Activation of nucleoside diphosphate kinase by mastoparan, a peptide isolated from wasp venom
نویسندگان
چکیده
منابع مشابه
A novel bioactive peptide from wasp venom
Wasp venoms contain a number of pharmacologically active biomolecules, undertaking a wide range of functions necessary for the wasp's survival. We purified and characterized a novel bioactive peptide (vespin) from the venoms of Vespa magnifica (Smith) wasps with unique primary structure. Its amino acid sequence was determined to be CYQRRVAITAGGLKHRLMSSLIIIIIIRINYLRDNSVIILESSY. It has 44 residue...
متن کاملMastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins).
Mastoparan, a peptide toxin from wasp venom, is a nonspecific secretagogue. We show here that mastoparan increases the GTPase activity and the rate of nucleotide binding of several purified GTP-binding regulatory proteins (G proteins) whose function is to couple cell-surface receptors to intracellular mediators. Mastoparan accelerated guanosine-5'-(3-O-thiotriphosphate binding and consequent G ...
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Nucleoside diphosphate kinase (NDPK) (EC 2.7.4.6), the enzyme transferring the phosphate residue from ATP to nucleoside diphosphates, is localized mainly in the cytoplasm and mitochondria and in smaller amounts in cell nuclei and the microsomal fraction. Exposure of etiolated oat seedlings to red light causes an increase of the enzyme activity by about 42% in nuclear fraction, 7% in etioplastic...
متن کاملNucleoside diphosphate kinase from Escherichia coli.
Nucleoside diphosphate (NDP) kinase from Escherichia coli was purified to homogeneity and was crystallized. Gel filtration analysis of the purified enzyme indicated that it forms a tetramer. The enzyme was phosphorylated with [gamma-32P]ATP, and the pH stability profile of the phosphoenzyme indicated that two different amino acid residues were phosphorylated. Both a histidine residue and serine...
متن کاملldentification as a Nucleoside Diphosphate Kinase'
A low molecular mas (18 kD) phosphoprotein (pp18) was characterized and purified from cultured sugarcane (Saccharum officinarum 1.) cell line H50-7209. Autophosphorylation assays were used to detect pp18 after separation by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PACE). Only pp18 was detected by a brief in situ phosphorylation method, whereas additional putative protein ki...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1992
ISSN: 0014-5793
DOI: 10.1016/0014-5793(92)80676-8