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 journalArticle

8 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1468-1470
Number of pages3
JournalJournal of the American Chemical Society
Volume134
Issue number3
DOIs
StatePublished - Jan 25 2012

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adenosylhomocysteine nucleosidase
Escherichia coli
Mass spectrometry
Mass Spectrometry
Water
Enzymes
Gases
Crystallography
Enzyme Inhibitors
Molecules
5'-methylthioadenosine phosphorylase

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

A complex of methylthioadenosine/ S -adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry. / Wang, Shanzhi; Lim, Jihyeon; Thomas, Keisha; Yan, Funing; Angeletti, Ruth H.; Schramm, Vern L.

In: Journal of the American Chemical Society, Vol. 134, No. 3, 25.01.2012, p. 1468-1470.

Research output: Contribution to journalArticle

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AU - Thomas, Keisha

AU - Yan, Funing

AU - Angeletti, Ruth H.

AU - Schramm, Vern L.

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