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

Autor: Thrower J; Department of Chemistry, University of California, Berkeley, California 94720, USA., Mirica LM, McCusker KP, Klinman JP
Jazyk: angličtina
Zdroj: Biochemistry [Biochemistry] 2006 Oct 31; Vol. 45 (43), pp. 13108-17.
DOI: 10.1021/bi061097q
Abstrakt: 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 O(2) 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 (k(cat)) 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.
Databáze: MEDLINE