| Literature DB >> 8436105 |
G Mignogna1, N Allocati, A Aceto, R Piccolomini, C Di Ilio, D Barra, F Martini.
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.Entities:
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Year: 1993 PMID: 8436105 DOI: 10.1111/j.1432-1033.1993.tb17566.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956