Literature DB >> 2661269

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

C Di Ilio1, A Aceto, R Piccolomini, N Allocati, A M Caccuri, D Barra, G Federici.   

Abstract

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.

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Year:  1989        PMID: 2661269     DOI: 10.1016/0014-5793(89)80684-2

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Glutathione transferase isoenzymes from Bufo bufo embryos at an early developmental stage.

Authors:  C Di Ilio; A Aceto; T Bucciarelli; B Dragani; S Angelucci; M Miranda; A Poma; F Amicarelli; D Barra; G Federici
Journal:  Biochem J       Date:  1992-04-01       Impact factor: 3.857

2.  An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences.

Authors:  S E Pemble; J B Taylor
Journal:  Biochem J       Date:  1992-11-01       Impact factor: 3.857

  2 in total

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