Pietro Pucci

Professor of Biochemistry

Name Pietro
Surname Pucci
Institution Università degli Studi della Campania Luigi Vanvitelli
Telephone +39 081 674 318 (UniNa)
Telephone 2 +39 081 373 7896 (Ceinge)
E-Mail pucci@unina.it
Address Department of Chemical Sciences, Federico II University, Via Cintia 6, 80126, Naples, Italy
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Pietro Pucci

Member PUBLICATIONS

  • Enzymatic methyl esterification of synthetic tripeptides: structural requirements of the peptide substrate. Detection of the reaction products by fast-atom-bombardment mass spectrometry.

    Publication Date: 15/10/1988 on European journal of biochemistry
    by Galletti P, Ingrosso D, Manna C, Sica F, Capasso S, Pucci P, Marino G

    Eukaryotic protein carboxyl methyltransferase catalyzes a two-substrates reaction in which the methyl group of S-adenosylmethionine is transferred to the free carboxyl group of D-aspartyl and L-isoaspartyl-containing peptide or protein substrates. It has been previously shown that at least three binding sites are required for the interaction of adenosylmethionine with the enzyme and/or the protein substrate [Oliva A., Galletti P., Zappia V., Paik W. K. & Kim S. (1980) Eur. J. Biochem. 104, 595-602], while very little is known concerning the structural requirements of the protein substrate. In this study several synthetic tripeptides were selected in order to elucidate the structural requirements of the methyl-accepting substrates. The results obtained with this series of peptides suggested that: (1) three residues appear to be the minimal length, so far identified, required for a productive enzyme-substrate interaction, several dipeptides being ineffective as substrates [McFadden P. N. & Clarke S. (1986) J. Biol. Chem. 261, 11,503-11,511]; (2) the isoaspartyl residue is not recognized unless its alpha-amino group is involved in a carboamide bond; (3) an hydrogen atom on the amide linkage following the isoaspartyl residue is essential for both recognition and catalysis; (4) oligopeptides containing both D-aspartyl and D-isoaspartyl residues are not recognized by this methyltransferase. On the basis of these results, interaction sites between the peptide substrate and the enzyme molecule have been proposed. This paper also reports the first application of fast-atom-bombardment mass spectrometry to the detection of the products of the enzymatic methyl esterification reaction. By this soft ionization technique, the methyl-esterified peptides as well as the corresponding cyclic imides generated during the spontaneous demethylation process have been identified.

  • Isolation and characterization of dipeptidyl peptidase IV from human meconium. Functional role of beta-casomorphins.

    Publication Date: 20/05/1985 on FEBS letters
    by Caporale C, Fontanella A, Petrilli P, Pucci P, Molinaro MF, Picone D, Auricchio S

    Dipeptidyl aminopeptidase IV (DAP-IV) (EC 3.4.14.1) was purified from meconium particles sedimenting at 105 000 X g. Its molecular properties and activity on synthetic and natural substrates (casomorphin and procasomorphin) were investigated.