Literature DB >> 16875

A new enzyme, NADPH-dihydropteridine reductase in bovine liver.

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.

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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


  1 in total

1.  Tetrahydrobiopterin, a cofactor for rat cerebellar nitric oxide synthase, does not function as a reactant in the oxygenation of arginine.

Authors:  J Giovanelli; K L Campos; S Kaufman
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-15       Impact factor: 11.205

  1 in total

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