A New Enzyme, NADPH-Dihydropteridine Reductase in Bovine Liver
- 1 March 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 81 (3), 681-685
- https://doi.org/10.1093/oxfordjournals.jbchem.a131504
Abstract
An enzyme designated as NADPH-dihydropteridine reductase was found in the extract of bovine liver and partially purified. In contrast to NADH-dependent dihydropteridine reductase [EC 1.6.99.7], the enzyme catalyzes the reduction of quinonoid-dihydropterin to tetrahydropterin the presence of NADPH. The two enzymes were separated by column chromatography on DEAE-Sephadex. Tyrosine formation in the phenylalanine hydroxylation system was also stimulated by NADPH-dihydropteridine reductase. The existence of these two dihydropteridine reductases suggests that the tetrahydro form of pteridine cofactor may be regenerated in two different ways in vivo.This publication has 2 references indexed in Scilit:
- Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresisArchives of Biochemistry and Biophysics, 1968
- Studies on the Mechanism of the Enzymatic Conversion of Phenylalanine to TyrosineJournal of Biological Chemistry, 1959