PMID: 6108501Jan 1, 1980Paper

The genes for and regulation of the enzyme activities of two multifunctional proteins required for the de novo pathway for UMP biosynthesis in mammals

Molecular Biology, Biochemistry, and Biophysics
M E Jones

Abstract

UMP biosynthesis requires six enzyme activities. Five of these enzyme centers are clustered into two multienzymatic proteins which are known to, or appear to, sequester the intermediates carbamyl approximately P, carbamyl aspartate and orotidylic acid. The advantages of sequestering these intermediates appear to be a conservation of energy, since two intermediates, carbamyl approximately P and orotidylate, might otherwise be rapidly degraded in mammalian cells. Carbamyl-aspartate appears not to be degraded rapidly in mammalian cells but it can pass into the blood and could possible disrupt brain metabolism by action as an acetylaspartate analog, if it passes the blood-brain barrier. For this, and possible for other reasons, there may be advantages to the fact that these intermediates are not other reasons, there may be advantages to the fact that these intermediates are not readily released from Complex A and U. In addition, these multienzymatic proteins may have other kinetic advantages, some of which have been discussed above. Studies with intact cells illustrate that azauridine, a chemical designed originally as an antineoplastic drug, produces a "ripple" effect when it inhibits the last enzyme of this pathway which leads to...Continue Reading

Citations

Apr 19, 2007·Journal of Basic Microbiology·Pooja RalliGerard O'Donovan
May 18, 2011·Journal of Aging Research·Claus DeslerLene Juel Rasmussen
Sep 24, 2004·The Journal of Biological Chemistry·Anupama AhujaDavid R Evans
Sep 24, 2010·Journal of Nucleic Acids·Claus DeslerLene Juel Rasmussen
Jul 26, 2014·Molecular Cancer Research : MCR·Arishya SharmaAlexandru Almasan

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