Measurement of Kinetic Isotope Effects in an Enzyme-Catalyzed Reaction by Continuous-Flow Mass Spectrometry

Kenneth M. Roberts, Paul F. Fitzpatrick

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

Abstract

Kinetic isotope effects (KIEs) provide powerful probes of the mechanisms of enzyme-catalyzed reactions. In this chapter, we describe the use of continuous-flow mass spectrometry to determine the deuterium KIE for the enzyme N-acetylpolyamine oxidase based on the ratio of labeled and unlabeled products in mass spectra of whole reaction mixtures.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages149-161
Number of pages13
DOIs
StatePublished - 2017

Publication series

NameMethods in Enzymology
Volume596
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Amine oxidase
  • Continuous flow
  • Enzyme
  • Flavoprotein
  • Isotope effect
  • Mass spectrometry
  • Polyamine oxidase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Roberts, K. M., & Fitzpatrick, P. F. (2017). Measurement of Kinetic Isotope Effects in an Enzyme-Catalyzed Reaction by Continuous-Flow Mass Spectrometry. In Methods in Enzymology (pp. 149-161). (Methods in Enzymology; Vol. 596). Academic Press Inc.. https://doi.org/10.1016/bs.mie.2017.07.001