Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate

Phosphofructokinase activity was detected in extracts from mycelium and yeast cells of the dimorphic fungus Mucor rouxii. The specific activity of phosphofructokinase is strongly dependent on fungus morphology, being 30-40 times higher in yeast extracts than in extracts of mycelium grown in a medium...

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Autores principales: Paveto, C., Passeron, S.
Formato: JOUR
Materias:
6 phosphofructokinase
cyclic amp
in vitro study
microorganism
mucor rouxii
theoretical study
Adenosine Triphosphate
Citrates
Cyclic AMP
Enzyme Reactivators
Guanosine Triphosphate
Kinetics
Mucor
Phosphofructokinase-1
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00039861_v178_n1_p1_Paveto
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00039861_v178_n1_p1_Paveto
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spelling todo:paper_00039861_v178_n1_p1_Paveto2023-10-03T13:56:52Z Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate Paveto, C. Passeron, S. 6 phosphofructokinase cyclic amp in vitro study microorganism mucor rouxii theoretical study Adenosine Triphosphate Citrates Cyclic AMP Enzyme Reactivators Guanosine Triphosphate Kinetics Mucor Phosphofructokinase-1 Phosphofructokinase activity was detected in extracts from mycelium and yeast cells of the dimorphic fungus Mucor rouxii. The specific activity of phosphofructokinase is strongly dependent on fungus morphology, being 30-40 times higher in yeast extracts than in extracts of mycelium grown in a medium devoid of glucose. These findings are in agreement with the type of metabolism in both forms of the fungus. Phosphofructokinase is inhibited by excess of ATP and by citrate. Both inhibitions are overcome by cyclic adenosine 3′,5′-monophosphate. The probable involvement of phosphofructokinase in controlling morphogenesis in Mucor rouxii and its interaction with cyclic adenosine 3′,5′-monophosphate is suggested. © 1977. Fil:Paveto, C. 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_00039861_v178_n1_p1_Paveto
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 6 phosphofructokinase
cyclic amp
in vitro study
microorganism
mucor rouxii
theoretical study
Adenosine Triphosphate
Citrates
Cyclic AMP
Enzyme Reactivators
Guanosine Triphosphate
Kinetics
Mucor
Phosphofructokinase-1
spellingShingle 6 phosphofructokinase
cyclic amp
in vitro study
microorganism
mucor rouxii
theoretical study
Adenosine Triphosphate
Citrates
Cyclic AMP
Enzyme Reactivators
Guanosine Triphosphate
Kinetics
Mucor
Phosphofructokinase-1
Paveto, C.
Passeron, S.
Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate
topic_facet 6 phosphofructokinase
cyclic amp
in vitro study
microorganism
mucor rouxii
theoretical study
Adenosine Triphosphate
Citrates
Cyclic AMP
Enzyme Reactivators
Guanosine Triphosphate
Kinetics
Mucor
Phosphofructokinase-1
description Phosphofructokinase activity was detected in extracts from mycelium and yeast cells of the dimorphic fungus Mucor rouxii. The specific activity of phosphofructokinase is strongly dependent on fungus morphology, being 30-40 times higher in yeast extracts than in extracts of mycelium grown in a medium devoid of glucose. These findings are in agreement with the type of metabolism in both forms of the fungus. Phosphofructokinase is inhibited by excess of ATP and by citrate. Both inhibitions are overcome by cyclic adenosine 3′,5′-monophosphate. The probable involvement of phosphofructokinase in controlling morphogenesis in Mucor rouxii and its interaction with cyclic adenosine 3′,5′-monophosphate is suggested. © 1977.
format JOUR
author Paveto, C.
Passeron, S.
author_facet Paveto, C.
Passeron, S.
author_sort Paveto, C.
title Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate
title_short Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate
title_full Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate
title_fullStr Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate
title_full_unstemmed Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate
title_sort some kinetic properties of mucor rouxii phosphofructokinase. effect of cyclic adenosine 3′,5′-monophosphate
url http://hdl.handle.net/20.500.12110/paper_00039861_v178_n1_p1_Paveto
work_keys_str_mv AT pavetoc somekineticpropertiesofmucorrouxiiphosphofructokinaseeffectofcyclicadenosine35monophosphate
AT passerons somekineticpropertiesofmucorrouxiiphosphofructokinaseeffectofcyclicadenosine35monophosphate
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