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 Scopus citations


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
Issue number3
StatePublished - Jan 25 2012


ASJC Scopus subject areas

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

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