The evolution of starch-binding domain
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Updated: Oct 19, 2026

Concanavalin A-Based Sedimentation Assay to Measure Substrate Binding of Glucan Phosphatases
Published on: December 23, 2022
1Institute of Microbiology, Slovak Academy of Sciences, Bratislava, Slovakia. sjanecek@ue.savba.sk
Abstract:
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.
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