Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes.

Autor:	Ngo HP; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Nguyen DQ; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Park H; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Park YS; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Kwak K; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Kim T; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Lee JH; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Cho KS; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea., Kang LW; Department of Biological Sciences, Konkuk University, Seoul 05029, Korea.
Jazyk:	angličtina
Zdroj:	BMB reports [BMB Rep] 2022 Sep; Vol. 55 (9), pp. 439-446.
Abstrakt:	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 Reports 2022; 55(9): 439-446].
Databáze:	MEDLINE
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