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Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi

Biochemistry, 1977
The NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi have been purified to homogeneity as judged by single bands on sodium dodecyl sulfate gel electrophoresis. The overall purification for the NADH specific enzyme is 3000-fold and 4000-fold for the NADPH specific enzyme from a crude extract. The final step in the purification procedure
Marlene Deluca, M Deluca
exaly   +4 more sources

Regulation of the NADH and NADPH-ferredoxin oxidoreductases in Clostridia of the butyric group

Biochimica Et Biophysica Acta - General Subjects, 1976
NADH and NADPH-ferredoxin oxidoreductases have been studied in Clostridium acetobutylicum, Cl. tyrobutyricum and Cl. pasteurianum. The study of the distribution and regulation of these enzymatic activities in well-defined culture conditions, reveals that the essential function of NADPH-ferredoxin oxidoreductase is to produce NADPH, while NADH ...
H Petitdemange, R Gay
exaly   +4 more sources

Continuous monitoring of reactions that produce NADH and NADPH using immobilized luciferase and oxidoreductases from Beneckea harveyi

Analytical Biochemistry, 1978
Abstract Highly purified NADH and NADPH:FMN oxidoreductase and luciferase isolated from Beneckea harveyi have been immobilized to arylamine glass beads which were cemented to glass rods. The immobilized enzyme rods are stable, reuseable, and specific for either NADH or NADPH.
C, Haggerty   +3 more
openaire   +3 more sources

Studies on the NADH and NADPH: Riboflavin 5′-phosphate (FMN) oxidoreductases from Beneckea harveyi: Characterization of the FMN binding sites

Archives of Biochemistry and Biophysics, 1982
Abstract Various flavin analogs were used as alternate substrates or competitive inhibitors to characterize the FMN binding sites of the NADH- and NADPH-specific FMN oxidoreductases from Beneckea harveyi . Several polyhydroxyl compounds were found to be poor competitive inhibitors for the FMN sites of these enzymes.
B, Nefsky, M, DeLuca
openaire   +3 more sources

Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases

microPublication Biology, 2023
Irc24p is a benzil oxidoreductase encoded on chromosome IX of Saccharomyces cerevisiae . We identified a putative paralog, Nre1p, encoded 284 bp downstream. Both proteins are small, cytoplasmic, and are 52% identical (70% similar).
Brandon L. Garcia, K. Riley
semanticscholar   +1 more source

Sequence and structure-guided discovery of a novel NADH-dependent 7β-hydroxysteroid dehydrogenase for efficient biosynthesis of ursodeoxycholic acid.

Bioorganic chemistry (Print), 2022
7β-Hydroxysteroid dehydrogenases (7β-HSDHs) have attracted increasing attention due to their crucial roles in the biosynthesis of ursodeoxycholic acid (UDCA).
Bin Huang   +7 more
semanticscholar   +1 more source

NADH(NADPH):(Acceptor) oxidoreductase activities of the bovine adrenal chromaffin granules

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
Abstract 1. 1. An analysis of the NADH(NADPH):(acceptor) oxidoreductase activities of adrenal chromaffin granules depleted of low molecular weight substances (notably catecholamines and ATP), has been made in terms of the flavoprotein(s) and cytochrome b 561 previously reported (Flatmark, T., Terland, O. and Helle, K. B.
O, Terland, T, Flatmark
openaire   +2 more sources

Properties of the hypothalamic 5α-dihydroprogesterone NADH- and NADPH-linked 3α-hydroxysteroid oxidoreductase activities

Journal of Steroid Biochemistry, 1981
Abstract Rat hypothalamic 5α-dihydroprogesterone NADH-linked 3α-hydroxysteroid oxidoreductase, (3α-HSD) activity, which is associated with plasma membranes, has a relatively sharp pH optimum of 5.5 and a temperature optimum range of 45–52°C. This enzyme exhibited apparent K m 's for the reductive reaction of 0.40 ± 0.09 μm and 29 ± 12 μ M for ...
J E, Krause, H J, Karavolas
openaire   +2 more sources

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