Quantitative structural enzymological studies of rat peroxisomal multifunctional enzyme, type-1 (MFE1)
Thesis event information
Date and time of the thesis defence
Place of the thesis defence
Auditorium Leena Palotie (Aapistie 5A)
Topic of the dissertation
Quantitative structural enzymological studies of rat peroxisomal multifunctional enzyme, type-1 (MFE1)
Doctoral candidate
M.Sc. Shruthi Sridhar
Faculty and unit
University of Oulu Graduate School, Faculty of Biochemistry and Molecular Medicine, RW/RV
Subject of study
Structural enzymology
Opponent
Associate Professor Federico Forneris, University of Pavia
Custos
Emeritus Professor Rikkert K. Wierenga, University of Oulu
Quantitative structural enzymological studies of rat peroxisomal multifunctional enzyme, type-1 (MFE1)
The studies of this thesis have been aimed at the quantitative structural enzymological characterization of MFE1. The enzyme is derived from rat peroxisome which catalyses the fatty acid molecules. kinetics data show that they have different activitiy rates.
The structural studies reported here describe a new conformation in which both active sites have adopted an incompetent state. Another crystal structure with the long chain product bound to the enzyme could also be obtained. The substrate channeling properties of MFE1 is also observed. The other experiments suggest that the rate limiting step is related to the regeneration of the enzyme.
The structural studies reported here describe a new conformation in which both active sites have adopted an incompetent state. Another crystal structure with the long chain product bound to the enzyme could also be obtained. The substrate channeling properties of MFE1 is also observed. The other experiments suggest that the rate limiting step is related to the regeneration of the enzyme.
Last updated: 1.3.2023