Human liver glutathione S-transferase ψ. Chemical characterization and secondary-structure comparison with other mammalian glutathione S-transferases

S. V. Singh, A. Kurosky, Y. C. Awasthi

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    Abstract

    The isolation and chemical characterization of the anionic human liver glutathione S-transferase (GST) ψ (pI 5.5) are described and compared with other GST isoenzymes reported for rat and human. Amino acid compositional analysis, substrate specificity and isoelectric focusing indicated that GST ψ is a unique isoenzyme form of GST. Strikingly, however, amino acid sequence analysis of the N-terminal region indicated that GST ψ was identical with GST μ in the first 23 amino acid residues reported. It is likely that these two enzyme forms are at least partially structurally related. In order to investigate further the genetic relationship of GST ψ to other reported GST isoenzymes, secondary-structure analysis was performed. Despite substantial differences in the N-terminal-region amino acid sequences of some of the GST isoenzymes, the secondary structure of all the isoenzymes is highly conserved at their N-termini. The general uniformity of the secondary structure of this enzyme class at their N-termini strongly indicated that the observed diversity of these isoenzymes probably occurred as a result of a mechanism of gene duplication followed by divergence rather than a mechanism of convergent evolution.

    Original languageEnglish (US)
    Pages (from-to)61-67
    Number of pages7
    JournalBiochemical Journal
    Volume243
    Issue number1
    StatePublished - 1987

    Fingerprint

    Glutathione Transferase
    Liver
    Isoenzymes
    Amino Acids
    Glutathione S-Transferase pi
    Gene Duplication
    Protein Sequence Analysis
    Isoelectric Focusing
    Enzymes
    Substrate Specificity
    Rats
    Amino Acid Sequence
    Genes
    Substrates

    ASJC Scopus subject areas

    • Biochemistry

    Cite this

    Human liver glutathione S-transferase ψ. Chemical characterization and secondary-structure comparison with other mammalian glutathione S-transferases. / Singh, S. V.; Kurosky, A.; Awasthi, Y. C.

    In: Biochemical Journal, Vol. 243, No. 1, 1987, p. 61-67.

    Research output: Contribution to journalArticle

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    N2 - The isolation and chemical characterization of the anionic human liver glutathione S-transferase (GST) ψ (pI 5.5) are described and compared with other GST isoenzymes reported for rat and human. Amino acid compositional analysis, substrate specificity and isoelectric focusing indicated that GST ψ is a unique isoenzyme form of GST. Strikingly, however, amino acid sequence analysis of the N-terminal region indicated that GST ψ was identical with GST μ in the first 23 amino acid residues reported. It is likely that these two enzyme forms are at least partially structurally related. In order to investigate further the genetic relationship of GST ψ to other reported GST isoenzymes, secondary-structure analysis was performed. Despite substantial differences in the N-terminal-region amino acid sequences of some of the GST isoenzymes, the secondary structure of all the isoenzymes is highly conserved at their N-termini. The general uniformity of the secondary structure of this enzyme class at their N-termini strongly indicated that the observed diversity of these isoenzymes probably occurred as a result of a mechanism of gene duplication followed by divergence rather than a mechanism of convergent evolution.

    AB - The isolation and chemical characterization of the anionic human liver glutathione S-transferase (GST) ψ (pI 5.5) are described and compared with other GST isoenzymes reported for rat and human. Amino acid compositional analysis, substrate specificity and isoelectric focusing indicated that GST ψ is a unique isoenzyme form of GST. Strikingly, however, amino acid sequence analysis of the N-terminal region indicated that GST ψ was identical with GST μ in the first 23 amino acid residues reported. It is likely that these two enzyme forms are at least partially structurally related. In order to investigate further the genetic relationship of GST ψ to other reported GST isoenzymes, secondary-structure analysis was performed. Despite substantial differences in the N-terminal-region amino acid sequences of some of the GST isoenzymes, the secondary structure of all the isoenzymes is highly conserved at their N-termini. The general uniformity of the secondary structure of this enzyme class at their N-termini strongly indicated that the observed diversity of these isoenzymes probably occurred as a result of a mechanism of gene duplication followed by divergence rather than a mechanism of convergent evolution.

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