Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050781 | FEBS Letters | 2007 | 5 Pages |
Abstract
Chitooligosaccharide oxidase (ChitO) catalyzes the oxidation of C1 hydroxyl moieties on chitooligosaccharides and in this way displays a different substrate preference as compared to other known oligosaccharide oxidases. ChitO was identified in the genome of Fusarium graminearum and a structural model revealed that one active site residue (Q268) was likely to be involved in the recognition of the N-acetyl moiety on the chitooligosaccharide substrates. The substrate specificity of wild type ChitO and the Q268R mutant were examined and confirmed that Q268 is indeed involved in N-acetyl recognition.
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Authors
Dominic P.H.M. Heuts, Dick B. Janssen, Marco W. Fraaije,