Catalytic properties of NADPH-specific dihydropteridine reductase from bovine liver.

Abstract:

:The catalytic properties of a new type of dihydropteridine reductase, NADPH-specific dihydropteridine reductase [EC 1.6.99.10], from bovine liver, were studied and compared with those of the previously characterized enzyme, NADH-specific dihydropteridine reductase [EC 1.6.99.7]. With quinonoid-dihydro-6-methylpterin, approximate Km values of NADPH-specific dihydropteridine reductase for NADPH and NADH were estimated to be 1.4 micron and 2,900 microns, respectively. The Vmax values were 1.34 mumol/min/mg with NADPH and 1.02 mumol/min/mg with NADPH. With NADPH, the Km values of the enzyme for the quinonoid-dihydro forms of 6-methylpterin and biopterin were 1.4 micron and 6.8 microns, respectively. The enzyme was inhibited by its reaction product, NADP+, in a competitive manner, and the inhibition constant was determined to be 3.2 microns. The enzyme was severely inhibited by L-thyroxine and by 2,6-dichlorophenolindophenol.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Nakanishi N,Hasegawa H,Akino M,Yamada S

doi

10.1093/oxfordjournals.jbchem.a135523

subject

Has Abstract

pub_date

1986-03-01 00:00:00

pages

645-52

issue

3

eissn

0021-924X

issn

1756-2651

journal_volume

99

pub_type

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