Molecular Evolution of the Myeloperoxidase Family |
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Authors: | Hiromi Daiyasu Hiroyuki Toh |
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Institution: | (1) Department of Bioinformatics, Biomolecular Engineering Research Institute, 6-2-3, Furuedai, Suita 565-0874, Japan, JP |
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Abstract: | Animal myeloperoxidase and its relatives constitute a diverse protein family, which includes myeloperoxidase, eosinophil
peroxidase, thyroid peroxidase, salivary peroxidase, lactoperoxidase, ovoperoxidase, peroxidasin, peroxinectin, cyclooxygenase,
and others. The members of this protein family share a catalytic domain of about 500 amino acid residues in length, although
some members have distinctive mosaic structures. To investigate the evolution of the protein family, we performed a comparative
analysis of its members, using the amino acid sequences and the coordinate data available today. The results obtained in this
study are as follows: (1) 60 amino acid sequences belonging to this family were collected by database searching. We found
a new member of the myeloperoxidase family derived from a bacterium. This is the first report of a bacterial member of this
family. (2) An unrooted phylogenetic tree of the family was constructed according to the alignment. Considering the branching
pattern in the obtained phylogenetic tree, together with the mosaic features in the primary structures, 60 members of the
myeloperoxidase family were classified into 16 subfamilies. (3) We found two molecular features that distinguish cyclooxygenase
from the other members of the protein family. (4) Several structurally deviated segments were identified by a structural comparison
between cyclooxygenase and myeloperoxidase. Some of the segments seemed to be associated with the functional and/or structural
differences between the enzymes.
Received: 25 January 2000 / Accepted: 19 July 2000 |
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Keywords: | : Cyclooxygenase — Mosaic proteins — Heme |
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