α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities

Laëtitia Bruel , Gerlind Sulzenbacher (1) , Marine Cervera Tison , Ange Pujol (2) , Cendrine Nicoletti (2) , Josette Perrier (2) , Anne Galinier (3) , David Ropartz (4) , Michel Fons , Frederique Pompeo (5) , Thierry Giardina

1 AFMB - Architecture et fonction des macromolécules biologiques
2 ISM2 - Institut des Sciences Moléculaires de Marseille
3 NPTME - Neurobiologie, plasticité tissulaire et métabolisme énergétique
4 BIA - Unité de recherche sur les Biopolymères, Interactions Assemblages
5 LCB - Laboratoire de chimie bactérienne

Background: Raffinose, an abundant carbohydrate in plants, is degraded into galactose and sucrose by intestinal microbial enzymes. Results: AgaSK is a protein coupling galactosidase and sucrose kinase activity. The structure of the galactosidase domain sheds light onto substrate recognition. Conclusion: AgaSK produces sucrose-6-phosphate directly from raffinose. Significance: Production of sucrose-6-phosphate directly from raffinose points toward a novel glycolytic pathway in bacteria.

Mots clés: microbial enzymes; sucrose; kinase activity; biochemistry and molecular biology

Mots clés: α-Galactosides; galactose

Domaines: Biochimie [q-bio.BM]

Laëtitia Bruel, Gerlind Sulzenbacher, Marine Cervera Tison, Ange Pujol, Cendrine Nicoletti, et al.. α-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities. Journal of Biological Chemistry, 2011, 286 (47), pp.40814 - 40823. ⟨10.1074/jbc.M111.286039⟩. ⟨hal-01793279⟩