http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12717
Relationships of Cysteine and Lysine residues with the substrate binding site of the mitochondrial ornithine/citrulline carrier: an inhibition kinetic approach combined with the analysis of the homology structural model (Articolo in rivista)
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- Label
- Relationships of Cysteine and Lysine residues with the substrate binding site of the mitochondrial ornithine/citrulline carrier: an inhibition kinetic approach combined with the analysis of the homology structural model (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
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- Annamaria Tonazzi; Nicola Giangregorio; Ferdinando Palmieri; Cesare Indiveri (literal)
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- Rivista
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- National Research Council Institute of Biomembranes and Bioenergetics (IBBE), via Amendola 165/A, 70126, Bari, Italy
Laboratory of Biochemistry and Molecular Biology, Department of Pharmaco-Biology, University of Bari, Via Orabona 4, 70125 Bari, Italy
Department of Cellular Biology, University of Calabria, Via P.Bucci cubo 4c, 87036 Arcavacata di Rende (CS), Italy (literal)
- Titolo
- Relationships of Cysteine and Lysine residues with the substrate binding site of the mitochondrial ornithine/citrulline carrier: an inhibition kinetic approach combined with the analysis of the homology structural model (literal)
- Abstract
- To gain insights in the relationships of specific amino acid residues with the active site of the mitochondrial ornithine/citrulline carrier, we
studied the effect of specific protein modifying reagents on the transport catalysed by the carrier reconstituted into liposomes. It was found that,
besides the sulfhydryl reagents NEM, MTSEA, p-hydroxymercuribenzoate, diamide also the lysine reagents PLP, DIDS, SITS, the carboxyl
reagents WRK, EDC and the arginine reagent methylglyoxal inhibited the carrier. NEM, MTSEA and PLP inhibited the ornithine/citrulline carrier
with a completely competitive type of mechanism. A 1:1 interaction of NEM with the carrier molecule has been demonstrated. The results are in
agreement with the localization of one sulfhydryl and at least one amino group in the substrate binding site. On the basis of the interferences
between SH reagents and PLP in the transport inhibition, it has been deduced that the distance between the SH and the NH2 residues of the active
site should be comparable to the distance between the g-NH2 and COOH residues of the ornithine molecule. The structural model of the ornithine/
citrulline carrier has been obtained by homology modelling using as template the ADP/ATP carrier structure. The combined analysis of the
experimental data and the structural model allows to deduce that Cys-132 is located in the substrate binding site, flanked by at least one Lys
residue (literal)
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