The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer
✍ Scribed by Tjaard Pijning; Gertie van Pouderoyen; Leon Kluskens; John van der Oost; Bauke W. Dijkstra
- Book ID
- 113621633
- Publisher
- Elsevier Science
- Year
- 2009
- Tongue
- English
- Weight
- 623 KB
- Volume
- 583
- Category
- Article
- ISSN
- 0014-5793
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## Abstract Cellulases have been used in many applications to treat various carbohydrate‐containing materials. __Thermotoga maritima__ cellulase 12A (__Tm__Cel12A) belongs to the GH12 family of glycoside hydrolases. It is a β‐1,4‐endoglucanase that degrades cellulose molecules into smaller fragment
The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM).