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5. Although 34 De Novo PYRIMIDINEBIOSYNTHESIS [4] the maximum velocity of carbamoyl-phosphate synthetase with ammonia is only 60% of that with glutamine, the affinity for ATP is much higher with ammonia. 4 mM at 10 mM glutamine and 10 mM HCO3-. 25 mM at 12 mM ATP and 10 mM HCO3-. All effectors act by altering the affinity of the enzyme for ATP. UMP decreases the affinity while ornithine, IMP, and phosphoribosyl-l-pyrophosphate increase it. The physiological significance of U M P as a negative effector and ornithine as a positive effector of activity is apparent.
Pardee,J. Biol. Chem, 237, 891 (1962). a j. C. Gerhart and H. K. Schachman,Biochemistry 4, 1054(1965). 4j. C. Gerhart and H. Holoubek,J. Biol. Chem. 242, 2886 (1967). 5 M. W. D. Thesis, Universityof California, Berkeley(1971). METHODS IN ENZYMOLOGY, VOL. LI Copyright ~) 1978 by Academic Press, lnc, All rights of reproduction in any form reserved, ISBN 0-12-181951-5 36 De Novo PYRIMIDINE BIOSYNTHESIS [5] was found to give higher yields of regulatory subunit and to reduce the time required for the separation.
Trotta, V. P. Wellner, L. M. Pinkus, and A. Meister, Proc. Natl. Acad. Sci. A. 70, 2717-2721 (1973). 29 p. p. Trotta, K. E. B. Platzer, R. H. Haschemeyer, and A. Meister, Proc. Natl. Acad. Sci. A. 71, 4607--4611 (1974). a0 A. T. H. Abdelal and J. L. Ingraham, J. Biol. Chem. 250, 4410--4417 (1975). [4] C a r b a m o y l - p h o s p h a t e Synthetase Salmonella (Glutamine): i B y J O H N L . INGRAHAM a n d A H M E D T . H . A B D E L A L HCO~ + 2 ATP + glutamine ~ K carbamoyl phosphate + glutamate + 2 ADP + phosphate In Salmonella typhimurium, a single species of carbamoyl-phosphate synthetase catalyzes the synthesis of all carbamoyl phosphate which serves two metabolic functions: it is an intermediate in the synthesis of 1See Volume 17A for earlier articles on glutamine-dependent carbamoyl-phosphate synthetase from Escherichia coli (22) and from Agaricus bisporus (23).