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.
Ikenaka, K.; Fukushima, M.; Shirasaka, T.; Fujii, S., 1981: Possible regulation of ribo nucleoside di phosphate reductase ec 126.96.36.199. Gann 72(1): 8-18 Two inhibitors of ribonucleoside diphosphate reductase (Rr) (Ec 188.8.131.52) in vitro were isolated from normal rat liver: they were a nondialyzable, heat-labile, high-Mw ribonucleoside diphosphate reductase inhibitor (Hrri) and a dialyzable, heat-stable, low-Mw [...]
Kodama, T.; Hori, S. H., 1982: Possible functional coupling of hexose 6 phosphate dehydrogenase ec 184.108.40.206 to microsomal electron transport system in rat kidney and liver. Biochimica et Biophysica Acta 715(2): 151-161 Intrarenal distributions of cytosolic glucose-6-phosphate dehydrogenase, microsomal hexose-6-phosphate dehydrogenase, Nadph-cytochrome c reductase, mixed-function oxidases and cytochrome P-450, and effects of phenobarbital, methylcholanthrene, fasting, [...]
Schmidt C.G., 1987: Positive correlation between decreased cellular uptake nadph glutathione reductase activity and adriamycin resistance in ehrlich ascites tumor lines. Archives Of Toxicology3: 154-157 From a wild type strain of Ehrlich ascites tumor (Eatwt) sublines resistant to daunorubicin (Eatdnm), etoposide (Eateto), and cisplatinum (Eatcis) have been developed in vivo. Increase in survival and cure [...]
Zaluzny L., 1983: Portal vein ligation selectively lowers hepatic cytochrome p 450 levels in rats. Gastroenterology: 275-282 In rats, surgical creation of a portacaval shunt leads to hepatic atrophy and lowered levels of cytochrome P450, the key component of liver enzymes involved with drug metabolism. These effects are largely attributable to diversion of portal blood [...]
Smith, S. L.; Patrick, P.; Stone, D.; Phillips, A. W.; Burchall, J. J., 1979: Porcine liver di hydro folate reductase ec 220.127.116.11 purification properties and amino acid sequence. Journal of Biological Chemistry 254(22): 11475-11484 Porcine liver dihydrofolate reductase was purified 18,000-fold to homogeneity. The properties of the purified enzyme were compared to those of dihydrofolate [...]
O’brien, M. M.; Schofield, P. J., 1980: Polyol pathway enzymes of human brain partial purification and properties of aldose reductase ec 18.104.22.168 and hexonate dehydrogenase. Biochemical Journal 187(1): 21-30 Aldose reductase and hexonate dehydrogenase were isolated from human brain and partially purified. The 2 enzymes exhibited distinctive substrate-specificity profiles with a variety of aldoses, and [...]
Aleksandrovskii-Ya, A.; Sukhno, A. A.; Rodionov-Yu, V., 1979: Polymeric substrates of oxido reductases on the basis of 4 4 bi pyridyl. Biokhimiya 44(12): 2130-2133 The synthesis and some properties of the soluble polymers on the basis of 4,4′-bipyridyl (polyviologens) are described. The polyviologens can be used as electron acceptors in the reactions catalyzed by glucose [...]
“Hynninen P.H., 1986: Polymer phase partition in the purification of cytochrome p 450 and cytochrome b 5 from the yeast brettanomyces anomalus. Biotechnology & Applied Biochemistry: 60-68 About 0.5% of the total cellular protein in the yeast Brettanomyces anomalus is membrane-bound cytochrome P-450, when this yeast is grown in the presence of 5% glucose as [...]
Robertson L.W., 1986: Polychlorinated biphenyls classified as either phenobarbital or 3 methylcholanthrene type inducers of cytochrome p 450 are both hepatic tumor promoters in diethylnitrosamine initiated rats. Cancer Letters: 243-254 The cytochrome P-450 isozymes, cytochrome P-450 Mc1 and Mc2, purified from rats treated with 3-methylcholanthrene (Mc), were found by immunohistochemical staining to be strongly induced [...]
Verity M.A., 1980: Poly myositis dermato myositis diagnostic and prognostic significance of muscle alkaline phosphatase. American Journal Of Pathology: 159-176 The distribution and intensity of alkaline phosphatase deposition in 54 patients with dermatomyositis-polymyositis (Pm-Dm) was analyzed by the enzyme histochemical method. Increased enzyme reactivity of endomysial capillaries was found in 28% of patients, equally distributed [...]