GTP analogue hydrolysis by the Gs protein: implication for the role of catalytic glutamine in the GTPase reaction.

Abstract:

:Hydrolysis of GTP, bound to members of the G-protein superfamily, terminates their downstream signaling activity. A conserved glutamine serves a critical role in this pivotal guanosine triphosphatase (GTPase) reaction. However, the role of the catalytic glutamine in GTP hydrolysis is still not well understood. We have employed substrate-assisted catalysis to probe the catalytic mechanism of Gs alpha using GTP analogues. These GTP analogues, each having different functional groups, were designed to support or refute particular putative GTPase mechanisms. We have found that a hydrogen donor group, in close proximity to the gamma-phosphate of GTP, is necessary and sufficient to substitute for the function of the catalytic glutamine in the GTPase reaction.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zor T,Andorn R,Sofer I,Chorev M,Selinger Z

doi

10.1016/s0014-5793(98)00930-2

subject

Has Abstract

pub_date

1998-08-21 00:00:00

pages

326-30

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00930-2

journal_volume

433

pub_type

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