| Autor: |
Hiroaki Hamana, Yoshiaki Yasutake, Miyuki Kato-Murayama, Toshiaki Hosaka, Mikako Shirouzu, Shin-ichi Sakasegawa, Daisuke Sugimori, Kazutaka Murayama |
| Předmět: |
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| Zdroj: |
Bioscience, Biotechnology & Biochemistry; Jan2023, Vol. 87 Issue 1, p74-81, 8p |
| Abstrakt: |
Lysoplasmalogen-specific phospholipase D (LyPls-PLD) hydrolyzes choline lysoplasmalogen to choline and1- (1-alkenyl) - sn -glycero-3-phosphate. Mutation of F211 to leucine altered its substrate specificity from lysoplasmalogen to 1-O-hexadecyl-2-hydroxy- sn -glycero-3-phosphocholine (lysoPAF). Enzymes specific to lysoPAF have good potential for clinical application, and understanding the mechanism of their activity is important. The crystal structure of LyPls-PLD exhibited a TIM barrel fold assigned to glycerophosphocholine phosphodiesterase, a member of glycerophosphodiester phosphodiesterase. LyPls-PLD possesses a hydrophobic cleft for the binding of the aliphatic chain of the substrate. In the structure of the F211L mutant, Met232 and Tyr258 form a "small lid" structure that stabilizes the binding of the aliphatic chain of the substrate. In contrast, F211 may inhibit small lid formation in the wild-type structure. LysoPAF possesses a flexible aliphatic chain; therefore, a small lid is effective for stabilizing the substrate during catalytic reactions. [ABSTRACT FROM AUTHOR] |
| Databáze: |
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