STRUCTURAL HOMOLOGY AMONG THE PEROXIDASE ENZYME FAMILY REVEALED BY HYDROPHOBIC CLUSTER-ANALYSIS

被引:54
作者
HENRISSAT, B [1 ]
SALOHEIMO, M [1 ]
LAVAITTE, S [1 ]
KNOWLES, JKC [1 ]
机构
[1] VALT TEKNILLINEN TUTKIMUSKESKUS, BIOTECH LAB, SF-02150 ESPOO, FINLAND
关键词
active site; hydrophobic cluster analysis; peroxidase; sequence comparison; structure conservation;
D O I
10.1002/prot.340080307
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. Copyright © 1990 Wiley‐Liss, Inc.
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页码:251 / 257
页数:7
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