Premium
Carbamate kinase can replace in vivo carbamoyl phosphate synthetase. Implications for the evolution of carbamoyl phosphate biosynthesis
Author(s) -
Alcántara Cristina,
Cervera Javier,
Rubio Vicente
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02168-2
Subject(s) - pyrococcus furiosus , carbamoyl phosphate synthetase , biochemistry , uracil , biosynthesis , phosphate , carbamyl phosphate , escherichia coli , adenylate kinase , chemistry , biology , enzyme , archaea , gene , dna
The exclusive involvement of carbamate kinase (CK) in fermentative ATP production and of carbamoyl phosphate synthetase (CPS) in the production of carbamoyl phosphate (CP) for pyrimidines and arginine biosynthesis was challenged by the finding of CK as the only activity synthesising CP in the archaea Pyrococcus furiosus and Pyrococcus abyssi . We now show that CK can replace CPS in vivo: transformation of Escherichia coli devoid of the CPS gene with plasmids encoding the CK from P. furiosus or from Enterococcus faecalis (which uses CK for making ATP) restores the ability of CPS‐deficient E. coli to grow in the absence of arginine and uracil if ammonia and bicarbonate are present.