N-terminal region of Proteus mirabilis glutathione transferase is not homologous to mammalian and plant glutathione transferases

The N-terminal amino acid sequence of glutathione transferase, Pm-GST-6.0, purified from Proteus mirabilis [(1988) Biochem. J. 255, 971–975] up to residue 38 and a comparative peptide fingerprint are reported. No obvious homology with the sequences of alpha, pi and mu classes of mammalian glutathion...

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Bibliographic Details
Published in:FEBS letters 1989-06, Vol.250 (1), p.57-59
Main Authors: Di Ilio, C., Aceto, A., Piccolomini, R., Allocati, N., Caccuri, A.M., Barra, D., Federici, G.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Bacteria
Biological and medical sciences
Enzymes and enzyme inhibitors
Fingerprint
Fundamental and applied biological sciences. Psychology
Glutathione transferase
Glutathione Transferase - genetics
Mammals - metabolism
Molecular Sequence Data
N-terminal sequence
Plants - enzymology
Plants - genetics
Proteus mirabilis - enzymology
Proteus mirabilis - genetics
Species Specificity
Transferases
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Summary:The N-terminal amino acid sequence of glutathione transferase, Pm-GST-6.0, purified from Proteus mirabilis [(1988) Biochem. J. 255, 971–975] up to residue 38 and a comparative peptide fingerprint are reported. No obvious homology with the sequences of alpha, pi and mu classes of mammalian glutathione transferases as well as with those of plant glutathione transferases has been noted. These results suggest that the classification so far adopted for glutathione transferases cannot be extended to the bacterial enzyme.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)80684-2