Expanding the Catalytic Promiscuity of Heparinase III fromPedobacter heparinus
| Autor: | Meiling Lu, Xuri Wu, Yijun Chen, Zongqiang Wang, Yayun Gu |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Stereochemistry Mutant Pedobacter heparinus medicine.disease_cause Catalysis Substrate Specificity Glycosaminoglycan 03 medical and health sciences chemistry.chemical_compound Residue (chemistry) medicine Phosphofructokinase 2 Disulfides Glycosaminoglycans Polysaccharide-Lyases 030102 biochemistry & molecular biology Organic Chemistry General Chemistry Heparan sulfate Protein Structure Tertiary Kinetics 030104 developmental biology chemistry Biochemistry Biocatalysis Mutagenesis Site-Directed Heparitin Sulfate Dimerization Pedobacter Cysteine |
| Zdroj: | Chemistry - A European Journal. 23:2548-2551 |
| ISSN: | 0947-6539 |
| DOI: | 10.1002/chem.201605929 |
| Popis: | Glycosaminoglycans (GAG) lyases are useful biocatalysts for the preparation of oligosaccharides, but their substrate spectra are limited to the same family. Thus, the degradation activity across families of GAG lyases is advantageous and desirable for various applications. In this study, residue Lys130 at the substrate entrance of monomeric heparinase III from Pedobacter heparinus ATCC 13125 was replaced by cysteine, and the resulting mutant K130C showed novel catalytic activity in degrading hyaluronic acid without affecting its native activity toward heparin and heparan sulfate. The broadened catalytic promiscuity by mutant K130C was the result of dimerization through a disulfide bond to expand the substrate binding pocket. This bifunctional enzyme is potentially valuable in the degradation of different types of GAGs. |
| Databáze: | OpenAIRE |
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