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 Physioljournal_title
Plant physiologyauthors
Loewus MW,Bedgar DL,Saito K,Loewus FAdoi
10.1104/pp.94.3.1492subject
Has Abstractpub_date
1990-11-01 00:00:00pages
1492-5issue
3eissn
0032-0889issn
1532-2548journal_volume
94pub_type
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