Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase

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DOIResolve DOI: http://doi.org/10.1002/pro.5560030312
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TypeArticle
Journal titleProtein Science
ISSN1469-896X
Volume3
Pages467475; # of pages: 9
AbstractUsing site-directed mutagenesis we have investigated the catalytic residues in a xylanase from Bacillus circulans. Analysis of the mutants E78D and E172D indicated that mutations in these conserved residues do not grossly alter the structure of the enzyme and that these residues participate in the catalytic mechanism. We have now determined the crystal structure of an enzyme-substrate complex to 108 A resolution using a catalytically incompetent mutant (E172C). In addition to the catalytic residues, Glu 78 and Glu 172, we have identified 2 tyrosine residues, Tyr 69 and Tyr 80, which likely function in substrate binding, and an arginine residue, Arg 112, which plays an important role in the active site of this enzyme. On the basis of our work we would propose that Glu 78 is the nucleophile and that Glu 172 is the acid-base catalyst in the reaction.
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LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Noteyes
Peer reviewedNo
NRC numberWAKARCHUK1994A
NPARC number9360575
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Record identifier7667d2dc-3cb5-4dda-af01-6215ad1bf968
Record created2009-07-10
Record modified2016-05-09
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