Research

Suc2 octa webScientists from IQFR have revealed the structure of the Saccharomyces invertase, a highly interesting enzyme for Biotechnology and a classical model used in early biochemical studies. In the study have participated scientists from IATA (CSIC).
Invertases catalyze the hydrolysis of the disaccharide sucrose into glucose and fructose, being key enzymes in the metabolism of plants and microorganisms. Besides its historic relevance, Saccharomyces invertase is one of the most widely used enzymes in food industry, and in the fermentation of cane molasses into ethanol. A new emerging application is the synthesis of prebiotics (FOS) for use in functional foods and pharmaceuticals.

 

Reference: Journal of Biological Chemistry (2013) 288, 9755- 9766 (doi:10.1074/jbc.M112.446435)
Three-dimensional structure of Saccharomyces invertase. Role of a non-catalytic domain in oligomerization and substrate specificity. http://www.jbc.org/content/288/14/9755#fn-9
MA Sainz-Polo. M Ramírez, A Lafraya, B González, J Marín-Navarro, J Polaina, J Sanz-Aparicio.


Its structural analysis has shown a sophisticated molecular architecture with a peculiar monomer assembly, unique to this enzyme within its family, which regulates its specificity. This assemblage is similar to the interactions that form b-amiloids, and is mediated by the non-catalytic domain. Therefore, our results highlight the role of the non-catalytic domains in fine-tuning substrate specificity and supplement our knowledge into the structural features that rule modularity, a central feature within carbohydrate-active enzymes.

Press note.