Abstract
Nonpeptidyl amine inhibitors are substrates of lysyl oxidase.
Highlights
The activity of highly purified bovine aortic lysyl oxidase against an insoluble aortic elastin substrate is inhibited by lysine, nonpeptidyl derivatives of lysine, P-aminopropionitrile (BAPN), and aliphatic mono- and diamines
Lysyl oxidase is a copper-dependent amine oxidase which catalyzes the oxidation of lysyl residues in collagen and elastin to peptidyl a-aminoadipic-S-semialdehyde (l), the reactive precursor to the variety of inter- and intrapolypeptide crosslinkages found in these proteins
A preliminary report from this laboratory revealed that nonpeptidyl amines, including lysine and its derivatives and homologues, as well as diamines interact with the enzyme since they inhibit the activity of highly purified aortic lysyl oxidase against an elastin-rich aortic substrate [5]
Summary
The activity of highly purified bovine aortic lysyl oxidase against an insoluble aortic elastin substrate is inhibited by lysine, nonpeptidyl derivatives of lysine, P-aminopropionitrile (BAPN), and aliphatic mono- and diamines. Formation of n-butyraldehyde from n-butylamine was measured by the aldehyde dehydrogenase-coupled oxidation of nbutyraldehyde to n-butanoic acid These studies reveal the ability of lysyl oxidase to utilize nonpeptidyl amines as substrates and indicate that these amines must be catalytically processed to irreversibly inhibit this enzyme. A preliminary report from this laboratory revealed that nonpeptidyl amines, including lysine and its derivatives and homologues, as well as diamines interact with the enzyme since they inhibit the activity of highly purified aortic lysyl oxidase against an elastin-rich aortic substrate [5]. We report evidence that these compounds are oxidized to a limited degree by lysyl oxidase yielding hydrogen peroxide and aldehyde products during the course of the time- and temperature-dependent irreversible inactivation of the enzyme which they induce
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