Fructose 2,6-Bisphosphate Hydrolyzing Enzymes in Higher Plants
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منابع مشابه
Fructose 2,6-bisphosphate hydrolyzing enzymes in higher plants.
The phosphatases that hydrolyze fructose 2,6-bisphosphate in a crude spinach (Spinacia oleracea L.) leaf extract were separated by chromatography on blue Sepharose, into three fractions, referred to as phosphatases I, II, and III, which were further purified by various means. Phosphatase I hydrolyzed fructose 2,6-bisphosphate, with a K(m) value of 30 micromolar, to a mixture of fructose 2-phosp...
متن کاملPhosphatidylinositol 4,5-bisphosphate phosphodiesterase in higher plants.
A phospholipase C which hydrolyses phosphatidylinositol 4,5-bisphosphate to release inositol trisphosphate was detected in a sedimentable fraction from celery and from some other higher plants. The particulate enzyme also hydrolyses phosphatidylinositol, whereas the soluble phosphatidylinositol phosphodiesterase described previously [Irvine, Letcher & Dawson (1980) Biochem. J. 192, 279-283] act...
متن کاملManipulation of fructose-2,6-bisphosphate levels in transgenic plants.
Introduction This report considers the contribution of recent studies on transgenic plants to our current understanding of the role of fructose-2,6-bisphosphate (Fru-2,6-P,) in the regulation of carbon metabolism. From data obtained using such plants we argue that this metabolite is quantitatively important in the control of carbohydrate metabolism in both photosynthetic and non-photosynthetic ...
متن کاملThe fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.
Two forms of the enzyme fructoseI ,6-bisphosphate aldolase (EC 4. I .2.13) are known, designated class I and class 11. The enzymes o f class I function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion (for review, see [ I , 21). The enzymes of class I1 utilize a divalent metal ion to act ...
متن کاملEffects of fructose 2,6-bisphosphate on phosphoglucomutase from plants.
Fructose 2,6-bisphosphate affects phosphoglucomutase from plant and animal sources in a similar way. As previously found with rabbit muscle phosphoglucomutase, fructose 2,6-bisphosphate cannot substitute for glucose 1,6-bisphosphate as a cofactor in the reaction catalyzed by phosphoglucomutase from potato tubers, pea seeds, and string-beans. In the presence of glucose 1,6-bisphosphate, fructose...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1989
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.90.3.827