Polyamines and basic proteins stimulate activation by cAMP and catalytic activity of Mucor rouxii cAMP-dependent protein kinase

Marcelo Guthmann, Ricardo Pastori, Silvia Moreno

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.

Original languageEnglish
Pages (from-to)395-402
Number of pages8
JournalCellular Signalling
Volume2
Issue number4
StatePublished - Dec 1 1990
Externally publishedYes

Fingerprint

kemptide
Mucor
Polyamines
Cyclic AMP-Dependent Protein Kinases
Histones
Proteins
Protamines
Polylysine
Spermidine
Spermine
Enzyme Assays
Protein Kinases
Lysine
Catalytic Domain
Phosphorylation
Enzymes

Keywords

  • cAMP-dependent
  • Mucor rouxii
  • Polyamines
  • Polycations
  • Protein kinase

ASJC Scopus subject areas

  • Cell Biology

Cite this

Polyamines and basic proteins stimulate activation by cAMP and catalytic activity of Mucor rouxii cAMP-dependent protein kinase. / Guthmann, Marcelo; Pastori, Ricardo; Moreno, Silvia.

In: Cellular Signalling, Vol. 2, No. 4, 01.12.1990, p. 395-402.

Research output: Contribution to journalArticle

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