Phosphoregulatory tyrosine of Xenopus mitogen-activated protein kinase is out of the reach of the enzyme catalytic center after autophosphorylation. Biochemical evidence for conformational changes upon phosphorylation.

Abstract excerpt

Autophosphorylation of the recombinant mitogen-activated protein kinase (MAPK) from Xenopus laevis has been studied to detect the conformational changes in the region of regulatory phosphorylation upon enzyme activation. Slow autophosphorylation of Xenopus MAPK occurred predominantly on tyrosine, the major phosphoregulatory site of MAPKs, through an intramolecular mechanism and was accompanied by a low magnitude...

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