Open AccessProteolytic activation of α,α‐trehalose 6‐phosphate synthase in Candida utilis
Author(s) -
VicenteSoler J.,
Arguelles J.C.,
Gacto M.
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04858.x
Subject(s) - antipain , pepstatin , biochemistry , enzyme , sephadex , proteases , phenylmethylsulfonyl fluoride , trehalose , atp synthase , serine protease , protease , biology , yeast , leupeptin , chemistry
Total trehalose 6‐phosphate synthase activity increased in cell‐free extracts from Candida utilis following short‐term preincubation of the enzyme samples at 37°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.