Heterologous expression and substrate specificity of ketoreductase domain in bacillaene polyketide synthase / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 1355-1362, 2015.
Article
Dans Chinois
| WPRIM
| ID: wpr-337485
ABSTRACT
The ketoreductase (KR) domain in the first extending module of the polyketide synthase (PKS) catalyzes the reductions of both an α-keto group and a β-keto group in the biosynthesis of bacillaene, suggesting the intrinsic substrate promiscuity. In order to further investigate the substrate specificity, the KR domain (BacKR1) was heterologously overexpressed in Escherichia coli. In vitro enzymatic analysis showed that only one of the four diastereomers was formed in the reduction of the racemic (±)-2-methyl-3-oxopentanoyl-N-acetylcysteamine thioester catalyzed by BacKR1. In addition, BacKR1 was revealed to catalyze the reductions of cyclohexanone and p-chloroacetophenone, indicating the potential of KR domians of PKSs as biocatalysts.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Spécificité du substrat
/
Protéines bactériennes
/
Catalyse
/
Oméga-Chloro-acétophénone
/
Structure tertiaire des protéines
/
Cyclohexanones
/
Polyketide synthases
/
Escherichia coli
/
Génétique
/
Métabolisme
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2015
Type:
Article
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