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Early studies from the Nishizuka laboratory implicated tyrosine phosphorylation as a mechanism to regulate PKC catalytic activity, showing that the tyrosine-phosphorylated enzyme is a constitutively activate enzyme that no longer requires DAG as a cofactor to phosphorylate substrates ( 52 and Tyr 187 ) and a series of tyrosine residues in the kinase domain [Tyr 451 , Tyr 469 , Tyr 512 , Tyr 523 ( 311 (in the more variable flexible hinge region of the enzyme) mediates the H 2 O 2 -dependent increase in PKC activity ( 311 in rodent PKC corresponds to Tyr 313 in human PKC

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