Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis

Partially purified cAMP phosphodiesterase from Mucor rouxii can be reversibly activated from 1.5- to 3-fold by treatment with MgATP, cAMP, and cAMP-dependent protein kinase, without change in its sedimentation behavior. Deactivation of activated enzyme can be observed in crude extracts under conditi...

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Detalles Bibliográficos
Autores principales: Moreno, S., Galvagno, M.A., Passeron, S.
Formato: JOUR
Materias:
adenosine triphosphate
cyclic amp
cyclic amp phosphodiesterase
protein kinase
fungus
nonhuman
3',5'-Cyclic-Nucleotide Phosphodiesterase
Adenosine Triphosphate
Centrifugation, Density Gradient
Cyclic AMP
Enzyme Activation
Mucor
Phosphorylation
Protein Kinases
Support, Non-U.S. Gov't
Trypsin
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v214_n2_p573_Moreno
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Partially purified cAMP phosphodiesterase from Mucor rouxii can be reversibly activated from 1.5- to 3-fold by treatment with MgATP, cAMP, and cAMP-dependent protein kinase, without change in its sedimentation behavior. Deactivation of activated enzyme can be observed in crude extracts under conditions which promote dephosphorylation; deactivation is prevented by 20 mm phosphate. cAMP phosphodiesterase can also be irreversibly activated by treatment with trypsin. The extent of activation by proteolysis is similar to that obtained by phosphorylation, but is accompanied by a decrease in the sedimentation coefficient of the enzyme. Activation by phosphorylation and proteolysis are not additive, suggesting that both mechanisms involve the same region of the enzyme molecule. © 1982.

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