Contemporary mass spectrometry for the direct detection of enzyme intermediates

Neil L. Kelleher*, Leslie M. Hicks

*Corresponding author for this work

Research output: Contribution to journalReview article

15 Scopus citations

Abstract

The field of enzymology has long used small-molecule mass spectrometry. However, the direct interrogation of covalent and non-covalent intermediates by large-molecule mass spectrometry of enzymes or large peptide substrates is illuminating an increasingly diverse array of chemistries used in nature. Recent advances now allow improved detection of several modifications formed at sub-stoichiometric levels on the same polypeptide, and elucidation of intermediate dynamics with low millisecond temporal resolution. Highlighting recent applications in both ribosomal and non-ribosomal biosynthesis of natural products, along with acetyl transferases, sulfonucleotide reducatases, and PEP-utilizing enzymes, the utility of small- and large-molecule mass spectrometry to reveal enzyme intermediates and illuminate mechanism is described briefly. From ever more complex mixtures, mass spectrometry continues to evolve into a key technology for a larger number of today's enzymologists.

Original languageEnglish (US)
Pages (from-to)424-430
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume9
Issue number5
DOIs
StatePublished - Oct 1 2005

ASJC Scopus subject areas

  • Biochemistry

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