IMR Press / FBL / Volume 3 / Issue 1 / DOI: 10.2741/A247

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article
Aminoalkylaziridines as substrates and inhibitors of lysyl oxidase: specific inactivation of the enzyme by N-(5-aminopentyl)aziridine
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1 Department of Biochemistry, Boston University School of Medicine, 80 East Concord Street, Boston, MA 02118
2 Department of Pharmaceutical Sciences, School of Pharmacy, West Virginia University, Morgantown, WV 26506
Front. Biosci. (Landmark Ed) 1998, 3(1), 23–26; https://doi.org/10.2741/A247
Published: 1 May 1998
Abstract

The reaction of lysyl oxidase was assessed with members of a series of aminoalkylaziridines in which the primary amino group and the aziridinyl nitrogen were separated by 3-7 methylene carbons. Among these, N-(5-aminopentyl)aziridine proved to be the poorest substrate by far and to inhibit the enzyme activity. Aminoalkylaziridines with chain lengths shorter or longer than five carbons did not inhibit the enzyme. The resulting inhibition was competitive with productive substrates and became irreversible with time, following pseudo first order kinetics with a KI of 0.22 mM. N-(5-aminopentyl)aziridine appears to act as a bifunctional affinity label covalently interacting with the active site of this enzyme.

Keywords
Enzymology
Connective Tissue
Lysyl Oxidase
Aminoalkylaziridines
Enzyme Inhibition
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