Open AccessProtein phosphorylation and trehalase activation in Candida utilis
Author(s) -
Arguelles J.C.,
VicenteSoler J.,
Gacto M.
Publication year - 1986
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.1574-6968.1986.tb01437.x
Subject(s) - trehalase , polyacrylamide gel electrophoresis , tetramer , enzyme , biochemistry , phosphorylation , gel electrophoresis , biology , sodium , chemistry , microbiology and biotechnology , organic chemistry
Candida utilis cells contain a regulatory trehalase enzyme (280 kDa) which can be activated by cAMP‐dependent phosphorylation. A 100‐fold purification of this enzyme activity results in the enrichment of a protein band of apparent M r 70 000 as identified by sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE). This component is phosphorylated in vivo under conditions in which trehalase activation occurs in whole cells. It is concluded that the trehalase enzyme might be a tetramer, composed of 4 identical 70‐kDa subunits.