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* A comprehensive review of xylan and lignin cross linkages
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* A recent review by pioneers in the field.
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** An excellent overview of the three-dimensional structures of the major families of glycosyl hydrolases.
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* The catalytic mechanism and overall structure of Clostridium thermocellum CelC, a member of Family 1 cellulases are compared to C. thermocellum XynZ, a member of the Family 10 xylanases.
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** The crystal structure of the catalytic domain of XlnA is a [[alpha]]/[[beta]]8 barrel. This describes the overall shape and catalytic site residues.
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** One of the first structure determinations of Family 10 xylanases.
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** An excellent synthesis of recent crystallographic information.
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** Xyn1 and Xyn2 from T. reesei both belong to Family 11, but are highly differentiated from one another. Structural differences explain both the pH optimum and kinetic characteristics.
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** At the pH optimum for the enzyme (5.0) Tyr88 interacts with Tyr77, but at pH 6.8, it bonds with Glu177, thereby disrupting the catalytic activity. This gives an excellent understanding the pH optimum.
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** The pKaof the acid/base catalyst, Glu172 of the Family 11 xylanase from Bacillus circulans is shown to be abnormally high (6.8) due to the electrostatic interaction with Glu78 and Arg112.
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* This Family 10 xylanase (XylD) from Cellumonas fimi is unusual in that it contains two binding domains, one of which is specific for xylan.
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* TfxA, a thermostable xylanase from T. fusca is unusual in that it is one of only two Family 11 xylanases known to possess a binding domain. The only other example is also found in an actinomycete xylanase, XylB from Streptomyces lividans.
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