A reductase is basically an enzyme that brings about or catalyzes a reduction reaction, which is also known as a “redox” (reduction oxidation) reaction. A redox reaction involves all chemical reactions in which the atoms have their oxidation states changed. An example of a simple redox process is the oxidation of carbon to produce carbon dioxide. Oxidation is the loss of electrons or an increase in oxidation state (as in a molecule, atom, or ion), while reduction is the gain of electrons or a decrease in oxidation state.
There are many kinds of reductase, such as the dihydrofolate reductase (or DHFR), an enzyme that produces a reduction reaction in dihydrofolic acid (and thus converting it to tetrahydrofolic acid) by using the NADPH as an electron donor. In humans, the DHFR gene encodes this enzyme. Bacterial organisms also possess distinct DHFR enzymes, while mammalian species have highly similar DHFR enzymes.
Another kind of reductase is the HMG-CoA reductase (or the 3-hydroxy-3-methyl-glutaryl-CoA reductase, HMGCR for short), which is an enzyme that controls the rate of the mevalonate pathway. This pathway is known for producing cholesterol and other kinds of isoprenoids. On the other hand, the methemoglobin reductase is responsible for converting methemoglobin to haemoglobin.
Ribonucleotide reductase (also known as the ribonucleoside diphosphate reductase) is an enzyme that brings about the formation of deoxyribonucleotides from ribonucleotides. This product is essential in the synthesis of DNA in various organisms. The ribonucleotide reductase (RNR) is essential in the total rate of DNA synthesis in all living organisms. Thioredoxin reductase, on the other hand, are the only known enzymes to reduce the group of redox proteins called thioredoxin.
This category contains scientific information on reductase, an enzyme that is known for catalyzing reduction and reduction oxidation reactions in various kinds of proteins.
Junien, C.; Leroux, A.; Lostanlen, D.; Reghis, A.; Boue, J.; Nicolas, H.; Boue, A.; Kaplan, J. C., 1981: Pre natal diagnosis of congenital enzymopenic met hemo globinemia with mental retardation due to generalized cytochrome b 5 reductase ec 184.108.40.206 deficiency 1st report of 2 cases. Prenatal Diagnosis 1(1): 17-24 Prenatal diagnosis of congenital enzymopenic methemoglobinemia [...]
Pratt H.P.M., 1982: Pre implantation mouse embryos synthesize membrane sterols. Developmental Biology: 101-110 The total cholesterol content of preimplantation mouse embryos increases.apprx. 3-fold (to 1 pmol) during the development of a blastocyst from a fertilized egg. From the 2-cell stage onwards, embryos are capable of converting mevalonate into the membrane sterols lanosterol and cholesterol. Activity [...]
Schiller J.G., 1979: Potentiometric method for substrate analysis using immobilized nad dependent oxido reductase enzymes. Biotechnology & Bioengineering: -1916 Two coenzyme-dependent oxidoreductases, glucose dehydrogenase and alcohol dehydrogenase, were immobilized in polyacrylamide gel over a platinum grid matrix and used as enzyme electrodes to measure their substrate concentrations in buffered aqueous solutions. The immobilized enzymes were [...]
Hassan, S. S. M.; Rechnltz, G. A., 1982: Potentiometric determination of nadp and glutathione reductase ec 220.127.116.11. Analytical Chemistry 54(2): 303-307 A Co2 gas sensing membrane electrode is employed for the potentiometric determination of Nadp+ and glutathione reductase enzyme using a rate approach. The resulting methods combine convenience, sensitivity and high selectivity with good analytical [...]
Kuroiwa Y., 1986: Potentiation of aflatoxin b 1 induced hepatotoxicity in male wistar rats with ethanol pretreatment. Journal Of Toxicological Sciences: 41-52 The interaction of ethanol and aflatoxin B1 (Afb1)-induced hepatotoxicity was studied in male Wistar rats using the activity of plasma Got and Gpt, liver triglyceride and histopathologic changes of liver necrosis as indices. [...]
Yuthavong Y., 1986: Potentiating effect of pyrimethamine and sulfadoxine against dihydrofolate reductase from pyrimethamine sensitive and pyrimethamine resistant plasmodium chabaudi. Antimicrobial Agents & Chemotherapy: 899-905 Dihydrofolate reductase was partially purified from a pyrimethamine-sensitive Plasmodium chabaudi clone and a pyrimethamine-resistant clone derived from it and used in a study of the inhibitory effect of pyrimethamine and [...]
Zeikus J.G., 1981: Potential applications of an alcohol aldehyde ketone oxido reductase from thermophilic bacteria. Enzyme & Microbial Technology: 144-148 Practical uses of a novel alcohol dehydrogenase from Thermoanaerobium brockii were examined in crude and purified form. Stoichiometeic reduction of Nadp (50 mg) was demonstrated with agarose-immobilized enzyme and 0.3 (vol/vol) 2-propanol solution as reductant. [...]
Masur H., 1987: Potent in vitro and in vivo antitoxoplasma activity of the lipid soluble antifolate trimetrexate. Journal Of Clinical Investigation: 478-482 Trimetrexate, a highly lipid-soluble quinazoline antifolate now undergoing trials as an anticancer agent, was found to be a potent inhibitor of the dihydrofolate reductase (Dhfr) isolated from Toxoplasma gondii. The concentration required for [...]
Riklis E., 1979: Post transcriptional control of nitrate reductase of cultured tobacco cells by amino acids. Plant Physiology (rockville): 663-664 Using the inhibitor of Rna synthesis, 4,5′,8-trimethylpsoralen plus near Uv light, the half-life of the rate-limiting Rna species required for the induction of nitrate reductase in Xd cells of tobacco was estimated to be 4 [...]