Changing the substrate specificity of a chitooligosaccharide oxidase from Fusarium graminearum by model-inspired site-directed mutagenesis

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 mod...

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Bibliographic Details
Published in:FEBS letters 2007-10, Vol.581 (25), p.4905-4909
Main Authors: Heuts, Dominic P.H.M., Janssen, Dick B., Fraaije, Marco W.
Format: Article
Language:English
Subjects:
Acetylglucosamine - chemistry
Acetylglucosamine - metabolism
Alcohol Oxidoreductases - chemistry
Alcohol Oxidoreductases - genetics
Alcohol Oxidoreductases - metabolism
Amino Acid Sequence
Binding Sites
ChitO
chitooligosaccharide oxidase
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - metabolism
Fusarium - enzymology
Fusarium graminearum
GlcNac
horseradish peroxidase
HRP
Kinetics
maltose binding protein
MBP
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
N-Acetyl- d-glucosamine
Oligosaccharide
Oligosaccharides - metabolism
Oxidase
Sequence Alignment
Site-directed mutagenesis
Substrate Specificity
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Description
Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.09.019