| Autor: |
Hiroaki Hamana, Yoshiaki Yasutake, Miyuki Kato-Murayama, Toshiaki Hosaka, Mikako Shirouzu, Shin-ichi Sakasegawa, Daisuke Sugimori, Kazutaka Murayama |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry. 87:74-81 |
| ISSN: |
1347-6947 |
| DOI: |
10.1093/bbb/zbac169 |
| Popis: |
Lysoplasmalogen-specific phospholipase D (LyPls-PLD) hydrolyzes choline lysoplasmalogen to choline and 1-(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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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