Anhydrobiosis in nematodes: Biosynthesis of trehalose

Stephen H. Loomis(Mote Marine Laboratory), K. A. C. Madin(Woods Hole Oceanographic Institution), John H. Crowe(Mote Marine Laboratory)
Journal of Experimental Zoology
March 1, 1980
Cited by 26

Abstract

Abstract The pathway for the synthesis of trehalose in Aphelenchus avenae was demonstrated. As in other systems, the enzymes involved in the synthesis of trehalose of A. avenae were found to be trehalose phosphate synthetase (TPS) and trehalosephosphate phosphatase (TPP). Some of the characteristics of trehalose phosphate synthetase were studied. It was found that the rate limiting step in the reaction is catalyzed by TPS. Partially purified TPS was specific for UDPG as the glucosyl donor, and showed a pH optimum of 8.0. The partially purified enzyme has a Km of 0.6 mM and a V max of 2.2 × 10 −3 μmoles/mg protein min for glucose‐6‐phosphate, and a Km of 2.4 mM and V max of 2.5 × 10 −3 μmoles/mg protein minfor UDPG.


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