Study of plant enzymes from metallopeptidase families M20 and M49
The general aim of the project was the characterization of metalloenzymes from two recently characterised metallopeptidase families: M20 (among them auxin conjugate hydrolase) and M49 (dipeptidyl peptidase III family). The project was divided into three major experimental parts. Part 1 was mainly dealing with the characterization of auxin conjugate hydrolases of the M20 metallopeptidase family where the effect of auxins on transcription, potential protein-protein interactions as well as structure-functuionm relationships by enzyme mutants were successfully analyzed. Part 2 dealt with the identification of novel M49 metallopeptidases in plants, especially in the moss Physcomitrella patens. Part 3 involved modeling of the different metallopeptidases by analyzing the influence of ligand binding on M49 ligand binding, the analysis of the role of zinc ions and ligand affinities.
Publications:
- Smolko, A., Šupljika, F., Martinčić, J., Jajčanin-Jozić, N., Grabar-Branilović, M., Tomić, S., Ludwig-Müller, J., Piantanida, I., Salopek-Sondi, B. (2016) The role of conserved Cys residues in Brassica rapa auxin amidohydrolase: Cys139 is crucial for the enzyme activity and Cys320 regulates enzyme stability. Phys. Chem. Chem. Phys. 18: 8890-8900
- Karačić, Z., Vukelić, B., Ho, G.H., Jozić, I., Sučec, I., Salopek-Sondi, B., Kozlović, M., Brenner, S.E., Ludwig-Müller, J., Abramić, M. (2017) A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III. Biological Chemistry 398: 101-112
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