- Chemist, Licenciada in Chemistry, Universidad Católica de Chile, Chile, 1976;
- Masters Degree in Exact Sciences, Chemistry, Universidad Católica de Chile, 1978;
- Dr. rer. nat., Biochemistry, Technische Universität München, Munich, Germany, 1983;
- Postdoctorate, Max Planck Institut für Biochemie, Germany, 1984.
My research centres on studying the regulation of carbohydrate metabolism, in particular the gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), from pig kidney. FBPase is a tetrameric allosteric enzyme that responds to a series of metabolic signals. In recent years, I have been particularly interested in the folding and unfolding mechanism of this enzyme, the study of its regulatory characteristics, as well as its interaction with other gluconeogenic enzymes such as aldolase isoenzyme B. The use of FBPase mutants in which certain phenylalanine residues have been replaced by tryptophan, has been an efficient tool, as the fluorescent tryptophan residues allow the detection of local conformational changes occurring in the protein on ligand-binding and during the course of the unfolding process. Through these studies, I hope to advance our molecular understanding of the mechanisms that regulate the function of this regulatory enzyme, that is, the processes that govern the folding and specific association of its subunits, as well as the interaction of the enzyme with other proteins.
- Ludwig, H.C., Pardo, F.N., Asenjo, J.L., Maureira, M.A., Yañez, A.J. y Slebe, J.C. (2007). Unraveling multistate unfolding of pig kidney fructose-1,6-bisphosphatase using single tryptophan mutants. FEBS J. en prensa.
- Yañez, A.J., Ludwig, H.C., Bertinat, R., Spichiger, C., Gatica, R., Berlien, G., León, O., Brito, M., Concha, I.I. y Slebe, J.C. (2005). Different involvement for aldolase isoenzymes in kidney glucose metabolism. Aldolase B but not aldolase A colocalizes and forms a complex with FBPase. J. Cell. Physiol. 202, 743-753.
- Reyes, A. M., Ludwig, H.C., Yañez, A.J., Rodriguez, P.H. y Slebe, J.C. (2003). Nativelike intermediate on the unfolding pathway of pig kidney fructose-1,6-bisphosphatase. Biochemistry 42, 6956-6964
- 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.
- Ludwig, H.C., Herrera, R., Reyes, A.M., Hubert, E. y Slebe, J.C. (1999). Suppression of kinetic AMP cooperativity of fructose-1,6-bisphosphatase by carbamoylation of lysine residues. J. Prot. Chem. 18, 533-545