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

Abstract:

: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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Loewus MW,Bedgar DL,Saito K,Loewus FA

doi

10.1104/pp.94.3.1492

subject

Has Abstract

pub_date

1990-11-01 00:00:00

pages

1492-5

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

94

pub_type

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