Chile
| Artículos de revistas
ADP-dependent phosphofructokinases from the archaeal order Methanosarcinales display redundant glucokinase activity
Fecha
2017Registro en:
Archives of Biochemistry and Biophysics, Volumen 633,
10960384
00039861
10.1016/j.abb.2017.09.008
Autor
Zamora, Ricardo A.
González Órdenes, Felipe
Castro Fernández, Víctor
Guixé Leguía, Victoria Cristina
Institución
Resumen
© 2017 Elsevier Inc. The genome of Methanosarcinales organisms presents both ADP-dependent glucokinase and phosphofructokinase genes. However, Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminal, where the catalytic GXGD motif is located. Characterization of its phosphofructokinase annotated protein shows that is a bifunctional enzyme able to supply the absence of the glucokinase activity. Moreover, kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrated that this enzyme is also bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as was previously reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. The presence of active glycolytic enzymes would be important when glycogen storage of these organisms