The steady-state kinetic parameters of the amine oxidases purified from Lathyrus cicera (LCAO) and Pisum sativum (PSAO) seedling were measured on a series of common substrates, previously tested on bovine serum amine oxidase (BSAO). LCAO, as PSAO, was substantially more reactive than BSAO with aliphatic diamines and histamine. The k(cat) and k(cat)/K-m for putrescine were four and six order of magnitude higher, respectively. Differences were smaller with some aromatic monoamines. The plot of k(cat) versus hydrogen ions concentration produced bell-shaped curves, the maximum of which was substrate dependent, shifting from neutral pH with putrescine to alkaline pH with phenylethylamine and benzylamine. The latter substrates made the site more hydrophobic and increased the pK(a) of both enzyme-substrate and enzyme-product adducts. The plot of k(cat)/K-m versus hydrogen ion concentration produced approximately parallel bell-shaped curves. Similar pK(a) couples were obtained from the latter curves, in agreement with the assignment as free enzyme and free substrate pK(a). The limited pH dependence of kinetic parameters suggests a predominance of hydrophobic interactions. (c) 2007 Elsevier Inc. All rights reserved.

Substrate specificity of copper-containing plant amine oxidases / Pietrangeli, Paola; R., Federico; Mondovi', Bruno; L., Morpurgo. - In: JOURNAL OF INORGANIC BIOCHEMISTRY. - ISSN 0162-0134. - STAMPA. - 101:7(2007), pp. 997-1004. [10.1016/j.jinorgbio.2007.03.014]

Substrate specificity of copper-containing plant amine oxidases

PIETRANGELI, Paola;MONDOVI', Bruno;
2007

Abstract

The steady-state kinetic parameters of the amine oxidases purified from Lathyrus cicera (LCAO) and Pisum sativum (PSAO) seedling were measured on a series of common substrates, previously tested on bovine serum amine oxidase (BSAO). LCAO, as PSAO, was substantially more reactive than BSAO with aliphatic diamines and histamine. The k(cat) and k(cat)/K-m for putrescine were four and six order of magnitude higher, respectively. Differences were smaller with some aromatic monoamines. The plot of k(cat) versus hydrogen ions concentration produced bell-shaped curves, the maximum of which was substrate dependent, shifting from neutral pH with putrescine to alkaline pH with phenylethylamine and benzylamine. The latter substrates made the site more hydrophobic and increased the pK(a) of both enzyme-substrate and enzyme-product adducts. The plot of k(cat)/K-m versus hydrogen ion concentration produced approximately parallel bell-shaped curves. Similar pK(a) couples were obtained from the latter curves, in agreement with the assignment as free enzyme and free substrate pK(a). The limited pH dependence of kinetic parameters suggests a predominance of hydrophobic interactions. (c) 2007 Elsevier Inc. All rights reserved.
2007
ph dependence; steady-state kinetics; trihydroxyphenylalanine quinone
01 Pubblicazione su rivista::01a Articolo in rivista
Substrate specificity of copper-containing plant amine oxidases / Pietrangeli, Paola; R., Federico; Mondovi', Bruno; L., Morpurgo. - In: JOURNAL OF INORGANIC BIOCHEMISTRY. - ISSN 0162-0134. - STAMPA. - 101:7(2007), pp. 997-1004. [10.1016/j.jinorgbio.2007.03.014]
File allegati a questo prodotto
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/237769
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 10
  • Scopus 47
  • ???jsp.display-item.citation.isi??? 45
social impact