TERTIARY STRUCTURE OF XYLANASE AND ESTIMATION OF ACTIVE SITES BY SITE DIRECTED MUTAGENESIS

Okada, Hirosuke

dc.contributor.author	Okada, Hirosuke
dc.date.accessioned	2023-11-03T09:31:46Z
dc.date.available	2023-11-03T09:31:46Z
dc.date.issued	1989
dc.date.submitted	2023-11-03
dc.identifier.citation	Advances in protein design, 81 - 86	en_US
dc.identifier.isbn	3527280243
dc.identifier.isbn	0895739534
dc.identifier.issn	0930-4320
dc.identifier.uri	http://hdl.handle.net/10033/623523
dc.description.abstract	The nucleotide sequence of xylanase gene(xynA) of Bacillus pumilus IPO, a hyperproducer of xylanase, was determined and the amino acid sequence was deduced from it. Xylanase is produced as a preenzyme consisting of the mature enzyme of 201 amino acid residues and a signal peptide of 27 residues. Xylanase was analyzed by X-ray crystallography at the level of 2.2 A resolution. It is consisted with two domains, smaller and larger, between two a crevasse suitable to accept xylan molecule was observed. The mutant xylanases obtained by site directed mutagenesis having amino acid alteration; Glu93-Ser93 and Glul82_Asp182 had no catalytic activity (less than 1/10,000).	en_US
dc.language.iso	en	en_US
dc.publisher	GBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweig	en_US
dc.relation.ispartofseries	GBF monographs ; Volume 12	en_US
dc.rights	Attribution-NonCommercial-ShareAlike 4.0 International	*
dc.rights.uri	http://creativecommons.org/licenses/by-nc-sa/4.0/	*
dc.title	TERTIARY STRUCTURE OF XYLANASE AND ESTIMATION OF ACTIVE SITES BY SITE DIRECTED MUTAGENESIS	en_US
dc.type	Book chapter	en_US
dc.type	conference paper	en_US
dc.contributor.department	Department of Fermentation Technology, and The International Cooperative Research Center for Biotechnology, Osaka University	en_US
dc.identifier.journal	Advances in protein design, 1988	en_US
refterms.dateFOA	2023-11-03T09:31:47Z