Plant Physiology 52:111-118 (1973)
© 1973 American Society of Plant Biologists
Articles
Nonreversible D-Glyceraldehyde 3-Phosphate Dehydrogenase of Plant Tissues 1
G. J. Kelly2 and
Martin Gibbs
a Department of Biology, Brandeis University, Waltham, Massachusetts 02154
Preparations of TPN-linked nonreversible D-glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.9), free of TPN-linked reversible D-glyceraldehyde 3-phosphate dehydrogenase, have been obtained from green shoots, etiolated shoots, and cotyledons of pea (Pisum sativum), cotyledons of peanut (Arachis hypogea), and leaves of maize (Zea mays). The properties of the enzyme were similar from each of these sources: the Km values for D-glyceraldehyde 3-phosphate and TPN were about 20 µM and 3 µM, respectively. The enzyme activity was inhibited by L-glyceraldehyde 3-phosphate, D-erythrose 4-phosphate, and phosphohydroxypyruvate. Activity was found predominantly in photosynthetic and gluconeogenic tissues of higher plants. A light-induced, phytochrome-mediated increase of enzyme activity in a photosynthetic tissue (pea shoots) was demonstrated. Appearance of enzyme activity in a gluconeogenic tissue (endosperm of castor bean, Ricinus communis) coincided with the conversion of fat to carbohydrate during germination. In photosynthetic tissue, the enzyme is located outside the chloroplast, and at in vivo levels of triose-phosphates and pyridine nucleotides, the activity is probably greater than that of DPN-linked reversible D-glyceraldehyde 3-phosphate dehydrogenase. Several possible roles for the enzyme in plant carbohydrate metabolism are considered.
2 Present address: Department of Agricultural Chemistry, University of Sydney, N.S.W. 2006, Australia.
1 This research was supported generously by the United States Atomic Energy Commission Grant AT (30-1) 3447 and by the National Science Foundation Grant GB 29126 X.
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