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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: Paveto, María Cristina
Publicado: 1977
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:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v178_n1_p1_Paveto
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 paper:paper_00039861_v178_n1_p1_Paveto
record_format dspace
spelling paper:paper_00039861_v178_n1_p1_Paveto2023-06-08T14:24:56Z Some kinetic properties of Mucor rouxii phosphofructokinase. Effect of cyclic adenosine 3′,5′-monophosphate Paveto, María Cristina 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. 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v178_n1_p1_Paveto 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, María Cristina
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.
author Paveto, María Cristina
author_facet Paveto, María Cristina
author_sort Paveto, María Cristina
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
publishDate 1977
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v178_n1_p1_Paveto
http://hdl.handle.net/20.500.12110/paper_00039861_v178_n1_p1_Paveto
work_keys_str_mv AT pavetomariacristina somekineticpropertiesofmucorrouxiiphosphofructokinaseeffectofcyclicadenosine35monophosphate
_version_ 1768544251286650880

Ejemplares similares