생화학분자생물학회입니다.
Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes: a brief review
작성자
Lin-Woo Kang작성일자
2022-11-15조회수
281Name: 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.