Variation in isomeric products of a phosphodiesterase from the chloroplasts ofPhaseolus vulgarisin response to cations
| Autor: | A. Gareth Brenton, Michael Oliver, Terence J. Walton, Harry Van Onckelen, Christopher J. Smith, Luc Roef, Russell P. Newton, David E. Games, Penny E. Diffley, Jan van Cleef, A.C.R. Wilkins, Mark A. Bayliss, Frank M. Harris, Erwin Witters, Alan Geisbrecht, Jan van Geyschem, Judith M. Vaughan |
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| Rok vydání: | 2001 |
| Předmět: |
inorganic chemicals
chemistry.chemical_classification biology Chemistry Stereochemistry Phosphodiesterase Plant Science biology.organism_classification Mass spectrometry Dissociation (chemistry) Chloroplast Hydrolysis Biochemistry Nucleotidase Nucleotide Phaseolus Ecology Evolution Behavior and Systematics |
| Zdroj: | Plant Biosystems - An International Journal Dealing with all Aspects of Plant Biology. 135:143-156 |
| ISSN: | 1724-5575 1126-3504 |
| DOI: | 10.1080/11263500112331350760 |
| Popis: | Fast-atom bombardment mass spectrometry (FABMS), and collisionally-induced dissociation and mass-analyzed ion kinetic energy spectrum scanning (CID/MIKES) have been used to examine cation effects on a Phaseolus chloroplast complex phosphodiesterase activity. The kinetic parameters of the activity, and the effects of Li+, Na+, K+, Mg2+, Mn2+ and Fe3+ upon them, were determined with 3′,5′-cyclic AMP, -GMP and -CMP, and 2′,3′-cyclic AMP, -GMP and -CMP as substrates. Irrespective of the presence of cations and of the complex nucleotidase, the preferred substrate is a 3′,5′-cyclic nucleotide, not a 2′,3′-cyclic nucleotide. In the presence of the nucleotidase 3′,5′-cyclic AMP and 3′,5′-cyclic GMP are the best substrates, unless Fe3+ ions are present. Mg2+ and Mn2+ stimulate hydrolysis of 3′,5′-cyclic AMP and 3′,5′-cyclic GMP by the complex. However, Fe3+ inhibits these activities but stimulates the hydrolysis of 3′,5′-cyclic CMP. Kinetic data indicate that each of these six substrates is hydrolyzed at ... |
| Databáze: | OpenAIRE |
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