The evolution of starch‐binding domain

FEBS Letters

Ševčı́k, Jozef¹  Janeček, Štefan² 

[1] Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská cesta 21, SK-84251 Bratislava, Slovakia;Institute of Microbiology, Slovak Academy of Sciences, Štefánikova 3, SK-81434 Bratislava, Slovakia

关键词: Amylolytic enzyme;    Starch-binding domain;    Evolution;    Sequence alignment;    Structure overlap;   

DOI  :  10.1016/S0014-5793(99)00919-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown