Characterization of a Phosphatidylserine Synthase of Vibrio parahaemolyticus.
Curr Microbiol
; 77(5): 710-715, 2020 May.
Article
en En
| MEDLINE
| ID: mdl-31897665
ABSTRACT
Phosphatidylserine synthase (Pss) is involved in the metabolic pathway in phospholipid synthesis in different organisms. In this study, Pss expression in Vibrio parahaemolyticus was verified through liquid chromatography tandem-mass spectrometry. To analyze the characteristics of Pss, the recombinant Pss was overexpressed and purified from Escherichia coli. The optimum temperature and pH of Pss were 40 °C and 8, respectively. When reacting with divalent metal, Pss activity decreased. In addition, Pss could not only use cytidine diphosphate diacylglycerol (CDP-DAG, 160), but also CDP-DAG (181) as a substrate to produce cytidine 5'-monophosphate. Furthermore, the 3D structure of Pss was predicted, and the results revealed that histidine and lysine of the two HKD motifs were present in the catalytic site. Moreover, CDP-DAG (160) was docked with the Pss model. To investigate whether the two HKD motifs in Pss are important to its activity, site-directed mutagenesis of histidine was performed. The results revealed that the activities of both H131A and H352A were diminished. Little is known regarding the catalytic site of type I Pss. This is the first report on the biochemical characterization of Pss in V. parahaemolyticus.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Contexto en salud:
3_ND
Problema de salud:
3_neglected_diseases
/
3_zoonosis
Asunto principal:
Proteínas Bacterianas
/
Vibrio parahaemolyticus
/
CDPdiacilglicerol-Serina O-Fosfatidiltransferasa
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Curr Microbiol
Año:
2020
Tipo del documento:
Article
País de afiliación:
Taiwán