Primary and secondary structural analyses of glutathione S-transferase π from human placenta

Hassan Ahmad, Douglas E. Wilson, Richard R. Fritz, Shivendra V. Singh, Rheem D. Medh, Gregg T. Nagle, Yogesh C. Awasthi, Alexander Kurosky

Research output: Contribution to journalArticle

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Abstract

The primary structure of glutathione S-transferase (GST) π from a single human placenta was determined. The structure was established by chemical characterization of tryptic and cyanogen bromide peptides as well as automated sequence analysis of the intact enzyme. The structural analysis indicated that the protein is comprised of 209 amino acid residues and gave no evidence of post-translational modifications. The amino acid sequence differed from that of the deduced amino acid sequence determined by nucleotide sequence analysis of a cDNA clone (Kano, T., Sakai, M., and Muramatsu, M., 1987, Cancer Res.47, 5626-5630) at position 104 which contained both valine and isoleucine whereas the deduced sequence from nucleotide sequence analysis identified only isoleucine at this position. These results demonstrated that in the one individual placenta studied at least two GST π genes are coexpressed, probably as a result of allelomorphism. Computer assisted consensus sequence evaluation identified a hydrophobic region in GST π (residues 155-181) that was predicted to be either a buried transmembrane helical region or a signal sequence region. The significance of this hydrophobic region was interpreted in relation to the mode of action of the enzyme especially in regard to the potential involvement of a histidine in the active site mechanism. A comparison of the chemical similarity of five known human GST complete enzyme structures, one of π, one of μ, two of α, and one microsomal, gave evidence that all five enzymes have evolved by a divergent evolutionary process after gene duplication, with the microsomal enzyme representing the most divergent form.

Original languageEnglish (US)
Pages (from-to)398-408
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume278
Issue number2
DOIs
StatePublished - May 1 1990

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Glutathione Transferase
Placenta
Sequence Analysis
Enzymes
Isoleucine
Amino Acids
Amino Acid Sequence
Nucleotides
Genes
Cyanogen Bromide
Gene Duplication
Consensus Sequence
Valine
Post Translational Protein Processing
Protein Sorting Signals
Histidine
Structural analysis
Catalytic Domain
Complementary DNA
Clone Cells

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Primary and secondary structural analyses of glutathione S-transferase π from human placenta. / Ahmad, Hassan; Wilson, Douglas E.; Fritz, Richard R.; Singh, Shivendra V.; Medh, Rheem D.; Nagle, Gregg T.; Awasthi, Yogesh C.; Kurosky, Alexander.

In: Archives of Biochemistry and Biophysics, Vol. 278, No. 2, 01.05.1990, p. 398-408.

Research output: Contribution to journalArticle

Ahmad, Hassan ; Wilson, Douglas E. ; Fritz, Richard R. ; Singh, Shivendra V. ; Medh, Rheem D. ; Nagle, Gregg T. ; Awasthi, Yogesh C. ; Kurosky, Alexander. / Primary and secondary structural analyses of glutathione S-transferase π from human placenta. In: Archives of Biochemistry and Biophysics. 1990 ; Vol. 278, No. 2. pp. 398-408.
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