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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RARYIBRMPOR-H9hRoHoZOgq5ZD-Yy1jL5n3A51O3cAHYk#_6 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RARYIBRMPOR-H9hRoHoZOgq5ZD-Yy1jL5n3A51O3cAHYk#_5 http://www.w3.org/ns/prov#value We determined the steady-state kinetic parameters of [Tyr(P)185]ERK2 with respect to the phosphorylation of MBP (Fig.1, Table II). The overall rate of substrate processing (k cat) was ?1000-fold higher than that of [unP]ERK2 and 50-fold lower than that of the fully active [PP]ERK2. 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