Ontology highlight
ABSTRACT:
SUBMITTER: Benoni R
PROVIDER: S-EPMC5957530 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Benoni Roberto R De Bei Omar O Paredi Gianluca G Hayes Christopher S CS Franko Nina N Mozzarelli Andrea A Bettati Stefano S Campanini Barbara B
FEBS letters 20170417 9
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 K<sub>i</sub> for l-Ser increasing from 4 mm for free CysE to 16 mm for the CSC. Feedback inhibition of Cy ...[more]