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Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes: a brief review

  • 작성자

    Lin-Woo Kang
  • 작성일자

    2022-11-15
  • 조회수

    186
Name: Lin-Woo Kang ( lkang@konkuk.ac.kr )
2015-present Professor, Department of Biological Sciences, KONKUK University
2010-2015 Associate professor, Department of Biological Sciences, KONKUK University
2006-2010 Assistant professor, Department of Advanced Technology Fusion, KONKUK University
2004-2006 Postdoctoral research fellow, Stanford University School of Medicine, USA
2000-2004 Ph.D., Department of Biochemistry and Biophysics, Johns Hopkins University School of Medicine, USA

Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes: a brief review

Pyridoxal 5’-phosphate (PLP)-dependent enzymes are ubiquitous, catalyzing various biochemical reactions of approximately 4% of all classified enzymatic activities. They transform amines and amino acids into important metabolites or signaling molecules and are important drug targets in many diseases. In the crystal structures of PLP-dependent enzymes, organic cofactor PLP showed diverse conformations depending on the catalytic step. The conformational change of PLP is essential in the catalytic mechanism. In the study, we review the sophisticated catalytic mechanism of PLP, especially in transaldimination reactions. Most drugs targeting PLP-dependent enzymes make a covalent bond to PLP with the transaldimination reaction. A detailed understanding of organic cofactor PLP will help develop a new drug against PLP-dependent enzymes.


BMB Rep. 2022 Sep;55(9):439-446. DOI: 10.5483/BMBRep.2022.55.9.090.

https://pubmed.ncbi.nlm.nih.gov/36104257/