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Cysteamine oxidation by lentil seedling amine oxidase
Author(s) -
Medda Rosaria,
Padiglia Alessandra,
Lorrai Anita,
De Marco Carlo,
Floris Giovanni
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201411
Subject(s) - cysteamine , cystamine , amine oxidase , chemistry , amine gas treating , putrescine , amine oxidase (copper containing) , biochemistry , polyphenol oxidase , enzyme , organic chemistry , peroxidase , diamine oxidase
Abstract Cysteamine is oxidatively deaminated by lentil amine oxidase. It shows saturation kinetic Km=9×10‐4 M like other substrates, but the aldehyde produced leads to loss of enzyme activity, which is restored by dialysis. When putrescine is the substrate of the amine oxidase cysteamine behaves like a competitive inhibitor, and shows Ki=5×10‐5 M. The possible involvement of the oxidation of cysteamine and the inhibitory effects of thioacetaldehyde in the cystamine oxidation by amine oxidase is discussed.