Titlebook: Cellular Regulation by Protein Phosphorylation; Ludwig M. G. Heilmeyer Conference proceedings 1991 Springer-Verlag Berlin Heidelberg 1991

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https://doi.org/10.1007/978-3-540-69315-4mutagenesis was used to introduce single amino-acid substitutions in either cAMP binding site A (Gly to Glu at position 135) or site B (Gly to Glu at position 261). Analysis of the mutated R subunits showed that both single mutants retain high affinity cAMP binding activity (Kd = 20 nM) while cAMP d

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Optimal Transportation Networkso regulatory and two catalytic (C) subunits. Upon binding cAMP the regulatory dimer releases two monomeric C-subunits, which then use MgATP to phosphorylate serine or threonine residues found typically in the sequence Arg-Arg-X-Ser/Thr in target proteins. Protein phosphorylation is a well-known mech

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Interior and Boundary Regularity,A 19 kDa phosphoprotein from mixed envelope membranes of spinach chloroplasts with extreme labelling kinetics has been characterized. Its localization between the inner and the outer envelope membrane can be deduced by the differential labelling between intact and broken chloroplasts (Table 1), (Soll and Bennett 1988, Soll et al. 1989).

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Dynamic Phosphorylation of a Small Chloroplast Protein Exhibiting So Far Undescribed Labelling PropeA 19 kDa phosphoprotein from mixed envelope membranes of spinach chloroplasts with extreme labelling kinetics has been characterized. Its localization between the inner and the outer envelope membrane can be deduced by the differential labelling between intact and broken chloroplasts (Table 1), (Soll and Bennett 1988, Soll et al. 1989).

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