Identification by gas chromatography-mass spectrometry of an adduct between pure pig plasma benzylamine oxidase and the inhibitor 3,5-diethoxy-4-aminomethylpyridine.

doi:10.3109/14756369509020134

Paper

Identification by gas chromatography-mass spectrometry of an adduct between pure pig plasma benzylamine oxidase and the inhibitor 3,5-diethoxy-4-aminomethylpyridine.

Published 1995 · F. Buffoni, G. Moneti, G. Pieraccini

Journal of enzyme inhibition

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4

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Abstract

3,5-Diethoxy-4-aminomethylpyridine (B24) interacts with pure pig plasma benzylamine oxidase (BAO), giving a Schiff base with the carbonyl active site. This Schiff base was reduced, isolated by chemical hydrolysis of the enzyme, purified by HPLC and identified by gas chromatography-mass spectrometry (GC-MS) after derivatization. The isolated B24 adduct had the same absorption spectrum, retention time on HPLC and GC and the same mass spectrum as B24-pyridoxamine. B24, which is a reversible enzyme inhibitor, is also a weak substrate and competes with benzylamine, which is the best substrate, for the active site. These results further indicate the presence of pyridoxal-phosphate covalently linked to the pig plasma benzylamine oxidase and involved in the active site of this enzyme.

In Vitro Study

Study Snapshot

The inhibitor 3,5-diethoxy-4-aminomethylpyridine (B24) interacts with pig plasma benzylamine oxidase, forming a Schiff base with the carbonyl active site, suggesting pyridoxal-phosphate involvement in the enzyme's active site.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Identification by gas chromatography-mass spectrometry of an adduct between pure pig plasma benzylamine oxidase and the inhibitor 3,5-diethoxy-4-aminomethylpyridine.

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References

Citations

Evidence of semicarbazide-sensitive amine oxidase activity in guinea pig tissues.

Guinea pigs have tissue-bound semicarbazide-sensitive amine oxidase activities with a high affinity for benzylamine, which can also be found in their blood plasma.

Biochemical aspects and functional role of the copper-containing amine oxidases

Copper-containing amine oxidases play a role in the metabolism of diamines and polyamines, with potential functions in maturing pro-elastin and controlling inflammation.

The mechanism of inhibition of benzylamine oxidase by 3,5-diethoxy-4-aminomethylpyridine (B24).

B24 inhibition of benzylamine oxidase depends on the molar ratio B24/BAO, with a competitive inhibition when the B24/BAO molar ratio is higher than 1, and a mixed inhibition when pre-incubated with the enzyme and the initial rate of benzyl