In Lactobacillus plantarum, carbamoyl phosphate is synthesized by two carbamoyl-phosphate synthetases (CPS): Carbon dioxide differentiates the arginine-repressed from the pyrimidine-regulated CPS
H. Nicoloff et al., In Lactobacillus plantarum, carbamoyl phosphate is synthesized by two carbamoyl-phosphate synthetases (CPS): Carbon dioxide differentiates the arginine-repressed from the pyrimidine-regulated CPS, J BACT, 182(12), 2000, pp. 3416-3422
Carbamoyl phosphate (CP) is an intermediate in pyrimidine and arginine bios
ynthesis. Carbamoyl-phosphate synthetase (CPS) contains a small amidotransf
erase subunit (GLN) that hydrolyzes glutamine and transfers ammonia to the
large synthetase subunit (SYN), where CP biosynthesis occurs in the presenc
e of ATP and CO2. Lactobacillus plantarum, a lactic acid bacterium, harbors
a pyrimidine-inhibited CPS (CPS-P; Elagoz et al., Gene 182:37-43, 1996) an
d an arginine-repressed CPS (CPS-A). Sequencing has shown that CPS-A is enc
oded by carA (GLN) and carB (SYN). Transcriptional studies have demonstrate
d that carB is transcribed both monocistronically and in the carAB arginine
-repressed operon. CP biosynthesis in L. plantarum was studied with three m
utants (Delta CPS-P, Delta CPS-A, and double deletion). In the absence of b
oth CPSs, auxotrophy for pyrimidines and arginine was observed. CPS-P produ
ced enough CP for both pathways. In CO2-enriched air but not in ordinary ai
r, CPS-A provided CP only for arginine biosynthesis. Therefore, the uracil
sensitivity observed in prototrophic wild-type L. plantarum without CO2 enr
ichment may be due to the low affinity of CPS-A for its substrate CO2 or to
regulation of the CP pool by the cellular CO2/bicarbonate level.