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 as a courtesy and upon agreement with Frontiers in Bioscience.

Aminoalkylaziridines as substrates and inhibitors of lysyl oxidase: specific inactivation of the enzyme by N-(5-aminopentyl)aziridine
Show Less
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;
Published: 1 May 1998

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.

Connective Tissue
Lysyl Oxidase
Enzyme Inhibition
Back to top