Understanding the Positional Binding and Substrate Interaction of a Highly Thermostable GH10 Xylanase from Thermotoga maritima by Molecular Docking
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DOI: 10.3390/biom8030064
Abstract: Glycoside hydrolase family 10 (GH10) xylanases are responsible for enzymatic cleavage of the internal glycosidic linkages of the xylan backbone, to generate xylooligosaccharides (XOS) and xyloses. The topologies of active-site cleft determine the substrate preferences… read more here.
Keywords: understanding positional; gh10; positional binding; thermotoga maritima ... See more keywords
The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region
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DOI: 10.3390/ijms23042315
Abstract: Endoxylanases belonging to family 10 of the glycoside hydrolases (GH10) are versatile in the use of different substrates. Thus, an understanding of the molecular mechanisms underlying substrate specificities could be very useful in the engineering… read more here.
Keywords: gh10; intrinsically disordered; family; disordered region ... See more keywords