Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP

Journal of Biochemistry
Osao AdachiM Ameyama

Abstract

Old yellow enzyme system has been found in the cytosol fraction of Gluconobacter suboxydans. This is the first time that the enzyme has been found in organisms other than yeast cells. Old yellow enzyme [EC 1.6.99.1], D-glucose-6-phosphate dehydrogenase [EC 1.1.1.49], and catalase were isolated and crystallized separately from the organism. The old yellow enzyme from G. suboxydans showed catalytic and physicochemical properties almost identical with those of the enzyme from yeast cells. NADPH was specifically oxidized by the old yellow enzyme and the reduced enzyme was spontaneously reoxidized by atmospheric oxygen. The old yellow enzyme from G. suboxydans also contained FMN as a prosthetic group, and two mol of FMN were found per mol of enzyme (molecular weight, 88,000 as determined by gel filtration). In the oxidation of D-glucose-6-phosphate to 6-phospho-D-gluconate, cyclic regeneration of NADP occurred smoothly in the presence of D-glucose-6-phosphate dehydrogenase and catalase, even when a limited amount of NADP or NADPH was present in the reaction mixture.

Citations

Jan 20, 2004·Bioscience, Biotechnology, and Biochemistry·Naoto TonouchiKenzo Yokozeki
Mar 1, 1987·Applied Biochemistry and Biotechnology·H K Chenault, G M Whitesides

Related Concepts

Catalase T
Molecular Sieve Chromatography
Polymorphism, Crystallization
SDS-PAGE
Flavin Mononucleotide Disodium Salt
Glucosephosphate Dehydrogenase
NADH, NADPH Oxidoreductases
NADP
NADPH Dehydrogenase
Dioxygen

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