- 건국대학교

	KU Research Team Proposes New Evidence for the Evolution of Enzymes
	관리자		1308		2014.03.26

Prof. Lin-Woo Kang and Prof. Ho-Phuong-Thuy Ngo's research team at the Dept. of Biological Sciences, College of Bioscience and Biotechnology, Konkuk University (KU); Prof. Maria João Ramos; and other researchers have paved the way for new drug development at the core of treatment for Parkinson's disease and epilepsy. The researchers investigated the structure and function of the pyridoxal 5'-phosphate (PLP)-dependent enzyme by X-ray crystallography and quantum mechanical calculations. PLP is the active form of vitamin B6 in cells.
The research outcomes were published in Acta Crystallographica Section D: Biological Crystallography (Feb. 2014; Vol. 70, Issue 2), a peer-reviewed journal of the International Union of Crystallography which covers structural biology. Most enzymes in the human body are composed of proteins, and coenzymes are known to assist with catalysis in certain enzymes by combining with them. The study is the first report that the organic cofactor itself performs catalytic reactions involving active conformational changes like most protein enzymes.
* Title of Article: "PLP undergoes conformational changes during the course of an enzymatic reaction"
In particular, Prof. Kang's research team crystallized five different three-dimensional structures of PLP-dependent enzyme cystathionine gamma-lyase. Among these five structures, the PLP cofactor has been found to perform the core function of enzyme catalysis.
According to the RNA world hypothesis, catalytic RNA molecules are considered the origin of life, and protein enzymes are believed to have evolved from them. Most organic cofactors are derivatives of RNA molecules and the direct catalytic mechanism by organic cofactor PLP in protein could be strong supportive evidence that catalytic RNAs (Ribozyme) evolved into protein enzymes. In addition, PLP-dependent enzymes are important targets for the treatment of Parkinson's disease and epilepsy; thus, the catalytic mechanism is expected to be useful for drug development.
Prof. Kang commented, "The newly proposed mechanism has set the foundation for expanding prior research on enzyme mechanism, which was limited to proteins, to one that deals with cofactors and nucleic acid derivatives."
This study was funded by the Rural Development Administration of Korea and the Korea Institute of Ocean Science & Technology.
For more information, please visit: <a href="http://journals.iucr.org/d/issues/2014/02/00/issconts.html">http://journals.iucr.org/d/issues/2014/02/00/issconts.html</a>
 
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Posted by Eun Jin Cho

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