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Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines
- Source :
- FEBS Letters, 594(17), 2819-2828. Wiley
- Publication Year :
- 2020
-
Abstract
- Chitooligosaccharide oxidase (ChitO) is a fungal carbohydrate oxidase containing a bicovalently bound FAD cofactor. The enzyme is known to catalyse the oxidation of chitooligosaccharides, oligomers of N-acetylated glucosamines derived from chitin degradation. In this study, the unique substrate acceptance was explored by testing a range of N-acetyl-D-glucosamine derivatives, revealing that ChitO preferentially accepts carbohydrates with a hydrophobic group attached to C2. The enzyme also accepts streptozotocin, a natural product used to treat tumours. Elucidation of the crystal structure provides an explanation for the high affinity towards C2-decorated glucosamines: the active site has a secondary binding pocket that accommodates groups attached at C2. Docking simulations are fully in line with the observed substrate preference. This work expands the knowledge on this versatile enzyme.
- Subjects :
- Models, Molecular
Protein Conformation, alpha-Helical
Gene Expression
Oligosaccharides
Chitin
Crystallography, X-Ray
Biochemistry
Substrate Specificity
chemistry.chemical_compound
Fusarium
Structural Biology
Glucosamine
Cloning, Molecular
chemistry.chemical_classification
0303 health sciences
Oxidase test
biology
Chemistry
030302 biochemistry & molecular biology
Recombinant Proteins
Flavin-Adenine Dinucleotide
Thermodynamics
Oxidoreductases
Protein Binding
chitooligosaccharides
crystal structure
covalent flavin
Stereochemistry
oxidation
Genetic Vectors
Biophysics
Cofactor
Fungal Proteins
03 medical and health sciences
Genetics
Escherichia coli
Protein Interaction Domains and Motifs
Molecular Biology
030304 developmental biology
Chitosan
Natural product
Binding Sites
Active site
Cell Biology
Carbohydrate
Kinetics
Enzyme
Docking (molecular)
biology.protein
glucosamine
Protein Conformation, beta-Strand
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 594
- Issue :
- 17
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....2dc9395e00151e46a6061d523fc70c7b