Abstract：
:In this paper, we report on the presence of cation binding areas on bovine serum amine oxidase, where metal ions of the groups IA and IIA, such as Na(+), K(+), Cs(+), Mg(2+), and Ca(2+), bind with various affinities. We found a cation-binding area that influences the enzyme activity if occupied, so that the catalytic reaction may be altered by some physiologically relevant cations, such as Ca(2+) and K(+). This binding area appears to be localized inside the enzyme active site, because some of these cations act as competitive inhibitors when highly charged amines, such as spermine and spermidine, are used as substrates. In particular, dissociation constant values (K(d)) of 23 and 27 mM were measured for Cs(+) and Ca(2+), respectively, using, as substrate, spermine, a polyamine of plasma. An additional cation-binding area, where metal ions such as Cs(+) (K(d) congruent with 0.1 mM) and Na(+) (K(d) congruent with 54 mM) bind without affecting the enzyme activity, was found by NMR.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Di Paolo ML,Scarpa M,Corazza A,Stevanato R,Rigo Adoi
10.1016/S0006-3495(02)73983-0subject
Has Abstractpub_date
2002-10-01 00:00:00pages
2231-9issue
4eissn
0006-3495issn
1542-0086pii
S0006-3495(02)73983-0journal_volume
83pub_type
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