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This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes
Ho-Phuong-Thuy Ngo1 (ph.D), Diem Quynh Nguyen1 (ph.D), Hyunjae Park1 (student), Yoon Sik Park1 (student), Kiwoong Kwak1 (student), Taejoon Kim1 (student), Jang Ho Lee1 (student), Kyoung Sang Cho1 (professor), Lin-Woo Kang 1,* (professor)
1Biological sciences, konkuk university
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.
Abstract, Accepted Manuscript(in press) [Submitted on May 25, 2022, Accepted on July 11, 2022]
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