Metabolic function of glycogen phosphorylase and trehalose phosphorylase in fruit-body formation ofFlammulina velutipes |
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Authors: | Yukata Kitamoto Atsushi Kobayashi Nobuhiro Mori Shoji Ohga |
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Institution: | (1) Department of Biochemistry and Biotechnology, Faculty of Agriculture, Tottori University, 4-101, 680-0945 Tottori, Minami, Koyamacho, Japan;(2) Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 394, Sasaguri-cho, 811-2415 Fukuoka, Japan |
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Abstract: | Glycogen phosphorylase in the vegetative mycelium ofFlammulina velutipes converts glycogen to α-glucose 1-phosphate (G1P) in the colony during fruit-body development. Glycogen may contribute to
the synthesis of trehalose as the starting material in the vegetative mycelium during the fruiting process of the colony,
and the trehalose produced is translocated into the fruit-bodies as the main carbohydrate substrate for their development.
Trehalose phosphorylase activity in the vegetative mycelium was at a relatively high level until fruit-body initiation, suggesting
the turnover of this disaccharide during the vegetative stage of the colony development. Trehalose phosphorylase activity
in the stipes showed a peak level at the early phase of fruit-body development, suggesting the continuing phosphorolysis of
trehalose by this enzyme. The stipes also showed a high specific activity of phosphoglucomutase at a sufficient level to facilitate
the conversion of G1P to α-glucose 6-phosphate (G6P). In the pilei a large amount of G1P remained until the growth of the
fruit-bodies ceased. Trehalase activities in the stipes and pilei were at a very low level, and this enzyme may not contribute
to the catabolism of trehalose in the fruit-body development. |
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Keywords: | Flammulina velutipes fruit-body glycogen phosphorylase phosphoglucomutase trehalose phosphorylase |
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