Disputation: Tamjidmaa Khatanbaatar

Doctoral candidate Tamjidmaa Khatanbaatar at the Department of chemistry, Faculty of Mathematics and Natural Sciences, is defending the thesis "Partners in crime – Structure-function studies on chorismate mutases and their associated enzymes" for the degree of Philosophiae Doctor.

Image may contain: A woman (Tamjidmaa) is looking straight at the camera and smiling. She is wearing a black sweater. She is standing against a grey background.

Tamjidmaa Khatanbaatar

The Disputation will be live streamed for everyone else.
The livestream will be activated 15 minutes before the Defence starts.

Trial lecture

April 14th, 10:15 AM, Auditorium 3, Chemistry building

Trial lecture title:

“The role of experimental structure determination in the times of accurate 3D prediction methods”

 

The trial lecture will be live streamed for everyone else.
The livestream will be activated 15 minutes before the trial lecture starts.

Kreeringssammendrag/Conferral summary 

Enzymer er molekylær maskiner som regulerer metabolismen til celler, inkludert metabolismen til bakterier som er farlige for mennesker. For å yte bedre, samhandler ofte enzymer med hverandre. I dette arbeidet har jeg funnet strukturen og interaksjonsmodusen til enzymer som er essensielle for overlevelsen til bakterier.

Main research findings

Aromatic amino acids are essential building blocks for proteins. Humans lack enzymes that produce aromatic amino acids, thus they must consume them with their diet. In contrast, plants, bacteria and fungi are capable of de novo synthesis of aromatic amino acids, including the essential amino acids phenylalanine and tryptophan. Enzymes involved in the biosynthesis of aromatic amino acids are very promising drug targets, to fight bacterial and fungal infections or plant parasitosis.

This PhD thesis is concerned with the study of chorismate mutase (CM), a fundamental metabolic enzyme. CM is often found associated to other enzymes from the same biosynthetic pathway, which regulate its activity. This work reports the structure of chorismate mutases from several bacteria, including human pathogens Mycobacterium tuberculosis and Pseudomonas aeruginosa, and novel bifunctional chorismate mutases from non-pathogenic bacteria. We shed light on their activity and regulation, including the mode of interaction with associated enzymes, laying the foundation for the discovery of new drugs.

Candidate contact information

 

LinkedIn: https://www.linkedin.com/in/tamjidmaa-khatanbaatar/

E-mail: Tamjidmaa.khatanbaatar@kjemi.uio.no

Published Mar. 28, 2023 1:02 PM - Last modified Mar. 28, 2023 1:02 PM