Sequence similarities in (α/β)8‐barrel enzymes revealed by conserved regions of α‐amylase

FEBS Letters

Janeček, Štefan¹ 

[1] Department of Biochemical Technology, Faculty of Chemical Technology, Slovak Technical University, Radlinského 9, CS-81237 Bratislava, Czech and Slovak Federal Republic

关键词: α-Amylase;    (α/β)8-Barrel enzyme;    Conserved region;    Sequence similarity;    Evolutionary relationship;   

DOI  :  10.1016/0014-5793(93)81729-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The parallel (α/β)₈-barrel is a frequently occurring protein-folding motif. Although the arrangement of secondary structural elements along the barrel is very similar in different (α/β)₈-barrel enzymes, there is a very low mutual amino acid sequence homology among the enzymes, contributing in part to the hazy view of their evolution. Here an approach to identifying at least the rough of evolutionarily conserved (α/β)₈-barrel sequence is presented. Based on the idea that highly conserved sequence regions of a particular enzyme should be more or less conserved in the sequences of the other evolutionary related enzymes, five sequence similarities of ten different (α/β)₈-barrel enzymes were revealed, using the five conserved regions of the amino acid sequence of the α-amylase (α/β)₈-barrel as the templates.

【 授权许可】

Unknown