Mechanistic investigations of 1-aminocyclopropane 1-carboxylic acid oxidase with alternate cyclic and acyclic substrates

Julia Thrower, Liviu M. Mirica, Kevin P. McCusker, Judith P. Klinman

Research output: Contribution to journalArticle

Abstract

The behavior of three cyclic and three acyclic analogues of 1-aminocyclopropane-1-carboxylic acid (ACC) with ACC oxidase has been analyzed with regard to turnover rates, product distribution, and O2 uncoupling. The cyclic analogues all form ethylene, and the acyclic analogues all undergo decarboxylation. The degree of uncoupling varies from almost none (ACC) to 21-fold (glycine), while turnover rates (Kcat) are all within a factor of 4-fold of that of ACC. The aggregate data point toward a rate-determining formation of an activated iron-oxo intermediate, which partitions between amine oxidation and reductive uncoupling in a manner that is dependent on substrate structure.

Original languageEnglish (US)
Pages (from-to)13108-13117
Number of pages10
JournalBiochemistry
Volume45
Issue number43
DOIs
StatePublished - Oct 31 2006
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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