The complete amino acid sequence of glutathione transferase from Proteus mirabilis was determined. The sequence was reconstructed by analysis of peptides obtained after cleavage by trypsin, Glu-C and Asp-N endoproteinases. The enzyme subunit is composed of 203 amino acid residues corresponding to a molecular mass of 22856 Da. Comparison of this sequence with other known primary structures of the corresponding enzyme from different sources shows a low level of identity (17-26%) with only seven conserved residues in all the sequences considered. This novel glutathione transferase could represent the prototype of a new class, possibly including other bacterial enzymes.
The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes / Mignogna, Giuseppina; Allocati, N; Aceto, A; Piccolomini, R; DI ILIO, C; Barra, Donatella; Martini, F.. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - STAMPA. - 211:(1993), pp. 421-425. [10.1111/j.1432-1033.1993.tb17566.x]
The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes.
MIGNOGNA, Giuseppina;BARRA, Donatella;
1993
Abstract
The complete amino acid sequence of glutathione transferase from Proteus mirabilis was determined. The sequence was reconstructed by analysis of peptides obtained after cleavage by trypsin, Glu-C and Asp-N endoproteinases. The enzyme subunit is composed of 203 amino acid residues corresponding to a molecular mass of 22856 Da. Comparison of this sequence with other known primary structures of the corresponding enzyme from different sources shows a low level of identity (17-26%) with only seven conserved residues in all the sequences considered. This novel glutathione transferase could represent the prototype of a new class, possibly including other bacterial enzymes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
