Human carbamoyl phosphate synthetase I (CPSI): Insights on the structural role of the unknown function domains

• Type: Another Publication in an International Scientific Journal
• Date: 2012

Authors

Monica Lopes Marques (Author) Other; Gilberto Igrejas (Author) Other; Antonio Amorim (Author) FCUP; Luisa Azevedo (Author) FCUP

Journal

Title: Biochemical and Biophysical Research Communications

Vol. 421

Pages: 409-412

ISSN: 0006-291X

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 7 Citations

Scopus - 7 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-002-A3T

DOI: 10.1016/j.bbrc.2012.04.033

Abstract (EN): Carbamoyl phosphate synthetase (CPS) is an ancient protein. In mammals it intervenes in the urea cycle. This enzyme is organized into six domains, three of which have no established role in the mammalian enzyme. Taking advantage of the high degree of conservation between the human and the Escherichia coli homologue a comparative study was carried out in order to infer about the biological role of these less characterized domains. We show that among the residues involved in the maintenance of quaternary structure of the E. call enzyme, several are highly conserved between human and bacterial enzyme and match the homologous positions of the "unknown function" domains in human enzyme, suggesting they are involved in the structural stability of the human enzyme as they are in bacteria.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 4