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

Tsaffrir Zor; Ronit Andorn; Ilya Sofer; Michael Chorev; Zvi Selinger

doi:10.1016/S0014-5793(98)00930-2

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

Tsaffrir Zor
, Ronit Andorn
, Ilya Sofer
, Michael Chorev
, Zvi Selinger^*

^*Corresponding author for this work

School of Pharmacy

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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 G_sα 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 γ-phosphate of GTP, is necessary and sufficient to substitute for the function of the catalytic glutamine in the GTPase reaction.

Original language	English
Pages (from-to)	326-330
Number of pages	5
Journal	FEBS Letters
Volume	433
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(98)00930-2
State	Published - 21 Aug 1998

Keywords

GTP binding protein
GTP hydrolysis
Substrate-assisted catalysis
cAMP

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10.1016/S0014-5793(98)00930-2

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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 Gsα 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 γ-phosphate of GTP, is necessary and sufficient to substitute for the function of the catalytic glutamine in the GTPase reaction.",

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T2 - Implication for the role of catalytic glutamine in the GTPase reaction

AU - Zor, Tsaffrir

AU - Andorn, Ronit

AU - Sofer, Ilya

AU - Chorev, Michael

AU - Selinger, Zvi

PY - 1998/8/21

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AB - 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 Gsα 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 γ-phosphate of GTP, is necessary and sufficient to substitute for the function of the catalytic glutamine in the GTPase reaction.

KW - GTP binding protein

KW - GTP hydrolysis

KW - Substrate-assisted catalysis

KW - cAMP

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

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