Proteolytic activation of α,α-trehalose 6-phosphate synthase in Candida utilis |
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Authors: | J. Vicente-Soler J.C. Arguelles M. Gacto |
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Affiliation: | Departamento de Genética y Microbiología, Facultad de Biología, Universidad de Murcia, Spain. |
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Abstract: | Total trehalose 6-phosphate synthase activity increased in cell-free extracts from Candida utilis following short-term preincubation of the enzyme samples at 37 degrees C. This endogenous activation was prevented by the inhibitors of serine-type proteases, phenylmethylsulfonyl fluoride, antipain or chymostatin, but not by other protease inhibitors such as pepstatin. Fractionation of the cell extracts by Sephadex G-200 gel filtration revealed that the activity of one of the two synthase enzymes present in these cells was enhanced after the activation treatment. These observations indicate the existence of a proteolytically activatable enzyme form in the trehalose 6-phosphate synthase complex of this yeast in addition to the previously characterized enzyme, whose activity appears to be inactivated by reversible phosphorylation. |
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Keywords: | Candida utilis Trehalose 6-phosphate synthase Enzyme activation |
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