Results 211 to 220 of about 330,401 (264)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +3 more sources
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
openaire +2 more sources
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 ...
P L, Hoffman +2 more
openaire +2 more sources
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 ...
P L, Hoffman +2 more
openaire +2 more sources
Current Drug Metabolism, 2010
Enzymatic carbonyl reduction means the formation of a hydroxy function out of a ketone or aldehyde moiety and applies for the metabolism of physiological (endogenous) or xenobiotic (exogenous) molecules. As for endogenous substrates, carbonyl reduction is often part of a reversible oxidoreductase process and involves the activation or inactivation of ...
Petra, Malátková +2 more
openaire +2 more sources
Enzymatic carbonyl reduction means the formation of a hydroxy function out of a ketone or aldehyde moiety and applies for the metabolism of physiological (endogenous) or xenobiotic (exogenous) molecules. As for endogenous substrates, carbonyl reduction is often part of a reversible oxidoreductase process and involves the activation or inactivation of ...
Petra, Malátková +2 more
openaire +2 more sources
Pharmacotherapy: The Journal of Human Pharmacology and Drug Therapy, 1990
The present management of diabetes consists of attempting to control blood sugar tightly in the normal range and to treat individual complications such as neuropathy and retinopathy as they appear. Whereas these measures are perhaps effective in slowing the progress of diabetic complications, they do not cure the underlying process.
W R, Kirchain, M S, Rendell
openaire +2 more sources
The present management of diabetes consists of attempting to control blood sugar tightly in the normal range and to treat individual complications such as neuropathy and retinopathy as they appear. Whereas these measures are perhaps effective in slowing the progress of diabetic complications, they do not cure the underlying process.
W R, Kirchain, M S, Rendell
openaire +2 more sources
Nature, 1958
THE enzymatic reduction of dihydrofolic acid (FH2) to tetrahydrofolic acid (FH4) has been reported by several investigators1–3. Futterman1 noted that dihydrofolic acid was reduced by chicken liver extracts when either reduced di- or tri-phospho-pyridine nucleotide served as the co-factor. We have found that the rate of reduction of dihydrofolic acid by
J M, PETERS, D M, GREENBERG
openaire +2 more sources
THE enzymatic reduction of dihydrofolic acid (FH2) to tetrahydrofolic acid (FH4) has been reported by several investigators1–3. Futterman1 noted that dihydrofolic acid was reduced by chicken liver extracts when either reduced di- or tri-phospho-pyridine nucleotide served as the co-factor. We have found that the rate of reduction of dihydrofolic acid by
J M, PETERS, D M, GREENBERG
openaire +2 more sources
Dihydromorphinone ketone reductases
Life Sciences, 1975Abstract Dihydromorphinone ketone reductases are new NADPH dependent drug metabolizing enzymes which occur predominantly in cytosol of liver and to a lesser extent in kidney and lung. The hepatic enzyme of the chicken has been found to differ from that of rabbit with respect to relative effectiveness of inhibitors and according to certain other ...
openaire +2 more sources
Current Opinion in Chemical Biology, 2004
The ability of some anaerobic bacteria to conserve energy via a soluble substrate level phosphorylation system by reducing glycine to acetyl-phosphate has been an intriguing mechanism for about half a century. The genes implicated in this system have been sequenced and form an operon structure with those of the thioredoxin system.
openaire +2 more sources
The ability of some anaerobic bacteria to conserve energy via a soluble substrate level phosphorylation system by reducing glycine to acetyl-phosphate has been an intriguing mechanism for about half a century. The genes implicated in this system have been sequenced and form an operon structure with those of the thioredoxin system.
openaire +2 more sources