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The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes.
- Source :
-
European Journal of Biochemistry . 2/1/93, Vol. 211 Issue 3, p421-425. 5p. - Publication Year :
- 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 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *MIRABILIS
*GLUTATHIONE transferase
*AMINO acid sequence
*TRYPSIN
*ENZYMES
*PEPTIDES
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 211
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 12123057
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1993.tb17566.x