Abstract
CYSTEAMINE has been shown to cause a transient inhibition of diamine oxidase1, which was explained by its coupling with pyridoxal phosphate in a thiazolidine ring. Even when linked to pyridoxal phosphate thiols may undergo oxidation to the corresponding disulphides2,3 in the case of cysteamine the non-enzymatic oxidation to cystamine liberates pyridoxal phosphate, and the diamine oxidase activity is restored. Because the enzyme oxidizes cystamine4, we have an interesting example of an inhibitor which is changed into a substrate during the reaction.
Similar content being viewed by others
Article PDF
References
De Marco, C., Mondoví, B., and Cavallini, D., Biochem. Pharmacology, 2, 509 (1962).
De Marco, C., and Bognolo, D., Arch. Biochem. Biophys., 98, 526 (1962).
De Marco, C., Bognolo, D., and Cavallini, D., Ital. J. Biochem., 12, 186 (1963).
Cavallini, D., De Marco, C., and Mondoví, B., Biochim. Biophys. Acta, 24, 353 (1957).
Yamada, H., and Yasunobu, K. T., J. Biol. Chem., 237, 1511 (1962).
Bergeret, B., and Blaschko, H., Brit. J. Pharm. and Chemotherapy, 12, 513 (1957).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
DE MARCO, C., COLETTA, M. & BOMBARDIERI, G. Inhibition of Plasma Monoamine Oxidase by Cysteamine. Nature 205, 176 (1965). https://doi.org/10.1038/205176a0
Published:
Issue Date:
DOI: https://doi.org/10.1038/205176a0
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.