Results 331 to 340 of about 854,050 (403)
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Chiral synthesis of LSD1 inhibitor GSK2879552 enabled by directed evolution of an imine reductase
Nature Catalysis, 2019Chris Macdermaid +2 more
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Structural Mechanism for Statin Inhibition of HMG-CoA Reductase
Science, 2001Johann Deisenhofer
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Lovastatin and beyond: the history of the HMG-CoA reductase inhibitors
Nature Reviews Drug Discovery, 2003J. Tobert
exaly +2 more sources
Identification of the gene for vitamin K epoxide reductase
Nature, 2004Tao Li +5 more
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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
openaire +2 more sources
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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Ferric reductases or flavin reductases?
Biometals, 1994Assimilation of iron by microorganisms requires the presence of ferric reductases which participate in the mobilization of iron from ferrisiderophores. The common structural and catalytic properties of these enzymes are described and shown to be identical to those of flavin reductases.
M, Fontecave, J, Covès, J L, Pierre
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Bacterial dimethyl sulphoxide reductases and nitrate reductases
Biochemical Society Transactions, 1991interactions which can be done when more structural information is available, but they do provide order of magnitude estimates of interaction strengths. Evidently, considerable rearrangement of charge driven by reduction significantly raises the effective dielectric. It seems likely that centres S-2 and FR-2 are apparently low-potential clusters merely
McEwan, Alastair G. +6 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
X L, Shi, N S, Dalal
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