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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Essentiality of a newly identified carbohydrate-binding module for the function of CelB (BH0603) from the
Benson Munyali Wamalwa1, Makiko Sakka, Paul Mwanza Shiundu
1Applied Microbiology Laboratory, Faculty of Bioresources, Mie University, 1577 Kurimamachiyacho, Tsu 514-8507, Japan.
CelB (BH0603) from Bacillus halodurans is a modular glycoside hydrolase with a family 5 catalytic module, an immunoglobulin-like module, and module PfamB of unknown function. The recombinant PfamB module bound to Avicel and was essential for CelB hydrolytic function. We propose that module PfamB be designated a new carbohydrate-binding module.
CelB (BH0603) from Bacillus halodurans is a modular glycoside hydrolase with a family 5 catalytic module, an immunoglobulin-like module, and module PfamB of unknown function. The recombinant PfamB module bound to Avicel and was essential for CelB hydrolytic function. We propose that module PfamB be designated a new carbohydrate-binding module.
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