Animal cells and systems

  • 제2권2호
  • /
  • Pages.243-248
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  • 1998
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  • 1976-8354(pISSN)
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  • 2151-2485(eISSN)
한국통합생물학회 (The Korean Society for Integrative Biology)
권호 표지

Absence of an Essential Thiol in Human Glutaminyl Cyclase: Implications for Mechanism

  • Temple, Jeffrey S. (Department of Chemistry and Biochmistry, University of Southern Mississippi) ;
  • Song, In-Seok (Department of Life Science, University of Seoul) ;
  • Burns, Kathleen H. (Department of Chemistry and Biochmistry, University of Southern Mississippi) ;
  • Bateman, Robert C. (Department of Chemistry and Biochmistry, University of Southern Mississippi)
  • 발행 : 1998.06.01
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초록

We have partially sequenced glutaminyl cyclases from several mammalian and one avian species and found that the two cysteine residues of the human glutaminyl cyclase are completely conserved. The mammalian glutaminyl cyclase has been reported to possess reactive thiols (Busby, Jr, et aI., 1987, J BioI Chern 262, 8532-8536). Mutagenesis of these cysteine residues, however, resulted in only a slight decrease in enzyme activity. Likewise, the recombinant human enzyme was completely resistant to attempted chemical modification of the putative reactive thiols. Although the human glutaminyl cyclase did not appear to have reactive thiols, it was sensitive to diethylpyrocarbonate and acetylimidazole, indicating the presence of functionally important histidine and tyrosine residues which could act as acid/base catalysts. Almost identical deuterium solvent isotope effect (1.2 vs 1.3) upon the reaction by the human and papaya enzymes, respectively, provides an evidence both animal and plant glutaminyl cyclases catalyze pyroglutamyl-peptide formation by intramolecular cyclization.

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참고문헌

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