A Calcium-Dependent Xylan-Binding Domain of Alkaline Xylanase from Alkaliphilic Bacillus sp. Strain 41M-1

Xylanase J of alkaliphilic Bacillus sp. strain 41M-1 contains a carbohydrate-binding module family 36 xylan-binding domain (XBD). Mutational analysis of the XBD revealed that Tyr237, Asp313, Trp317, and Asp318 were involved in Ca 2+ -dependent xylan-binding, and that Asp313 and Asp318 were especiall...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2011, Vol.75 (2), p.379-381
Hauptverfasser:	YAZAWA, Risa, TAKAKURA, Jun, SAKATA, Tomoko, IHSANAWATI, YATSUNAMI, Rie, FUKUI, Toshiaki, KUMASAKA, Takashi, TANAKA, Nobuo, NAKAMURA, Satoshi
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus Bacillus - enzymology Bacillus sp Biochemistry Biological and medical sciences Biotechnology Calcium - metabolism carbohydrate-binding module (CBM) family 36 Carbohydrates Endo-1,4-beta Xylanases - chemistry Endo-1,4-beta Xylanases - genetics Endo-1,4-beta Xylanases - metabolism Fundamental and applied biological sciences. Psychology Models, Molecular Modules Mutation Protein Structure, Tertiary Strain xylan-binding domain Xylanase Xylans - metabolism
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Zusammenfassung:	Xylanase J of alkaliphilic Bacillus sp. strain 41M-1 contains a carbohydrate-binding module family 36 xylan-binding domain (XBD). Mutational analysis of the XBD revealed that Tyr237, Asp313, Trp317, and Asp318 were involved in Ca 2+ -dependent xylan-binding, and that Asp313 and Asp318 were especially important.
ISSN:	0916-8451 1347-6947 1347-6947
DOI:	10.1271/bbb.100730