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001-es BibID:	BIBFORM046026
035-os BibID:	(Scopus)79953702826 (WoS)000289151700006 (PMID)21294844
Első szerző:	Di Paolo, Maria Luisa
Cím:	Active site residue involvement in monoamine or diamine oxidation catalysed by pea seedling amine oxidase / Maria Luisa Di Paolo, Michele Lunelli, Monika Fuxreiter, Adelio Rigo, Istvan Simon, Marina Scarpa
Dátum:	2011
ISSN:	1742-464X
Megjegyzések:	The structures of copper amine oxidases from various sources show good similarity, suggesting similar catalytic mechanisms for all members of this enzyme family. However, the optimal substrates for each member differ, depending on the source of the enzyme and its location. The structural factors underlying substrate selectivity still remain to be discovered. With this in view, we examined the kinetic behaviour of pea seedling amine oxidase with cadaverine and hexylamine, the first bearing two, and the second only one, positively charged amino group. The dependence of K(m) and catalytic constant (k(c)) values on pH, ionic strength and temperature indicates that binding of the monoamine is driven by hydrophobic interactions. Instead, binding of the diamine is strongly facilitated by electrostatic factors, controlled by polar side-chains and two titratable residues present in the active site. The position of the docked substrate is also essential for the participation of titratable amino acid residues in the following catalytic steps. A new mechanistic model explaining the substrate-dependent kinetics of the reaction is discussed. újratöltve - BIBFORM031431
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Febs Journal. - 278 : 8 (2011), p. 1232-1243. -
További szerzők:	Lunelli, Michele Fuxreiter Mónika (1969-) (kutató vegyész) Rigo, Adelio Simon István Scarpa, Marina
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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