| Literature DB >> 16875 |
N Nakanishi, H Hasegawa, S Watabe.
Abstract
An enzyme designated as NADPH-dihydropteridine reductase was found in the extract of bovine liver and partially purified. In contrast to NADH-dpendent dihydropteridine reductase [EC 1.6.99.7], the enzyme catalyzes the reduction of quinonid-dihydropterin to tetrahydropterin in 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 from ofpteridine cofactor may be regenerated in two different ways in vivo.Entities:
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Year: 1977 PMID: 16875 DOI: 10.1093/oxfordjournals.jbchem.a131504
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387