Published in Cancer Weekly, August 11th, 2009
"The c-Met catalytic domain was highly active in the unphosphorylated state (k(cat) = 1.0 s(-1)) and achieved 160-fold enhanced catalytic efficiency (k(cat/)K(m)) upon activation to 425000 s(-1) M-1. c-Met mutants had 2-10-fold higher basal enzymatic: activity (k(cat)) but achieved maximal activities similar to those of wild-type c-Met, except for Y1235D, which underwent a reduction in maximal activity. Small...
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