- Licenciado in Biology, Facultad de Ciencias, Universidad de Chile, Santiago, 1982.
- Ph.D., Biology, Biochemistry Programme, Universidad de Chile, Santiago, 1990.
- Postdoctoral fellow, University of Missouri-Kansas City, Kansas City, MO, USA, 1990-1993.
Proteins within a cell are the macromolecules that carry out specific biological processes. Through proteins, cells can breakdown food substances to obtain energy, communicate and interact with the environment and replicate their genetic material. Protein engineering is a fascinating mixture of molecular biology, protein structure studies, computing and biochemistry. This interaction makes it possible to incorporate site-specific mutations into the genes of any protein, which in turn makes it possible to study the role of any amino acid or group of amino acids if the mutant protein can be produced in the appropriate expression system.
Our group has been interested in developing a line of advanced research on protein structure and function. As our study system, we have been using integral membrane proteins that behave as facilitative transporters. We are currently interested in the regulation of hexose transporter activity, by both natural and synthetic compounds. For this, we are using a variety of biochemical and biophysical methods, including reconstitution of purified proteins, site-directed mutagenesis, heterologous expression, fluorescence spectroscopy and bioinformatics. Likewise, we are interested in applying modern protein engineering strategies (directed evolution, drug design) to design enzymes of industrial interest.
- Godoy, A., Ormazabal, V., Moraga-Cid, G., Zúñiga, F.A., Sotomayor, P., Barra, V., Vasquez, O., Montecinos, M., Mardones, L., Guzmán, L., Villagrán, M., Aguayo, L.G., Oñate, S.A., Reyes, A.M., Cárcamo, J.G., Rivas, C.I. y Vera, J.C. (2007). Mechanistic insights and functional determinants of the transport cycle of the ascorbic acid transporter SVCT2. Activation by sodium and absolute dependence on bivalent cations. J. Biol. Chem. 282, 615-624.
- Rodríguez, P., Rivas, C.I., Godoy, A., Villanueva, M., Fischbarg, J., Vera, J.C. y Reyes, A.M. (2005). Redefining the Facilitated Transport of Mannose in Human Cells: Absence of a Glucose-Insensitive, High-Affinity Facilitated Mannose Transport System. Biochemistry 44, 313-320.
- Reyes, A.M., Ludwig, H.C., Yañez, A., Rodríguez, P.H. y Slebe, J.C. (2003). Native-like intermediate in the unfolding pathway of pig kidney fructose-1,6-bisphosphatase. Biochemistry 42, 6956-6964.
- Reyes, A.M., Bustamante, F., Rivas, C.I., Ortega, M., Donet, C., Rossi, J.P., Fischbarg, J. y Vera, J.C. (2002). Nicotinamide is not a substrate of the hexose transporter GLUT1. Biochemistry 41, 8075-8081.
- Vera, J.C., Reyes, A.M., Velásquez, F.V., Rivas, C.I., Zhang, R.H., Strobel, P., Slebe, J.C., Núñez-Alarcón, J. y Golde, D.W. (2001). Direct inhibition of the hexose transporter GLUT1 by tyrosine kinase inhibitors. Biochemistry 40, 777-790.
- Cárcamo, J.G., Yañez, A.J., Ludwig, H.C., León, O., Pinto, R.O., Reyes, A.M., y Slebe, J.C. (2000). The C1-C2 interface residue lysine 50 of pig kidney fructose-1,6-bisphosphatase has a crucial role in the cooperative signal transmission of the AMP inhibition. Eur. J. Biochem. 267, 2242-2251.