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

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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.
Last updated: 4.11.2020