Analysis of the glycoside hydrolase family 8 catalytic core in cellulase-chitosanases from Bacillus species

Niveditha Prakash and Shubha Gopal (2014) Analysis of the glycoside hydrolase family 8 catalytic core in cellulase-chitosanases from Bacillus species. International Journal of Computational Bioinformatics and In Silico Modeling, 3 (1). pp. 315-320. ISSN 2320-0634

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Abstract

The glycoside hydrolase family 8 (GH-8) consists of bifunctional cellulase-chitosanases many of which are produced by species of Bacillus. Chitosanolytic enzymes can be useful in producing low molecular weight chitooligosaccharides which have several applications. In addition, a bifunctional enzyme would be more beneficial than the use of two individual enzymes in the production of chitooligosaccharides and in the degradation of the complex cellulose, chitin and chitosan rich biomass that occurs in nature. The crystal structure of a previously determined GH-8 chitosanase has revealed that the catalytic site is constructed on a scaffold of a double α6/α6 barrel which consists of six helix-loop-helix motifs. Bifunctional cellulase-chitosanases from Bacillus species isolated hitherto were analysed and were found to have the double α6/α6 barrel as previously predicted. The signature pattern of glycoside hydrolase family 8 (GH-8) was determined for the sequences. Some of the protein sequences among them were modelled and their closest structural analogs were determined. The structures were found to be related to endoglucanases, xylanases, epimerases and also terpenoid cyclases all of which have the double α6/α6 barrel architecture. This study provides a detailed insight into the structure of cellulase-chitosanase catalytic core and identifies related enzymes with similar catalytic core thereby signifying a possible evolutionary relationship.

Item Type: Article
Subjects: B Life Science > Microbiology
Divisions: Department of > Microbiology
Depositing User: Arshiya Kousar
Date Deposited: 05 Oct 2019 06:37
Last Modified: 05 Oct 2019 06:42
URI: http://eprints.uni-mysore.ac.in/id/eprint/8748

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