Conversion of l-Sorbosone to l-Ascorbic Acid by a NADP-Dependent Dehydrogenase in Bean and Spinach Leaf | Zendy

Mary W. Loewus | Zendy; Diana L. Bedgar | Zendy; Kazumi Saito | Zendy; Frank A. Loewus | Zendy

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Conversion of l-Sorbosone to l-Ascorbic Acid by a NADP-Dependent Dehydrogenase in Bean and Spinach Leaf

Author(s) -

Mary W. Loewus,

Diana L. Bedgar,

Kazumi Saito,

Frank A. Loewus

Publication year - 1990

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.94.3.1492

Subject(s) - spinacia , spinach , phaseolus , ascorbic acid , dehydrogenase , enzyme , biochemistry , lycorine , nad+ kinase , biology , chemistry , botany , food science , chloroplast , gene , alkaloid

An NADP-dependent dehydrogenase catalyzing the conversion of l-sorbosone to l-ascorbic acid has been isolated from Phaseolus vulgaris L. and Spinacia oleracea L. and partially purified. It is stable at -20 degrees C for up to 8 months. Molecular masses, as determined by gel filtration, were 21 and 29 kilodaltons for bean and spinach enzymes, respectively. K(m) for sorbosone were 12 +/- 2 and 18 +/- 2 millimolar and for NADP(+), 0.14 +/- 0.05 and 1.2 +/- 0.5 millimolar, for bean and spinach, respectively. Lycorine, a purported inhibitor of l-ascorbic acid biosynthesis, had no effect on the reaction.

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