The evolution of starch-binding domain

被引:96
作者
Janecek, S
Sevcík, J
机构
[1] Slovak Acad Sci, Inst Microbiol, SK-81434 Bratislava, Slovakia
[2] Slovak Acad Sci, Inst Mol Biol, SK-84251 Bratislava, Slovakia
关键词
amylolytic enzyme; starch-binding domain; evolution; sequence alignment; structure overlap;
D O I
10.1016/S0014-5793(99)00919-9
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
Amylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain the starch-binding domain (SBD) positioned almost exclusively at the C-terminus, Detailed analysis of all available SBD sequences from 43 different amylases revealed its independent evolutionary behaviour with regard to the catalytic domains. In the evolutionary tree based on sequence alignment of the SBDs, taxonomy is respected so that fungi and actinomycetes form their own separate parts surrounded by bacteria that are also clustered according to taxonomy. The only known N-terminal SBD from Rhizopus oryzae glucoamylase is on the longest branch separated from all C-terminal SBDs. The 3-dimensional (3-D) structures of fungal glucoamylase and bacterial CGTase SBDs are compared and used to discuss the interesting SBD evolution. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:119 / 125
页数:7
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