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Purification of Trehalose Synthase From Baker's Yeast. Its Temperature-Dependent Activation by Fructose 6-phosphate and Inhibition by Phosphate

Purification of Trehalose Synthase From Baker's Yeast. Its Temperature-Dependent Activation by Fructose 6-phosphate and Inhibition by Phosphate

J Londesborough, O E Vuorio

Eur J Biochem. 1993 Sep 15;216(3):841-8.

PMID: 8404904

Abstract:

A trehalose synthase purified from baker's yeast contained 56-kDa, 102-kDa and 123-kDa polypeptides as its main components. The 102-kDa polypeptide was isolated and shown to be a specific trehalose-6-phosphatase. The trehalose-6-phosphate synthase (Tre6P synthase) activator described by Londesborough and Vuorio [(1991) J. Gen. Microbiol. 137, 323-330] was shown to be phosphoglucoisomerase and to function entirely by generating fructose 6-phosphate. Below 35 degrees C, fructose 6-phosphate is a powerful activator of the Tre6P synthase activity of intact trehalose synthase, especially at physiological phosphate concentration, but does not affect its trehalose-6-phosphatase activity nor the Tre6P synthase activity of truncated trehalose synthase containing truncated versions of the 123-kDa polypeptide. At 50 degrees C, activation by fructose 6-phosphate and inhibition by phosphate are greatly decreased, resulting in an unusually high temperature-dependence for the Tre6P synthase activity at a physiological phosphate concentration (2 mM).

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001416	Phosphoglucose Isomerase from baker's yeast (S. cerevisiae)		9001-41-6	Price

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