通过疏水簇分析揭示的过氧化物酶家族中的结构同源性。
Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis.
作者信息
Henrissat B, Saloheimo M, Lavaitte S, Knowles J K
机构信息
Centre de Recherches sur les Macromolécules Végétales, C.N.R.S., Grenoble, France.
出版信息
Proteins. 1990;8(3):251-7. doi: 10.1002/prot.340080307.
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.
许多过氧化物酶的氨基酸序列与构成酵母细胞色素c过氧化物酶已知活性位点裂隙的短区域显示出有限的同源性。否则，在该酶与其他过氧化物酶的线性比对中没有明显的同源性。我们对八个过氧化物酶序列进行了疏水簇分析。我们的结果表明，这些过氧化物酶在进化上相关，并且它们具有许多折叠特征。
Zotero 插件