Characterization of two casein kinase activities in the fungus Mucor rouxii
Two cyclic-nucleotide independent soluble casein kinase activities (CK I and CK II) from the fungus Mucor rouxii have been isolated, characterized and found to fit in the general classification of type 1 (CK I) and 2 (CK II) casein kinases, according to their enzymatic and structural properties. Bot...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_08957479_v12_n4_p183_Pardo |
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todo:paper_08957479_v12_n4_p183_Pardo2023-10-03T15:42:25Z Characterization of two casein kinase activities in the fungus Mucor rouxii Pardo, P. Moreno, S. casein kinase radioisotope serine threonine fungus mucor rouxii nonhuman priority journal Amino Acids Centrifugation, Density Gradient Chromatography, Affinity Chromatography, Gel Comparative Study Heparin Kinetics Mucor Phosphorylation Polyamines Protein Kinases Solubility Substrate Specificity Support, Non-U.S. Gov't Two cyclic-nucleotide independent soluble casein kinase activities (CK I and CK II) from the fungus Mucor rouxii have been isolated, characterized and found to fit in the general classification of type 1 (CK I) and 2 (CK II) casein kinases, according to their enzymatic and structural properties. Both enzymes phosphorylate acidic substrates, require Mg2+ and have a chromatographic behaviour on DEAE-Sepharose and phosphocellulose similar to their mammalian counterparts. CK I has a sedimentation coefficient of 3.5 S, uses ATP as a phosphate donor (K(m) = 40 μM), phosphorylates casein mainly on serine residues, its activity is strongly inhibited by KCl and polyamines. CK II has a sedimentation coefficient of 7.4 S, uses ATP and GTP as phosphate donors (K(m) ATP = 10 μM; K(m) GTP = 40 μM), phosphorylates casein in serine and threonine, its activity is stimulated by KCl and by polyamines and is inhibited by heparin (I50 = 0.5 μg/ml). Casein kinase activity associated to particulate fraction (40% of total) has been partially characterized and shown to be similar to the soluble CK I activity. Fil:Pardo, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08957479_v12_n4_p183_Pardo |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
casein kinase radioisotope serine threonine fungus mucor rouxii nonhuman priority journal Amino Acids Centrifugation, Density Gradient Chromatography, Affinity Chromatography, Gel Comparative Study Heparin Kinetics Mucor Phosphorylation Polyamines Protein Kinases Solubility Substrate Specificity Support, Non-U.S. Gov't |
| spellingShingle |
casein kinase radioisotope serine threonine fungus mucor rouxii nonhuman priority journal Amino Acids Centrifugation, Density Gradient Chromatography, Affinity Chromatography, Gel Comparative Study Heparin Kinetics Mucor Phosphorylation Polyamines Protein Kinases Solubility Substrate Specificity Support, Non-U.S. Gov't Pardo, P. Moreno, S. Characterization of two casein kinase activities in the fungus Mucor rouxii |
| topic_facet |
casein kinase radioisotope serine threonine fungus mucor rouxii nonhuman priority journal Amino Acids Centrifugation, Density Gradient Chromatography, Affinity Chromatography, Gel Comparative Study Heparin Kinetics Mucor Phosphorylation Polyamines Protein Kinases Solubility Substrate Specificity Support, Non-U.S. Gov't |
| description |
Two cyclic-nucleotide independent soluble casein kinase activities (CK I and CK II) from the fungus Mucor rouxii have been isolated, characterized and found to fit in the general classification of type 1 (CK I) and 2 (CK II) casein kinases, according to their enzymatic and structural properties. Both enzymes phosphorylate acidic substrates, require Mg2+ and have a chromatographic behaviour on DEAE-Sepharose and phosphocellulose similar to their mammalian counterparts. CK I has a sedimentation coefficient of 3.5 S, uses ATP as a phosphate donor (K(m) = 40 μM), phosphorylates casein mainly on serine residues, its activity is strongly inhibited by KCl and polyamines. CK II has a sedimentation coefficient of 7.4 S, uses ATP and GTP as phosphate donors (K(m) ATP = 10 μM; K(m) GTP = 40 μM), phosphorylates casein in serine and threonine, its activity is stimulated by KCl and by polyamines and is inhibited by heparin (I50 = 0.5 μg/ml). Casein kinase activity associated to particulate fraction (40% of total) has been partially characterized and shown to be similar to the soluble CK I activity. |
| format |
JOUR |
| author |
Pardo, P. Moreno, S. |
| author_facet |
Pardo, P. Moreno, S. |
| author_sort |
Pardo, P. |
| title |
Characterization of two casein kinase activities in the fungus Mucor rouxii |
| title_short |
Characterization of two casein kinase activities in the fungus Mucor rouxii |
| title_full |
Characterization of two casein kinase activities in the fungus Mucor rouxii |
| title_fullStr |
Characterization of two casein kinase activities in the fungus Mucor rouxii |
| title_full_unstemmed |
Characterization of two casein kinase activities in the fungus Mucor rouxii |
| title_sort |
characterization of two casein kinase activities in the fungus mucor rouxii |
| url |
http://hdl.handle.net/20.500.12110/paper_08957479_v12_n4_p183_Pardo |
| work_keys_str_mv |
AT pardop characterizationoftwocaseinkinaseactivitiesinthefungusmucorrouxii AT morenos characterizationoftwocaseinkinaseactivitiesinthefungusmucorrouxii |
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1807321992536260608 |