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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hwa, Kuo Yuan Subramani, Boopathi Shen, San-Tai Lee, Yu-May |
| Description | Author Affiliation: Hwa KY ( Department of Molecular Science and Engineering, National Taipei University of Technology, Taipei, Taiwan, ROC); Subramani B ( Department of Molecular Science and Engineering, National Taipei University of Technology, Taipei, Taiwan, ROC.); Shen ST ( Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, ROC.); Lee YM ( Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, ROC.) |
| Abstract | ß-Glycosidase from Thermococcus kodakarensis KOD1 is a hyperthermophilic enzyme with ß-glucosidase, ß-mannosidase, ß-fucosidase and ß-galactosidase activities. Sequence alignment with other ß-glycosidases from hyperthermophilic archaea showed two unique active site residues, Gln77 and Asp206. These residues were represented by Arg and Asp in all other hyperthermophilic ß-glycosidases. The two active site residues were mutated to Q77R, D206N and D206Q, to study the role of these unique active site residues in catalytic activity and to alter the substrate specificity to enhance its ß-glucosidase activity. The secondary structure analysis of all the mutants showed no change in their structure and exhibited in similar conformation like wild-type as they all existed in dimer form in an SDS-PAGE under non-reducing conditions. Q77R and D206Q affected the catalytic activity of the enzyme whereas the D206N altered the catalytic turn-over rate for glucosidase and mannosidase activities with fucosidase activity remain unchanged. Gln77 is reported to interact with catalytic nucleophile and Asp206 with axial C2-hydroxyl group of substrates. Q77R might have made some changes in three dimensional structure due to its electrostatic effect and lost its catalytic activity. The extended side chains of D206Q is predicted to affect the substrate binding during catalysis. The high-catalytic turn-over rate by D206N for ß-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures. |
| File Format | HTM / HTML |
| ISSN | 01410229 |
| Volume Number | 77 |
| e-ISSN | 18790909 |
| Journal | Enzyme and Microbial Technology |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-09-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Microbiology Discipline Biochemistry Discipline Biotechnology Archaeal Proteins Chemistry Metabolism Glycoside Hydrolases Thermococcus Enzymology Amino Acid Sequence Amino Acid Substitution Genetics Catalytic Domain Enzyme Activation Enzyme Stability Hot Temperature Kinetics Molecular Sequence Data Mutagenesis, Site-directed Protein Conformation Recombinant Proteins Sequence Homology, Amino Acid Substrate Specificity Thermodynamics Alpha-l-fucosidase Beta-galactosidase Beta-glucosidase Beta-mannosidase Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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