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

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

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
Externally published	Yes

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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title = "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 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.",

keywords = "GTP binding protein, GTP hydrolysis, Substrate-assisted catalysis, cAMP",

author = "Tsaffrir Zor and Ronit Andorn and Ilya Sofer and Michael Chorev and Zvi Selinger",

note = "Funding Information: for helpful comments on the manuscript. We thank M. Bar-Yaacov for superb technical help. The authors' research was supported by grants from the National institute of Health (EY03529), the United States-Israel Binational Science Foundation (BSF 95-00165) and the Kuhne Minerva Center.",

year = "1998",

month = aug,

day = "21",

doi = "10.1016/S0014-5793(98)00930-2",

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volume = "433",

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journal = "FEBS Letters",

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T1 - GTP analogue hydrolysis by the Gs protein

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

N1 - Funding Information: for helpful comments on the manuscript. We thank M. Bar-Yaacov for superb technical help. The authors' research was supported by grants from the National institute of Health (EY03529), the United States-Israel Binational Science Foundation (BSF 95-00165) and the Kuhne Minerva Center.

PY - 1998/8/21

Y1 - 1998/8/21

N2 - 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.

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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JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

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

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Keywords

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