While PTPKIS 1 shows activity to generic phosphatase substrates

3710KbAbstractIn the presence of a relatively high concentration of sodium azide N nitrosodiphenylamine undergoes irreversible denitrosation in aqueous acidic media to give diphenylamine. The reaction is catalysed by both H(^+) (with k(_o)oc h(_o)) and various nucleophiles steroid, and for which, at low nucleophile concentrations steroid, a solvent isotope effect of (^k)D/k(_H)= 2.0 is observed. These facts are consistent with rate determining attack by the nucleophile upon the protonated form of the nitrosamine.

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steroids for women It is shown that this chloroplastic protein can bind to glucans through a carbohydrate binding domain (CBM) located within its previously predicted kinase interaction sequence (KIS), while another novel KIS containing protein (AKINy) shows no such interaction. Further analysis of the CBM identifies conserved residues vital for carbohydrate binding and common to CBMs, as well as sugar tongs, not present in similar CBMs or the GBD/KIS domain of the previously studies AMPK, but found within the binding domain of the PTPKIS family proteins. While PTPKIS 1 shows activity to generic phosphatase substrates, it is unable to dephosphorylate either phosphotyrosine or phosphothreonine containing peptides. steroids for women

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