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

ABSTRACT: 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].

SUBMITTER: Ngo HP

PROVIDER: S-EPMC9537024 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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

Ngo Ho-Phuong-Thuy HP Nguyen Diem Quynh DQ Park Hyunjae H Park Yoon Sik YS Kwak Kiwoong K Kim Taejoon T Lee Jang Ho JH Cho Kyoung Sang KS Kang Lin-Woo LW

BMB reports 20220901 9

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 m ...[more]

PMID: 36104257

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