|
KMID : 0624620220550090439
|
|
BMB Reports
2022 Volume.55 No. 9 p.439 ~ p.446
|
|
|
Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes
|
|
Ngo Ho-Phuong-Thuy
Nguyen Diem Quynh
Park Hyun-Jae
Park Yoon-Sik
Kwak Ki-Woong
Kim Tae-Joon
Lee Jang-Ho
Cho Kyoung-Sang
Kang Lin-Woo
|
|
|
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.
|
|
|
KEYWORD
|
|
|
Conjugated π-bond system, Drug target, Organic cofactor, Pyridoxal 5’-phosphate (PLP), Transaldimination
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|