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Functional analysis of α-1,3-glucanase domain structure from Streptomyces thermodiastaticus HF3-3
- Source :
- The Journal of General and Applied Microbiology. 67:85-91
- Publication Year :
- 2021
- Publisher :
- Microbiology Research Foundation, 2021.
-
Abstract
- α-1,3-Glucanase from Streptomyces thermodiastaticus HF3-3 (Agl-ST) has been classified in the glycoside hydrolase (GH) family 87. Agl-ST is a multi-modular domain consisting of an N-terminal β-sandwich domain (β-SW), a catalytic domain, an uncharacterized domain (UC), and a C-terminal discoidin domain (DS). Although Agl-ST did not hydrolyze α-1,4-glycosidic bonds, its amino acid sequence is more similar to GH87 mycodextranase than to α-1,3-glucanase. It might be categorized into a new subfamily of GH87. In this study, we investigated the function of the domains. Several fusion proteins of domains with green fluorescence protein (GFP) were constructed to clarify the function of each domain. The results showed that β-SW and DS domains played a role in binding α-1,3-glucan and enhancing the hydrolysis of α-1,3-glucan. The binding domains, β-SW and DS, also showed binding activity toward xylan, although it was lower than that for α-1,3-glucan. The combination of β-SW and DS domains demonstrated high binding and hydrolysis activities of Agl-ST toward α-1,3-glucan, whereas the catalytic domain showed only a catalytic function. The binding domains also achieved effective binding and hydrolysis of α-1,3-glucan in the cell wall complex of Schizophyllum commune.
- Subjects :
- 0106 biological sciences
Domain of a function
0303 health sciences
Mycodextranase
biology
030306 microbiology
Stereochemistry
Chemistry
Schizophyllum commune
Glucanase
biology.organism_classification
01 natural sciences
Applied Microbiology and Biotechnology
Microbiology
Fusion protein
03 medical and health sciences
010608 biotechnology
Glycoside hydrolase
Peptide sequence
Discoidin domain
Subjects
Details
- ISSN :
- 13498037 and 00221260
- Volume :
- 67
- Database :
- OpenAIRE
- Journal :
- The Journal of General and Applied Microbiology
- Accession number :
- edsair.doi...........988d90e8cd15d34fe9c9b3fc057872f3