Results 301 to 310 of about 679,415 (356)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
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
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
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
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).
S, Sato, P F, Kador
openaire +2 more sources
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
J, Coves, M, Eschenbrenner, M, Fontecave
openaire +2 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
Journal of Neurochemistry, 1985
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
openaire +2 more sources
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A, Cromlish, T G, Flynn
openaire +2 more sources
Molecular and General Genetics MGG, 1981
The existence of a nitrate-reductase operon in the tryptophane region was deduced from the effects of prophage insertion in each of chlI and chlC genes and from transposition of the Mu-mediated host DNA fragments of F-prime. This operon appears to be polarized from chlC to chlI and the gene order in the region is trp -- chlI -- chlC -- purB.
V, Bonnefoy-Orth +3 more
openaire +2 more sources
The existence of a nitrate-reductase operon in the tryptophane region was deduced from the effects of prophage insertion in each of chlI and chlC genes and from transposition of the Mu-mediated host DNA fragments of F-prime. This operon appears to be polarized from chlC to chlI and the gene order in the region is trp -- chlI -- chlC -- purB.
V, Bonnefoy-Orth +3 more
openaire +2 more sources
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
openaire +6 more sources
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
openaire +6 more sources