Stereoselective ring opening of 1-phenylcyclopropylamine catalyzed by monoamine oxidase-B

Autor:	Xingliang Lu, Joseph M. Cesarone, Richard B. Silverman
Rok vydání:	1993
Předmět:	Reaction mechanism biology Stereochemistry Chemistry Monoamine oxidase Active site General Chemistry Flavin group Biochemistry Catalysis Adduct Colloid and Surface Chemistry biology.protein Stereoselectivity Monoamine oxidase B Cysteine
Zdroj:	Journal of the American Chemical Society. 115:4955-4961
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja00065a002
Popis:	The inactivation of monoamine oxidase (MAO) by 1-phenylcyclopropylamine (1-PCPA, 1) has been proposed (Silverman, R. B.; Zieske, P. A. Biochemistry 1985, 74, 2128-2138) to proceed via a radical mechanism involving ring opening of an unstable cyclopropylaminyl radical (Scheme 1). This intermediate has been shown to partition between attachment to the N-S position of the covalently-bound flavin cofator, which results in irreversible inactivation, and attachment to an active-site cysteine residue, which results in an unstable adduct that hydrolyzes to release acrylphenoneand active enzyme over time. The stereochemistry and mechanism of the ring-opening step is investigate in this paper
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::a6ac6da0f06218d5914650ab343c9741 https://doi.org/10.1021/ja00065a002 Zobrazit plný text záznamu