Abstract:
:Activated p38gamma MAP kinase exhibited significant basal ATPase activity in the absence of a kinase substrate, and addition of a phosphoacceptor substrate increased k(cat)/K(m)20-fold. AMP-PCP was competitive with ATP binding and non-competitive with phosphoacceptor substrate binding. The nucleotide binding site affinity label 5'-(p-fluorosulfonylbenzoyl)adenosine (FSBA) bound stoichiometrically at Lys-56 in the ATP site of both unphosphorylated and activated p38gamma. AMP-PCP only protected the activated enzyme from FSBA inactivation, implying that AMP-PCP does not bind unphosphorylated p38gamma. Basal ATPase activities were also observed for activated p38alpha, ERK2 and JNK3 suggesting that the enzymatic mechanism may be similar for all classes of MAP kinases.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fox T,Fitzgibbon MJ,Fleming MA,Hsiao HM,Brummel CL,Su MSdoi
10.1016/s0014-5793(99)01488-xkeywords:
subject
Has Abstractpub_date
1999-11-19 00:00:00pages
323-8issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01488-Xjournal_volume
461pub_type
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