Substitution of a non-active-site residue located on the T3 loop increased the catalytic efficiency of endo -polygalacturonases
| Autor: | Rui Ma, Xia Pan, Huiying Luo, Bin Yao, Tu Tao, Wang Yuan, Kun Meng |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
010304 chemical physics biology Stereochemistry Active site Bioengineering Achaetomium biology.organism_classification 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Catalysis 03 medical and health sciences Residue (chemistry) chemistry.chemical_compound 030104 developmental biology chemistry 0103 physical sciences Hydrolase biology.protein Glycosyl Catalytic efficiency Site-directed mutagenesis |
| Zdroj: | Process Biochemistry. 51:1230-1238 |
| ISSN: | 1359-5113 |
| Popis: | Endo-polygalacturonases (PGs) of glycosyl hydrolase (GH) family 28 share a right handed parallel β-helical structure with a cleft formed by T1 and T3 loops. To reveal the effect of non-active-site residues on endo-PG catalysis, Thr113 of Achaetomium sp. endo-PG (PG8fn) located on the T3 loop was substituted. The experimental results indicated that the catalytic efficiency of PG8fn depends on the side-chain structure of residue at position 113, following the order of Glu (negatively charged) |
| Databáze: | OpenAIRE |
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