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.

Identification By Gas Chromatography-Mass Spectrometry Of An Adduct Between Pure Pig Plasma Benzylamine Oxidase And The Inhibitor 3,5-Diethoxy-4-Aminomethylpyridine / F. BUFFONI; G. MONETI; G. PIERACCINI; V. BERTINI. - In: JOURNAL OF ENZYME INHIBITION. - ISSN 8755-5093. - STAMPA. - 8:(1995), pp. 267-279.

Identification By Gas Chromatography-Mass Spectrometry Of An Adduct Between Pure Pig Plasma Benzylamine Oxidase And The Inhibitor 3,5-Diethoxy-4-Aminomethylpyridine

BUFFONI, FRANCA;MONETI, GLORIANO;PIERACCINI, GIUSEPPE;
1995

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.
1995
8
267
279
F. BUFFONI; G. MONETI; G. PIERACCINI; V. BERTINI
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/348820
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