Presence of two trehalose-6-phosphate synthase enzymes in Candida utilis.
Total trehalose-6-phosphate synthase activity decreased in cell extracts from Candida utilis under conditions inducing activation of the regulatory trehalase by protein kinase catalysed phosphorylation. The synthase activity was reactivated by treatment with alkaline phosphatase revealing the presence of an enzyme whose activity is inactivated by reversible phosphorylation. The occurrence in the trehalose-6-phosphate synthase complex of a second synthase enzyme whose activity is not controlled by phosphorylation and dephosphorylation was demonstrated following gel filtration of cell extracts. The activity of the isolated enzymes was differently modified in vitro by the presence of alkaline phosphatase, ATP, glucose or protein kinase.
Vicente-Soler
J
J
Departamento de Genética y Microbiología, Facultad de Biología, Universidad de Murcia, Spain.
Arguelles
J C
JC
Gacto
M
M
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000469:Alkaline Phosphatase / Q000494:pharmacology; D002175:Candida / Q000201:enzymology*; D004789:Enzyme Activation; D005947:Glucose / Q000494:pharmacology; D005964:Glucosyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010766:Phosphorylation
D000255:Adenosine Triphosphate; D005964:Glucosyltransferases; C023180:trehalose-6-phosphate synthase; D000469:Alkaline Phosphatase; D005947:Glucose