On the mechanism of action of GTP-transforming enzymes

Mark J. Dufton; Colin L. Gibson; Andrew R. Pitt; Salah Athmani; Colin J. Suckling

doi:10.1016/S0960-894X(97)00093-0

On the mechanism of action of GTP-transforming enzymes

Mark J. Dufton, Colin L. Gibson, Andrew R. Pitt, Salah Athmani, Colin J. Suckling^*

^*Corresponding author for this work

Analytical, Measurements and Physical Chemistry

University of Strathclyde

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

Abstract

Mechanisms for the ring conversion of GTP into cofactor precursors by GTP cyclohydrolases and molybdopterin synthase are proposed and discussed in the context of the crystal structure of the GTP cyclohydrolase I - 2'-deoxy-GTP complex. The mechanisms suggest that common features of acid-base catalysis may underly the reactions catalysed in all three cases.

Original language	English
Pages (from-to)	779-784
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	7
Issue number	7
DOIs	https://doi.org/10.1016/S0960-894X(97)00093-0
Publication status	Published - 8 Apr 1997

Keywords

bacillus subtilis
crystal structure
enzyme activity
enzyme binding
enzyme mechanism
enzyme structure
escherichia coli
in vitro study

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10.1016/S0960-894X(97)00093-0

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abstract = "Mechanisms for the ring conversion of GTP into cofactor precursors by GTP cyclohydrolases and molybdopterin synthase are proposed and discussed in the context of the crystal structure of the GTP cyclohydrolase I - 2'-deoxy-GTP complex. The mechanisms suggest that common features of acid-base catalysis may underly the reactions catalysed in all three cases.",

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AU - Dufton, Mark J.

AU - Gibson, Colin L.

AU - Pitt, Andrew R.

AU - Athmani, Salah

AU - Suckling, Colin J.

PY - 1997/4/8

Y1 - 1997/4/8

N2 - Mechanisms for the ring conversion of GTP into cofactor precursors by GTP cyclohydrolases and molybdopterin synthase are proposed and discussed in the context of the crystal structure of the GTP cyclohydrolase I - 2'-deoxy-GTP complex. The mechanisms suggest that common features of acid-base catalysis may underly the reactions catalysed in all three cases.

AB - Mechanisms for the ring conversion of GTP into cofactor precursors by GTP cyclohydrolases and molybdopterin synthase are proposed and discussed in the context of the crystal structure of the GTP cyclohydrolase I - 2'-deoxy-GTP complex. The mechanisms suggest that common features of acid-base catalysis may underly the reactions catalysed in all three cases.

KW - bacillus subtilis

KW - crystal structure

KW - enzyme activity

KW - enzyme binding

KW - enzyme mechanism

KW - enzyme structure

KW - escherichia coli

KW - in vitro study

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U2 - 10.1016/S0960-894X(97)00093-0

DO - 10.1016/S0960-894X(97)00093-0

M3 - Article

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VL - 7

SP - 779

EP - 784

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 7

ER -

On the mechanism of action of GTP-transforming enzymes

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Keywords

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