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Cyclic AMP‐dependent protein kinase does not phosphorylate cyclic GMP‐dependent protein kinase in vitro
Author(s) -
Hofmann F.,
Gensheimer H.-P.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80345-7
Subject(s) - autophosphorylation , protein kinase a , cgmp dependent protein kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , map2k7 , cyclin dependent kinase 9 , biochemistry , pde10a , chemistry , protein subunit , mapk14 , kinase , microbiology and biotechnology , biology , enzyme , phosphodiesterase , gene
The autophosphorylation reaction of purified cGMP‐dependent protein kinase has been studied. Apparent initial rates of autophosphorylation in the absence of cyclic nucleotides and in the presence of cGMP and cAMP are 0.006, 0.04, 0.4 mol. P i incorp./min −1 .mol cGMP‐kinase subunit −1 . In the presence of cGMP and cAMP ∼1 and 2 mol P 1 are incorporated/mol enzyme subunit. These values are independent of the enzyme concentration. Stimulation of autophosphorylation by cAMP is not due to activation of a contaminating cAMP‐dependent protein kinase since: (a) addition of the heatstable inhibitor protein of cAMP‐kinase does not inhibit autophosphorylation; and (b) catalytic subunit of cAMP‐kinase added at a 10‐fold excess over cGMP‐kinase does not phosphorylate cGMP‐kinase.