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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1982
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v214_n2_p573_Moreno http://hdl.handle.net/20.500.12110/paper_00039861_v214_n2_p573_Moreno |
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paper:paper_00039861_v214_n2_p573_Moreno2023-06-08T14:25:00Z Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis Moreno, Silvia N. J. Galvagno, Miguel Angel 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 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. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Galvagno, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1982 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v214_n2_p573_Moreno http://hdl.handle.net/20.500.12110/paper_00039861_v214_n2_p573_Moreno |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Moreno, Silvia N. J. Galvagno, Miguel Angel Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| topic_facet |
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 |
| description |
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. |
| author |
Moreno, Silvia N. J. Galvagno, Miguel Angel |
| author_facet |
Moreno, Silvia N. J. Galvagno, Miguel Angel |
| author_sort |
Moreno, Silvia N. J. |
| title |
Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| title_short |
Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| title_full |
Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| title_fullStr |
Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| title_full_unstemmed |
Control of Mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| title_sort |
control of mucor rouxii adenosine 3′:5′-monophosphate phosphodiesterase by phosphorylation-dephosphorylation and proteolysis |
| publishDate |
1982 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v214_n2_p573_Moreno http://hdl.handle.net/20.500.12110/paper_00039861_v214_n2_p573_Moreno |
| work_keys_str_mv |
AT morenosilvianj controlofmucorrouxiiadenosine35monophosphatephosphodiesterasebyphosphorylationdephosphorylationandproteolysis AT galvagnomiguelangel controlofmucorrouxiiadenosine35monophosphatephosphodiesterasebyphosphorylationdephosphorylationandproteolysis |
| _version_ |
1768544205826686976 |