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 language | English (US) |
|---|---|
| Title of host publication | Methods in Enzymology |
| Publisher | Academic Press Inc. |
| Pages | 149-161 |
| Number of pages | 13 |
| DOIs | |
| State | Published - 2017 |
Publication series
| Name | Methods in Enzymology |
|---|---|
| Volume | 596 |
| 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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Cite this
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