Reversible inactivation of bovine plasma amine oxidase by cysteamine and related analogs.

Biochem Biophys Res Commun

Department of Chemistry, Kwangwoon University, Seoul 139-701, Republic of Korea.

Published: December 2010

AI Article Synopsis

  • Cysteamine and certain analogs are identified as reversible inhibitors of bovine plasma amine oxidase (BPAO), while one analog acts as a weak irreversible inhibitor.
  • The study shows that a sulfhydryl-amine group is crucial for the reversible inhibition of BPAO.
  • A proposed mechanism involves the formation of a cofactor adduct called thiazolidine between BPAO and cysteamine.

Article Abstract

Cysteamine (1) was reported many years ago to reversibly inhibit lentil seedling amine oxidase, through the formation of a complex with thioacetaldehyde, the turnover product of 1. Herein, cysteamine (1) and its analogs 2-(methylamino)ethanethiol (3) and 3-aminopropanethiol (6) were found to be reversible inhibitors of bovine plasma amine oxidase (BPAO), but 2-(methylthio)ethylamine (7) was determined to be a weak irreversible inhibitor of BPAO. Based on our results, indicating the necessity of a sulfhydryl-amine for reversible inactivation of BPAO, the failure of inhibited BPAO to recover activity after gel filtration, the first-order kinetics of activity recovery upon dialysis, and 2,4,6-trihydroxyphenylalanine quinine (TPQ) cofactor transformation which indicated from the results of phenylhydrazine titration and substrate protection, we propose a mechanism for the reversible inactivation of BPAO by 1 involving the formation of a cofactor adduct, thiazolidine, between BPAO and 1.

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http://dx.doi.org/10.1016/j.bbrc.2010.11.052DOI Listing

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