms of aldehyde‐reducing enzymes. One major form (AR3), as previously shown, has properties that indicate its identity with NADPH‐dependent aldehyde reductase isolated from brain and other organs of various species; i.e., low molecular weight, use of NADPH as the preferred cofactor, and sensitivity to inhibition ...
Bendicht Wermuth +2 more
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Molecular Genetics and Metabolism, 1998
A common mutation in methylenetetrahydrofolate reductase (MTHFR), C677T, results in a thermolabile variant with reduced activity. Homozygous mutant individuals (approximately 10% of North Americans) are predisposed to mild hyperhomocysteinemia, when ...
Ilan S. Weisberg +4 more
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A common mutation in methylenetetrahydrofolate reductase (MTHFR), C677T, results in a thermolabile variant with reduced activity. Homozygous mutant individuals (approximately 10% of North Americans) are predisposed to mild hyperhomocysteinemia, when ...
Ilan S. Weisberg +4 more
semanticscholar +1 more source
Journal of Medicinal Chemistry, 2015
Aldose reductase (AR) is an aldo-keto reductase that has been widely investigated as an enzyme crucially involved in the pathogenesis of chronic complications associated with diabetes mellitus.
R. Maccari, R. Ottanà
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Aldose reductase (AR) is an aldo-keto reductase that has been widely investigated as an enzyme crucially involved in the pathogenesis of chronic complications associated with diabetes mellitus.
R. Maccari, R. Ottanà
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