The Glu residue in the conserved Asn-Glu-Pro sequence of two highly divergent endo-β-1,4-glucanases is essential for enzymatic activity

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DOIResolve DOI: http://doi.org/10.1016/0006-291X(90)91998-8
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TypeArticle
Journal titleBiochemical and Biophysical Research Communications
Volume169
Issue3
Pages10351039; # of pages: 5
AbstractWe initially aligned 28 different cellulase sequences in pairwise fashion and found half of them have the sequence -Asn-Glu-Pro- located in a region flanked by hydrophobic-rich amino acids. Based on lysozyme as a model, the glutamate residue could be essential for enzyme function. We tested this possibility by site-directed mutagenesis of the genes coding Bacillus polymyxa and Bacillus subtilis endo-β-1,4-glucanases. The genes and amino acid sequences of these two enzymes show very little similarity. Change of Glu-194 and Glu-169 to the isosteric glutamine form in these respective enzymes resulted in a dramatic loss of CMCase activity which could be restored by reverse mutation. Similar mutations to less-conserved residues, Glu-72 and Glu-147, of the B. subtilis enzyme did not cause any loss of activity.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedNo
NRC numberBAIRD1990
NPARC number9369401
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Record identifier3917428d-2e9f-474d-8c93-d90f23992014
Record created2009-07-10
Record modified2016-05-09
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