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

Authors
  • Loewus, M W
  • Bedgar, D L
  • Saito, K
  • Loewus, F A
Type
Published Article
Journal
PLANT PHYSIOLOGY
Publisher
American Society of Plant Biologists
Publication Date
Nov 01, 1990
Volume
94
Issue
3
Pages
1492–1495
Identifiers
PMID: 16667860
Source
Medline
License
Unknown

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.

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