Kinetic mechanism and ATP-binding site reactivity of p38gamma MAP kinase.

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 Lett

journal_title

FEBS letters

authors

Fox T,Fitzgibbon MJ,Fleming MA,Hsiao HM,Brummel CL,Su MS

doi

10.1016/s0014-5793(99)01488-x

keywords:

subject

Has Abstract

pub_date

1999-11-19 00:00:00

pages

323-8

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)01488-X

journal_volume

461

pub_type

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