lysine-tyrosylquinone has been researched along with benzylamine* in 2 studies
2 other study(ies) available for lysine-tyrosylquinone and benzylamine
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Characterization of a model compound for the lysine tyrosylquinone cofactor of lysyl oxidase.
We characterized a model compound for the lysine tyrosylquinone (LTQ) cofactor of lysyl oxidase which is one of the mammalian copper-dependent amine oxidases. The model compound, 4-butylamino-5-methyl-o-quinone, was prepared from n-butylamine and 4-methylcatechol by the oxidation with sodium iodate and characterized by spectroscopic analyses. The absorption maximum at 494 nm is consistent with that of lysyl oxidase. The model compound was capable of deaminating benzylamine to benzaldehyde at 37 degrees C in buffered aqueous acetonitrile. The aldehyde production was markedly elevated in the presence of the Cu(II)-EDTA complex but inhibited by free Cu(II). The catalytic cycle was observed at pH 10 in the presence of Cu(II), and the pH activity profile showed a broad optimum at about pH 9.0. In the presence of beta-aminopropionitrile and upon deoxygenation with N2 aldelyde, production was decreased. The important features of the reaction were consistent with the enzymatic reaction. Topics: Acetonitriles; Aminopropionitrile; Antioxidants; Benzaldehydes; Benzoquinones; Benzylamines; Butylamines; Catechols; Copper; Edetic Acid; Hydrogen-Ion Concentration; Iodates; Lysine; Magnetic Resonance Spectroscopy; Models, Chemical; Oxygen; Protein-Lysine 6-Oxidase; Quinones; Spectrophotometry; Time Factors; Ultraviolet Rays | 2001 |
Catalytic turnover of benzylamine by a model for the lysine tyrosylquinone (LTQ) cofactor of lysyl oxidase.
Lysyl oxidase differs from other copper amine oxidases in that its active quinone cofactor reflects cross-linking of a lysyl residue into the tyrosine-derived quinone nucleus found in the plasma and other copper amine oxidases. A model for the lysyl oxidase cofactor (LTQ), 3,3-dimethyl-2,3-dihydroindole-5,6-quinone (4), was synthesized and found to be stable to both hydrolysis and oxidation events that prevent simpler models from functioning as turnover catalysts. We show that 4 catalyzes the aerobic oxidative deamination of benzylamine, though turnover eventually ceases on account of oxidation of the dihydrobenzoxazole tautomer of the "product Schiff base" to form a benzoxazole, a reaction that may be physiologically relevant. The mechanism of the overall reaction profile was elucidated by a combination of optical and NMR spectroscopy and O(2) uptake studies. Topics: Benzylamines; Catalysis; Deamination; Kinetics; Lysine; Models, Chemical; Protein-Lysine 6-Oxidase; Quinones | 2001 |