Ontology highlight
ABSTRACT:
SUBMITTER: de Cima S
PROVIDER: S-EPMC4655335 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
de Cima Sergio S Polo Luis M LM Díez-Fernández Carmen C Martínez Ana I AI Cervera Javier J Fita Ignacio I Rubio Vicente V
Scientific reports 20151123
Human carbamoyl phosphate synthetase (CPS1), a 1500-residue multidomain enzyme, catalyzes the first step of ammonia detoxification to urea requiring N-acetyl-L-glutamate (NAG) as essential activator to prevent ammonia/amino acids depletion. Here we present the crystal structures of CPS1 in the absence and in the presence of NAG, clarifying the on/off-switching of the urea cycle by NAG. By binding at the C-terminal domain of CPS1, NAG triggers long-range conformational changes affecting the two d ...[more]