A complex of methylthioadenosine/ S -adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry

Shanzhi Wang; Jihyeon Lim; Keisha Thomas; Funing Yan; Ruth H. Angeletti; Vern L. Schramm

doi:10.1021/ja211176q

A complex of methylthioadenosine/ S -adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry

Shanzhi Wang, Jihyeon Lim, Keisha Thomas, Funing Yan, Ruth H. Angeletti, Vern L. Schramm

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

9 Scopus citations

Abstract

An enzyme-stabilized nucleophilic water molecule has been implicated at the transition state of Escherichia coli methylthioadenosine nucleosidase (EcMTAN) by transition state analysis and crystallography. We analyzed the EcMTAN mass in complex with a femtomolar transition state analogue to determine whether the inhibitor and nucleophilic water could be detected in the gas phase. EcMTAN-inhibitor and EcMTAN-inhibitor-nucleophilic water complexes were identified by high-resolution mass spectrometry under nondenaturing conditions. The enzyme-inhibitor-water complex is sufficiently stable to exist in the gas phase.

Original language	English (US)
Pages (from-to)	1468-1470
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	134
Issue number	3
DOIs	https://doi.org/10.1021/ja211176q
State	Published - Jan 25 2012

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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title = "A complex of methylthioadenosine/ S -adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry",

abstract = "An enzyme-stabilized nucleophilic water molecule has been implicated at the transition state of Escherichia coli methylthioadenosine nucleosidase (EcMTAN) by transition state analysis and crystallography. We analyzed the EcMTAN mass in complex with a femtomolar transition state analogue to determine whether the inhibitor and nucleophilic water could be detected in the gas phase. EcMTAN-inhibitor and EcMTAN-inhibitor-nucleophilic water complexes were identified by high-resolution mass spectrometry under nondenaturing conditions. The enzyme-inhibitor-water complex is sufficiently stable to exist in the gas phase.",

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T1 - A complex of methylthioadenosine/ S -adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry

AU - Wang, Shanzhi

AU - Lim, Jihyeon

AU - Thomas, Keisha

AU - Yan, Funing

AU - Angeletti, Ruth H.

AU - Schramm, Vern L.

PY - 2012/1/25

Y1 - 2012/1/25

N2 - An enzyme-stabilized nucleophilic water molecule has been implicated at the transition state of Escherichia coli methylthioadenosine nucleosidase (EcMTAN) by transition state analysis and crystallography. We analyzed the EcMTAN mass in complex with a femtomolar transition state analogue to determine whether the inhibitor and nucleophilic water could be detected in the gas phase. EcMTAN-inhibitor and EcMTAN-inhibitor-nucleophilic water complexes were identified by high-resolution mass spectrometry under nondenaturing conditions. The enzyme-inhibitor-water complex is sufficiently stable to exist in the gas phase.

AB - An enzyme-stabilized nucleophilic water molecule has been implicated at the transition state of Escherichia coli methylthioadenosine nucleosidase (EcMTAN) by transition state analysis and crystallography. We analyzed the EcMTAN mass in complex with a femtomolar transition state analogue to determine whether the inhibitor and nucleophilic water could be detected in the gas phase. EcMTAN-inhibitor and EcMTAN-inhibitor-nucleophilic water complexes were identified by high-resolution mass spectrometry under nondenaturing conditions. The enzyme-inhibitor-water complex is sufficiently stable to exist in the gas phase.

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A complex of methylthioadenosine/ S -adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry

Abstract

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