Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex.
FEBS Lett
; 591(9): 1212-1224, 2017 05.
Article
en En
| MEDLINE
| ID: mdl-28337759
ABSTRACT
In bacteria and plants, serine acetyltransferase (CysE) and O-acetylserine sulfhydrylase-A sulfhydrylase (CysK) collaborate to synthesize l-Cys from l-Ser. CysE and CysK bind one another with high affinity to form the cysteine synthase complex (CSC). We demonstrate that bacterial CysE is activated when bound to CysK. CysE activation results from the release of substrate inhibition, with the Ki for l-Ser increasing from 4 mm for free CysE to 16 mm for the CSC. Feedback inhibition of CysE by l-Cys is also relieved in the bacterial CSC. These findings suggest that the CysE active site is allosterically altered by CysK to alleviate substrate and feedback inhibition in the context of the CSC.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Cisteína
/
Cisteína Sintasa
/
Proteínas de Escherichia coli
/
Serina O-Acetiltransferasa
Idioma:
En
Revista:
FEBS Lett
Año:
2017
Tipo del documento:
Article
País de afiliación:
Italia