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.
Ahmed, F.; Dunlap, R. B., 1984: Preparation of levo 5 6 7 8 tetrahydrofolate using immobilized dihydrofolate reductase ec 184.108.40.206. Analytical Biochemistry 141(1): 149-154 Dihydrofolate reductase from methotrexate-resistant Lactobacillus casei was immobilized on carbodiimide-activated Ch-Sepharose. The immobilized enzyme was utilized in the synthesis of (-)-5,6,7,8-tetrahydrofolate from dihydrofolate and Nadph in a batchwise reaction system. The [...]
Gil, G.; Sitges, M.; Hegardt, F. G., 1981: Preparation of highly radioactive homogeneous phosphorus 32 labeled hydroxymethyl glutaryl coenzyme a reductase ec 220.127.116.11 from rat liver. Archives of Biochemistry and Biophysics 210(1): 224-229 A procedure for the preparation of highly radioactive homogeneous 32p-labeled 3-hydroxy-3-methylglutaryl CoA reductase from rat liver microsomes was developed. The enzymatic preparation [...]
Bacon P.E., 1984: Preparation of carbon 14 labeled udp and carbon 14 labeled gdp. Preparative Biochemistry: 231-238 Procedures were developed for the routine enzymatic synthesis of Udp and Gdp from commercially available enzymes and Ump and Gmp. Using high pressure liquid chromatography, the products are recovered in high yield (60-80%) and with high purity. The [...]
Zanetti, G.; Cidaria, D.; Curti, B., 1982: Preparation of apo protein from spinach ferredoxin nadp reductase ec 18.104.22.168 the resolution process and characterization of the fad reconstituted holo enzyme. European Journal of Biochemistry 126(3): 453-458 Ferredoxin-Nadp reductase resolved into apoprotein and flavin by incubation with 2.5 M CaCl2 at pH 7.5 and 2.degree. C. Essential [...]
Sebek O.K., 1980: Preparation of 2 di norprostaglandin i 2 metabolites from 6 keto prostaglandin f 1 alpha by mycobacterium rhodochrous. Prostaglandins: 729-734 The transformation of 6-keto-Pgf1.alpha. to 2 prostacyclin metabolites, 2,3-dinor-6-keto-Pgf1.alpha. and 2,3-dinor-6,15-diketo-13,14-dihydro-Pgf1.alpha. by M. rhodochrous Uc-6176 is described. The finding that the bacterium oxidized 6-keto-Pgf1.alpha. to the 6,15-diketo metabolite Ii shows that it [...]
Depierre J.W., 1984: Preparation and characterization of subcellular fractions suitable for studies of drug metabolism from the trunk kidney of the northern pike esox lucius and assay of certain enzymes of xenobiotic metabolism in these subfractions. Biochemical Pharmacology: 2447-2460 The present study was designed to prepare and characterize subcellular fractions from the trunk kidney of [...]
Depierre J.W., 1985: Preparation and characterization of subcellular fractions from the head kidney of the northern pike esox lucius with particular emphasis on xenobiotic metabolizing enzymes. Biochemical Pharmacology: 789-802 Subcellular fractions from the head kidney of the northern pike (E. lucius) were prepared and characterized, with special emphasis on the preparation of a microsomal fraction [...]
Strobel H.W., 1986: Preparation and characterization of fad dependent nadph cytochrome p 450 reductase. Journal Of Biological Chemistry7: 7824-7830 Nadph-cytochrome P-450 reductase releases Fad upon dilution into slightly acidic potassium bromide. Chromatography on high performance hydroxylapatite resolved the Fad-dependent reductase from holoreductase. The Fad dependence was matched by a low Fad content, with the ratio [...]
Rilling H.C., 1986: Prenyltransferase and squalene synthetase in livers of neonate rats. Biochimica Et Biophysica Acta: 500-506 The liver of the newly born rat has approximately the same capacity for cholesterol biosynthesis as that of the adult animal. However, during nursing, the ability to synthesize cholesterol diminishes markedly during the early neonate period and by [...]
“Schmidt H., 1986: Prenatal diagnosis of dihydrobiopterin synthetase deficiency a variant form of phenylketonuria. European Journal Of Pediatrics: 176-178 Amniocentesis was performed at 19 weeks gestation in a mother who had previously delivered a boy with “”dihydrobiopterin synthetase”” (Dhbs) deficiency. The amniotic fluid contained neopterin in high (1365 nmol/l) and biopterin in very low concentrations [...]