Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family

Shioko Kimura, Masao Ikeda-Saito

Research output: Contribution to journalArticlepeer-review

135 Citations (Scopus)

Abstract

Human myeloperoxidase and human thyroid peroxidase nucleotide and amino acid sequences were compared. The global similarities of the nucleotide and amino acid sequences are 46% and 44%, respectively. These similarities are most evident within the coding sequence, especially that encoding the myeloperoxidase functional subunits. These results clearly indicate that myeloperoxidase and thyroid peroxidase are members of the same gene family and diverged from a common ancestral gene. The residues at 416 in myeloperoxidase and 407 in thyroid peroxidase were estimated as possible candidates for the proximal histidine residues that link to the iron centers of the enzymes. The primary structures around these histidine residues were compared with those of other known peroxidases. The similarity in this region between the two animal peroxidases (amino acid 396–418 in thyroid peroxidase and 405–427 in myeloperoxidase) is 74%; however, those between the animal peroxidases and other yeast and plant peroxidases are not significantly high, although several conserved features have been observed. The possible location of the distal histidine residues in myeloperoxidase and thyroid peroxidase amino acid sequences are also discussed.

Original languageEnglish
Pages (from-to)113-120
Number of pages8
JournalProteins: Structure, Function, and Bioinformatics
Volume3
Issue number2
DOIs
Publication statusPublished - 1988 Jan 1

Keywords

  • distal histidine
  • evolution
  • heme enzyme
  • proximal histidine

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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