Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis.
A number of peroxidase amino acid sequences show limited homology to short regions comprising the known active site cleft of yeast cytochrome c peroxidase. Otherwise no clear homology is visible in linear alignments between this enzyme and other peroxidases. We have subjected eight peroxidase sequences to hydrophobic cluster analysis. Our results suggest that these peroxidases are evolutionary related and that they share many folding characteristics.
Henrissat
B
B
Centre de Recherches sur les Macromolécules Végétales, C.N.R.S., Grenoble, France.
Saloheimo
M
M
Lavaitte
S
S
Knowles
J K
JK
D000595:Amino Acid Sequence; D001665:Binding Sites; D003578:Cytochrome-c Peroxidase / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D010544:Peroxidases; D003578:Cytochrome-c Peroxidase