Abstract
Trehalose-6-phosphate synthase is another example of an enzyme of carbohydrate metabolism, in Saccharomyces, which could be regulated by interconversion of forms. Deactivation was mediated both in vivo and in vitro by a cyclic AMP-dependent protein kinase. Reversibility of this process was obtained by a phosphatase treatment leading to an increase in activity. The phosphorylated, less active form of the enzyme proved to be more susceptible to activation by ATP.Mg. Mutants with well defined lesions in the cyclic AMP-dependent protein kinase system were used to corroborate our findings of a possible regulatory mechanism of trehalose-6-phosphate synthase activity by interconversion of forms.
MeSH Terms
Genes
Genes, Fungal
Genes, Regulator
Glucosyltransferases/genetics,metabolism
Kinetics
Multienzyme Complexes/genetics
Phosphorylation
Protein Kinases/metabolism
Saccharomyces cerevisiae/enzymology,genetics
Species Specificity
Chemicals
Multienzyme Complexes
Glucosyltransferases
trehalose-6-phosphate synthase
Protein Kinases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Panek A C
Departamento de Bioquímica, Instituto de Química, CCMN, Universidade Federal do Rio de Janeiro, Brasil.
de Araujo P S
Moura Neto V
Panek A D
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