Mechanistic studies on ethanolamine ammonia lyase

Vahe Bandarian, G. H. Reed

Research output: Contribution to journalArticle

Abstract

Ethanolamine ammonia lyase catalyzes the deamination of ethanolamine to form acetaldehyde and ammonia - a transformation that requires coenzyme 612- The function of coenzyme 612 is to abstract a hydrogen atom from C1 of the substrate, ethanolamine, to generate a free radical intermediate. This intermediate then rearranges to form a product radical which reacquires the hydrogen that had been abstracted from C1. Deamination of the carbinolamine affords acetaldehyde and ammonia. The participation of free radical intermediates in this reaction was shown two decades ago. We have utilized electron paramagnetic resonance and UV/vis spectroscopies to gain insights into the interaction of holoenzyme with substrates and with substrate analogs.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - 1997
Externally publishedYes

Fingerprint

Ethanolamine Ammonia-Lyase
ammonia-lyases
Deamination
Ethanolamine
ethanolamine
Acetaldehyde
Coenzymes
Ammonia
Free Radicals
Hydrogen
deamination
coenzymes
acetaldehyde
Holoenzymes
hydrogen
Electron Spin Resonance Spectroscopy
Substrates
ammonia
ultraviolet-visible spectroscopy
Spectrum Analysis

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Mechanistic studies on ethanolamine ammonia lyase. / Bandarian, Vahe; Reed, G. H.

In: FASEB Journal, Vol. 11, No. 9, 1997.

Research output: Contribution to journalArticle

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