The complete amino-acid sequence of mavicyanin, a small blue copper-containing glycoprotein isolated from zucchini peelings, is presented. The sequence of this cupredoxin was deduced from analysis of peptides obtained after cleavage of the protein with trypsin or Asp-N endoproteinase. Mavicyanin consists of a single polypeptide chain of 108 amino-acid residues. Accurate molecular weight determination by electrospray mass spectrometry (12 752 Da) indicates a mass difference of approx. 1005 Da with respect to the mass of the protein, as determined on the basis of the amino-acid sequence (11 747 Da). This difference was tentatively assigned to the carbohydrate moiety, not yet characterized, attached to the protein via an N-linkage to Asn-58 and O-linkages to unidentified Ser/Thr residues. The comparison of the primary structure of mavicyanin with those of other cupredoxins shows that three copper ligands (His-44, Cys-57 and His-90) are conserved, while a glutamine residue (Gln-95), as in stellacyanin, is possibly the fourth ligand. An amino-acid sequence alignment of mavicyanin with copper proteins currently identified as phytocyanins is also proposed, showing same invariant residues in key positions related to the maintenance of the beta-barrel fold and to the active site.

Mavicyanin, a stellacyanin-like protein from zucchini peelings: Primary structure and comparison with other cupredoxins / Schinina', Maria Eugenia; Silvana, Maritano; Barra, Donatella; Mondovi', Bruno; Augusto, Marchesini. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY. - ISSN 0167-4838. - 1297:1(1996), pp. 28-32. [10.1016/0167-4838(96)00079-9]

Mavicyanin, a stellacyanin-like protein from zucchini peelings: Primary structure and comparison with other cupredoxins

SCHININA', Maria Eugenia;BARRA, Donatella;MONDOVI', Bruno;
1996

Abstract

The complete amino-acid sequence of mavicyanin, a small blue copper-containing glycoprotein isolated from zucchini peelings, is presented. The sequence of this cupredoxin was deduced from analysis of peptides obtained after cleavage of the protein with trypsin or Asp-N endoproteinase. Mavicyanin consists of a single polypeptide chain of 108 amino-acid residues. Accurate molecular weight determination by electrospray mass spectrometry (12 752 Da) indicates a mass difference of approx. 1005 Da with respect to the mass of the protein, as determined on the basis of the amino-acid sequence (11 747 Da). This difference was tentatively assigned to the carbohydrate moiety, not yet characterized, attached to the protein via an N-linkage to Asn-58 and O-linkages to unidentified Ser/Thr residues. The comparison of the primary structure of mavicyanin with those of other cupredoxins shows that three copper ligands (His-44, Cys-57 and His-90) are conserved, while a glutamine residue (Gln-95), as in stellacyanin, is possibly the fourth ligand. An amino-acid sequence alignment of mavicyanin with copper proteins currently identified as phytocyanins is also proposed, showing same invariant residues in key positions related to the maintenance of the beta-barrel fold and to the active site.
1996
(c-sativus); blue copper protein; blue copper-protein; c. sativus; phytocyanin; protein primary structure; redox protein; stellacyanin
01 Pubblicazione su rivista::01a Articolo in rivista
Mavicyanin, a stellacyanin-like protein from zucchini peelings: Primary structure and comparison with other cupredoxins / Schinina', Maria Eugenia; Silvana, Maritano; Barra, Donatella; Mondovi', Bruno; Augusto, Marchesini. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY. - ISSN 0167-4838. - 1297:1(1996), pp. 28-32. [10.1016/0167-4838(96)00079-9]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/245335
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