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Journal articles on the topic 'Carbamoyl phosphate synthetase'

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Published: 4 June 2021

Last updated: 10 February 2022

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1

Schofield, J. P. "Molecular studies on an ancient gene encoding for carbamoyl-phosphate synthetase." Clinical Science 84, no. 2 (February 1, 1993): 119–28. http://dx.doi.org/10.1042/cs0840119.

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1. Carbamoyl-phosphate synthetase (EC 6.3.5.5.) catalyses the synthesis of carbamoyl phosphate, the immediate precursor of arginine and pyrimidine biosynthesis, and is highly conserved throughout evolution. The large subunit of all carbamoyl-phosphate synthetases sequenced to date comprises two highly homologous halves, the product of a proposed ancestral gene duplication. The sequences of the enzymes of Escherichia coli, Drosophila melanogaster, Saccharomyces cerevisiae, rat and Syrian hamster all have duplications, suggesting that this event occurred in the progenote predating the separation of the major phylae. Until now, only limited data on carbamoyl-phosphate synthetase were available for the primitive eukaryote Dictyostelium discoideum and for the Archaea Methanosarcina barkeri MS. The DNA sequence of the D. discoideum carbamoylphosphate gene and additional sequence for the carbamoyl-phosphate synthetase gene of M. barkeri MS have been determined, and a duplicated structure for both is clearly demonstrated. 2. Genes with ancient duplications provide unique information on their evolution. A study of the intron/exon organization of the rat carbamoylphosphate synthetase I gene and the carbamoylphosphate synthetase hamster II gene in the CAD multi-gene complex shows that at least some of their introns are very old. Evidence is provided that some introns must have been present in the ancestral precursor before its duplication. 3. The human carbamoyl-phosphate synthetase I gene has been isolated and characterized. A human liver cDNA library was constructed and probed for carbamoyl-phosphate synthetase I. A human genomic DNA cosmid library was also probed for the carbamoyl-phosphate synthetase I gene. The cDNA sequence of the human carbamoyl-phosphate synthetase I gene has been determined, and work has been initiated to confirm that at least part of this gene is contained within two cosmids spanning 46 kb. This will enable future studies to be made on mutations in this gene in the rare autosomal recessive deficiency of carbamoyl-phosphate synthetase I.

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2

Thoden, James B., Xinyi Huang, Frank M. Raushel, and Hazel M. Holden. "Carbamoyl-phosphate Synthetase." Journal of Biological Chemistry 277, no. 42 (July 18, 2002): 39722–27. http://dx.doi.org/10.1074/jbc.m206915200.

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3

Anderson, P. M. "Glutamine-dependent carbamoyl-phosphate synthetase and other enzyme activities related to the pyrimidine pathway in spleen of Squalus acanthias (spiny dogfish)." Biochemical Journal 261, no. 2 (July 15, 1989): 523–29. http://dx.doi.org/10.1042/bj2610523.

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The first two steps of urea synthesis in liver of marine elasmobranchs involve formation of glutamine from ammonia and of carbamoyl phosphate from glutamine, catalysed by glutamine synthetase and carbamoyl-phosphate synthetase, respectively [Anderson & Casey (1984) J. Biol. Chem. 259, 456-462]; both of these enzymes are localized exclusively in the mitochondrial matrix. The objective of this study was to establish the enzymology of carbamoyl phosphate formation and utilization for pyrimidine nucleotide biosynthesis in Squalus acanthias (spiny dogfish), a representative elasmobranch. Aspartate carbamoyltransferase could not be detected in liver of dogfish. Spleen extracts, however, had glutamine-dependent carbamoyl-phosphate synthetase, aspartate carbamoyltransferase, dihydro-orotase, and glutamine synthetase activities, all localized in the cytosol; dihydro-orotate dehydrogenase, orotate phosphoribosyltransferase, and orotidine-5′-decarboxylase activities were also present. Except for glutamine synthetase, the levels of all activities were very low. The carbamoyl-phosphate synthetase activity is inhibited by UTP and is activated by 5-phosphoribosyl 1-pyrophosphate. The first three enzyme activities of the pyrimidine pathway were eluted in distinctly different positions during gel filtration chromatography under a number of different conditions; although complete proteolysis of inter-domain regions of a multifunctional complex during extraction cannot be excluded, the evidence suggests that in dogfish, in contrast to mammalian species, these three enzymes of the pyrimidine pathway exist as individual polypeptide chains. These results: (1) establish that dogfish express two different glutamine-dependent carbamoyl-phosphate synthetase activities, (2) confirm the report [Smith, Ritter & Campbell (1987) J. Biol. Chem. 262, 198-202] that dogfish express two different glutamine synthetases, and (3) provide indirect evidence that glutamine may not be available in liver for biosynthetic reactions other than urea formation.

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4

Guy, Hedeel I., Anne Bouvier, and David R. Evans. "The Smallest Carbamoyl-phosphate Synthetase." Journal of Biological Chemistry 272, no. 46 (November 14, 1997): 29255–62. http://dx.doi.org/10.1074/jbc.272.46.29255.

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5

Husson, A., M. Bouazza, C. Buquet, and R. Vaillant. "Role of dexamethasone and insulin on the development of the five urea-cycle enzymes in cultured rat foetal hepatocytes." Biochemical Journal 225, no. 1 (January 1, 1985): 271–74. http://dx.doi.org/10.1042/bj2250271.

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The activity changes of the urea-cycle enzymes were monitored in cultured foetal hepatocytes after dexamethasone and insulin treatments. Addition of dexamethasone induced the development of carbamoyl-phosphate synthetase, argininosuccinate synthetase, argininosuccinase and arginase activities as soon as day 16.5 of gestation. When insulin was added together with dexamethasone, it markedly inhibited the steroid-induced increase in carbamoyl-phosphate synthetase, argininosuccinate synthetase and argininosuccinase activities.

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6

Braxton, B. L., Leisha S. Mullins, Frank M. Raushel, and Gregory D. Reinhart. "Allosteric Dominance in Carbamoyl Phosphate Synthetase†." Biochemistry 38, no. 5 (February 1999): 1394–401. http://dx.doi.org/10.1021/bi982097w.

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7

Nara, Takeshi, Ganghan Gao, Hiroshi Yamasaki, Junko Nakajima-Shimada, and Takashi Aoki. "Carbamoyl-phosphate synthetase II in kinetoplastids." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1387, no. 1-2 (September 1998): 462–68. http://dx.doi.org/10.1016/s0167-4838(98)00127-7.

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8

Martinez-Ramon, A., E. Knecht, V. Rubio, and S. Grisolia. "Levels of carbamoyl phosphate synthetase I in livers of young and old rats assessed by activity and immunoassays and by electron microscopic immunogold procedures." Journal of Histochemistry & Cytochemistry 38, no. 3 (March 1990): 371–76. http://dx.doi.org/10.1177/38.3.2303702.

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Carbamoyl phosphate synthetase I, the most abundant protein of rat liver mitochondria, plays a key role in synthesis of urea. Because aging affects some liver functions, and because there is no information on the levels of carbamoyl phosphate synthetase I during aging, we assayed the activity of this enzyme and determined immunologically the level of carbamoyl phosphate synthetase I in liver homogenates from young (4 months) and old (18 or 26 months) rats. In addition, we used electron microscopic immunogold procedures to locate and measure the amount of the enzyme in the mitochondrial matrix. There is no significant change in enzyme activity or enzyme protein content with age, although there is a higher concentration of the enzyme in the mitochondria (c. 1.5 times greater) from old rats, which is compensated by a decrease in the fractional volume of the mitochondrial compartment during aging.

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9

Yang, Xiaoyan, Jing Shi, Haihong Lei, Bin Xia, and Dezhi Mu. "Neonatal-onset carbamoyl phosphate synthetase I deficiency." Medicine 96, no. 26 (June 2017): e7365. http://dx.doi.org/10.1097/md.0000000000007365.

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10

Ahuja, Anupama, Cristina Purcarea, Hedeel I. Guy, and David R. Evans. "A Novel Carbamoyl-Phosphate Synthetase fromAquifex aeolicus." Journal of Biological Chemistry 276, no. 49 (September 26, 2001): 45694–703. http://dx.doi.org/10.1074/jbc.m106382200.

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11

Holden, Hazel M., James B. Thoden, and Frank M. Raushel. "Carbamoyl phosphate synthetase: a tunnel runs through it." Current Opinion in Structural Biology 8, no. 6 (December 1998): 679–85. http://dx.doi.org/10.1016/s0959-440x(98)80086-9.

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12

Kasahara, M., and M. Obmori. "Carbamoyl Phosphate Synthetase of the Cyanobacterium Anabaena cylindrica." Plant and Cell Physiology 38, no. 6 (January 1, 1997): 734–39. http://dx.doi.org/10.1093/oxfordjournals.pcp.a029227.

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13

Graves, Lee M., Hedeel I. Guy, Piotr Kozlowski, Min Huang, Eduardo Lazarowski, R. Marshall Pope, Matthew A. Collins, Erik N. Dahlstrand, H. Shelton Earp, and David R. Evans. "Regulation of carbamoyl phosphate synthetase by MAP kinase." Nature 403, no. 6767 (January 2000): 328–32. http://dx.doi.org/10.1038/35002111.

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14

Thoden, James B., Xinyi Huang, Jungwook Kim, Frank M. Raushel, and Hazel M. Holden. "Long-range allosteric transitions in carbamoyl phosphate synthetase." Protein Science 13, no. 9 (September 2004): 2398–405. http://dx.doi.org/10.1110/ps.04822704.

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15

Javid-Majd, Farah, Leisha S. Mullins, Frank M. Raushel, and Michelle A. Stapleton. "The Differentially Conserved Residues of Carbamoyl-Phosphate Synthetase." Journal of Biological Chemistry 275, no. 7 (February 18, 2000): 5073–80. http://dx.doi.org/10.1074/jbc.275.7.5073.

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16

Guy, Hedeel I., Bernard Schmidt, Guy Hervé, and David R. Evans. "Pressure-induced Dissociation of Carbamoyl-Phosphate Synthetase Domains." Journal of Biological Chemistry 273, no. 23 (June 5, 1998): 14172–78. http://dx.doi.org/10.1074/jbc.273.23.14172.

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17

Kothe, Michael, Cristina Purcarea, Hedeel I. Guy, David R. Evans, and Susan G. Powers-Lee. "Direct demonstration of carbamoyl phosphate formation on the C-terminal domain of carbamoyl phosphate synthetase." Protein Science 14, no. 1 (January 1, 2009): 37–44. http://dx.doi.org/10.1110/ps.041041305.

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18

Cohen, N. S., F. S. Kyan, S. S. Kyan, C. W. Cheung, and L. Raijman. "The apparent Km of ammonia for carbamoyl phosphate synthetase (ammonia) in situ." Biochemical Journal 229, no. 1 (July 1, 1985): 205–11. http://dx.doi.org/10.1042/bj2290205.

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Experiments with carbamoyl phosphate synthetase (ammonia) in solution and in isolated mitochondria are reported which show the following. NH3 rather than NH4+ is the substrate of the enzyme. The apparent Km of NH3 for the purified enzyme is about 38 microM. The apparent Km for NH3 measured in intact isolated mitochondria is about 13 microM. This value was obtained for both coupled and uncoupled mitochondria and was unchanged when the rate of carbamoyl phosphate synthesis was increased 2-fold by incubating uncoupled mitochondria in the presence of 5 mM-N-acetylglutamate. According to the literature, the concentration of NH3 in liver is well below the measured apparent Km. On the basis of this and previous work we conclude that, quantitatively, changes in liver [NH3] and [ornithine] are likely to be the most important factors in the fast regulation of synthesis of carbamoyl phosphate and urea. This conclusion is consistent with all available evidence obtained with isolated mitochondria, isolated hepatocytes, perfused liver and whole animals.

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19

Gaasbeek Janzen, J. W., A. F. Moorman, W. H. Lamers, and R. Charles. "Development of the heterogeneous distribution of carbamoyl-phosphate synthetase (ammonia) in rat-liver parenchyma during postnatal development." Journal of Histochemistry & Cytochemistry 33, no. 12 (December 1985): 1205–11. http://dx.doi.org/10.1177/33.12.4067274.

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Carbamoyl-phosphate synthetase (ammonia) is homogeneously distributed in rat-liver parenchyma at birth, as demonstrated by immunohistochemistry. A heterogeneous distribution can first be demonstrated at 6 days post partum, but can be masked by use of a too sensitive detection system. This heterogeneity is established by a decrease in enzyme content around the hepatic venules and a considerable increase in enzyme content in the remaining parenchyma. The perivenous decrease in enzyme content does not occur in all hepatocytes synchronously. The adult type of heterogeneity is characterized by a perivenous layer, only two to three cells thick, in which carbamoyl-phosphate synthetase can no longer be detected, irrespective of the sensitivity of the assay used. This situation is fully established at the age of two months.

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20

Hewagama, Anura, Hedeel I. Guy, John F. Vickrey, and David R. Evans. "Functional Linkage between the Glutaminase and Synthetase Domains of Carbamoyl-phosphate Synthetase." Journal of Biological Chemistry 274, no. 40 (October 1, 1999): 28240–45. http://dx.doi.org/10.1074/jbc.274.40.28240.

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21

Smith, D. D., and J. W. Campbell. "Distribution of glutamine synthetase and carbamoyl-phosphate synthetase I in vertebrate liver." Proceedings of the National Academy of Sciences 85, no. 1 (January 1, 1988): 160–64. http://dx.doi.org/10.1073/pnas.85.1.160.

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22

Guillou, F., S. D. Rubino, R. S. Markovitz, D. M. Kinney, and C. J. Lusty. "Escherichia coli carbamoyl-phosphate synthetase: domains of glutaminase and synthetase subunit interaction." Proceedings of the National Academy of Sciences 86, no. 21 (November 1, 1989): 8304–8. http://dx.doi.org/10.1073/pnas.86.21.8304.

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23

Cohen, N. S., C. W. Cheung, and L. Raijman. "Altered enzyme activities and citrulline synthesis in liver mitochondria from ornithine carbamoyltransferase-deficient sparse-furash mice." Biochemical Journal 257, no. 1 (January 1, 1989): 251–57. http://dx.doi.org/10.1042/bj2570251.

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Male mice carrying the spfash mutation have 5-10% of the normal activity of ornithine carbamoyltransferase, yet are only slightly hyperammonaemic and develop quite well. A study of liver mitochondria from normal and spfash males showed that they differ in important ways. (1) The spfash liver contains about 33% more mitochondrial protein per g than does normal liver. (2) The specific activities of carbamoyl-phosphate synthetase (ammonia) and glutamate dehydrogenase are about 15% lower than normal in mitochondria from spfash mice, whereas those of beta-hydroxybutyrate dehydrogenase and cytochrome oxidase are 22% higher and 30% lower respectively. (3) In the presence of 10 mM-ornithine and the substrates for carbamoyl phosphate synthesis, coupled and uncoupled mitochondria from spfash mice synthesize citrulline at unexpectedly high rates, about 25 and 44 nmol/min per mg respectively. Though these are somewhat lower than the corresponding rates obtained with normal mitochondria, the difference does not arise from the deficiency in ornithine carbamoyltransferase, but from the lower carbamoyl-phosphate synthetase activity of the mutant mitochondria. (4) At lower external [ornithine] (less than 2 mM), a smaller fraction of the carbamoyl phosphate synthesized is converted into citrulline in spfash than in normal mitochondria. These studies show that what appears to be a single mutation brings about major adaptations in the mitochondrial component of liver. In addition, they clarify the role of ornithine transport and of protein-protein interactions in citrulline synthesis in normal mitochondria.

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24

Powers-Lee, S. G., and K. Corina. "Domain structure of rat liver carbamoyl phosphate synthetase I." Journal of Biological Chemistry 261, no. 33 (November 1986): 15349–52. http://dx.doi.org/10.1016/s0021-9258(18)66714-6.

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25

Sahay, Nisha, Hedeel I. Guy, Xin Liu, and David R. Evans. "Regulation of anEscherichia coli/Mammalian Chimeric Carbamoyl-phosphate Synthetase." Journal of Biological Chemistry 273, no. 47 (November 20, 1998): 31195–202. http://dx.doi.org/10.1074/jbc.273.47.31195.

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26

Kim, Jungwook, and Frank M. Raushel. "Access to the carbamate tunnel of carbamoyl phosphate synthetase." Archives of Biochemistry and Biophysics 425, no. 1 (May 2004): 33–41. http://dx.doi.org/10.1016/j.abb.2004.02.031.

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27

Marrero, Mario, Russell A. Prough, Robert S. Putnam, Michael Bennett, and Leon Milewich. "Inhibition of carbamoyl phosphate synthetase-I by dietary dehydroepiandrosterone." Journal of Steroid Biochemistry and Molecular Biology 38, no. 5 (May 1991): 599–609. http://dx.doi.org/10.1016/0960-0760(91)90319-z.

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28

Alcántara, Cristina, Javier Cervera, and Vicente Rubio. "Carbamate kinase can replace in vivo carbamoyl phosphate synthetase. Implications for the evolution of carbamoyl phosphate biosynthesis." FEBS Letters 484, no. 3 (November 8, 2000): 261–64. http://dx.doi.org/10.1016/s0014-5793(00)02168-2.

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29

Nicoloff, Hervé, Jean-Claude Hubert, and Françoise Bringel. "In Lactobacillus plantarum, Carbamoyl Phosphate Is Synthesized by Two Carbamoyl-Phosphate Synthetases (CPS): Carbon Dioxide Differentiates the Arginine-Repressed from the Pyrimidine-Regulated CPS." Journal of Bacteriology 182, no. 12 (June 15, 2000): 3416–22. http://dx.doi.org/10.1128/jb.182.12.3416-3422.2000.

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ABSTRACT Carbamoyl phosphate (CP) is an intermediate in pyrimidine and arginine biosynthesis. Carbamoyl-phosphate synthetase (CPS) contains a small amidotransferase subunit (GLN) that hydrolyzes glutamine and transfers ammonia to the large synthetase subunit (SYN), where CP biosynthesis occurs in the presence of ATP and CO2.Lactobacillus plantarum, a lactic acid bacterium, harbors a pyrimidine-inhibited CPS (CPS-P; Elagöz et al., Gene 182:37–43, 1996) and an arginine-repressed CPS (CPS-A). Sequencing has shown that CPS-A is encoded by carA (GLN) and carB (SYN). Transcriptional studies have demonstrated that carB is transcribed both monocistronically and in the carABarginine-repressed operon. CP biosynthesis in L. plantarumwas studied with three mutants (ΔCPS-P, ΔCPS-A, and double deletion). In the absence of both CPSs, auxotrophy for pyrimidines and arginine was observed. CPS-P produced enough CP for both pathways. In CO2-enriched air but not in ordinary air, CPS-A provided CP only for arginine biosynthesis. Therefore, the uracil sensitivity observed in prototrophic wild-type L. plantarum without CO2 enrichment 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.

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30

Thoden, James B., Sophie G. Miran, James C. Phillips, Andrew J. Howard, Frank M. Raushel, and Hazel M. Holden. "Carbamoyl Phosphate Synthetase: Caught in the Act of Glutamine Hydrolysis†,‡." Biochemistry 37, no. 25 (June 1998): 8825–31. http://dx.doi.org/10.1021/bi9807761.

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31

Miles, Bryant W., Jennifer A. Banzon, and Frank M. Raushel. "Regulatory Control of the Amidotransferase Domain of Carbamoyl Phosphate Synthetase†." Biochemistry 37, no. 47 (November 1998): 16773–79. http://dx.doi.org/10.1021/bi982018g.

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32

Raushel, Frank M., James B. Thoden, Gregory D. Reinhart, and Hazel M. Holden. "Carbamoyl phosphate synthetase: a crooked path from substrates to products." Current Opinion in Chemical Biology 2, no. 5 (January 1998): 624–32. http://dx.doi.org/10.1016/s1367-5931(98)80094-x.

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33

Miles, Bryant W., and Frank M. Raushel. "Synchronization of the Three Reaction Centers within Carbamoyl Phosphate Synthetase†." Biochemistry 39, no. 17 (May 2000): 5051–56. http://dx.doi.org/10.1021/bi992772h.

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34

Braxton, B. L., Leisha S. Mullins, Frank M. Raushel, and Gregory D. Reinhart. "Allosteric Effects of Carbamoyl Phosphate Synthetase fromEscherichia coliAre Entropy-Driven†." Biochemistry 35, no. 36 (January 1996): 11918–24. http://dx.doi.org/10.1021/bi961305m.

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35

Kasahara, Mureo, Seisuke Sakamoto, Takanobu Shigeta, Akinari Fukuda, Rika Kosaki, Atsuko Nakazawa, Shinji Uemoto, Masahiro Noda, Yasuhiro Naiki, and Reiko Horikawa. "Living-donor liver transplantation for carbamoyl phosphate synthetase 1 deficiency." Pediatric Transplantation 14, no. 8 (September 23, 2010): 1036–40. http://dx.doi.org/10.1111/j.1399-3046.2010.01402.x.

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36

Nunley, S., and D. Ghosh. "Teaching NeuroImages: MRI findings in carbamoyl phosphate synthetase 1 deficiency." Neurology 84, no. 18 (May 4, 2015): e138-e139. http://dx.doi.org/10.1212/wnl.0000000000001546.

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37

Kim, Jungwook, Stanley Howell, Xinyi Huang, and Frank M. Raushel. "Structural Defects within the Carbamate Tunnel of Carbamoyl Phosphate Synthetase†." Biochemistry 41, no. 42 (October 2002): 12575–81. http://dx.doi.org/10.1021/bi020421o.

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38

Huang, Min, Piotr Kozlowski, Matthew Collins, Yanhong Wang, Timothy A. Haystead, and Lee M. Graves. "Caspase-Dependent Cleavage of Carbamoyl Phosphate Synthetase II during Apoptosis." Molecular Pharmacology 61, no. 3 (March 1, 2002): 569–77. http://dx.doi.org/10.1124/mol.61.3.569.

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39

Summar, Marshall L., James V. Gainer, Mias Pretorius, Hector Malave, Stephanie Harris, Lynn D. Hall, Alec Weisberg, Douglas E. Vaughan, Brian W. Christman, and Nancy J. Brown. "Relationship Between Carbamoyl-Phosphate Synthetase Genotype and Systemic Vascular Function." Hypertension 43, no. 2 (February 2004): 186–91. http://dx.doi.org/10.1161/01.hyp.0000112424.06921.52.

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40

Zhang, Guoqing, Yulin Chen, Huiqun Ju, Fei Bei, Jing Li, Jian Wang, Jianhua Sun, and Jun Bu. "Carbamoyl phosphate synthetase 1 deficiency diagnosed by whole exome sequencing." Journal of Clinical Laboratory Analysis 32, no. 2 (April 26, 2017): e22241. http://dx.doi.org/10.1002/jcla.22241.

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41

Flores, Maria Vega C., and Thomas S. Stewart. "Plasmodium falciparum: A Microassay for the Malarial Carbamoyl Phosphate Synthetase." Experimental Parasitology 88, no. 3 (March 1998): 243–45. http://dx.doi.org/10.1006/expr.1998.4240.

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42

Kothe, M. "Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetase." Protein Science 13, no. 2 (February 1, 2004): 466–75. http://dx.doi.org/10.1110/ps.03416804.

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43

Cardona, Diana M., Xiaokui Zhang, and Chen Liu. "Loss of Carbamoyl Phosphate Synthetase I in Small-Intestinal Adenocarcinoma." American Journal of Clinical Pathology 132, no. 6 (December 2009): 877–82. http://dx.doi.org/10.1309/ajcp74xgrfwtflju.

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44

Flores, Maria Vega C., William J. O'Sullivan, and Thomas S. Stewart. "Characterisation of the carbamoyl phosphate synthetase gene from Plasmodium falciparum." Molecular and Biochemical Parasitology 68, no. 2 (December 1994): 315–18. http://dx.doi.org/10.1016/0166-6851(94)90176-7.

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45

Stapleton, Michelle A., Farah Javid-Majd, Marilyn F. Harmon, Brent A. Hanks, Jennifer L. Grahmann, Leisha S. Mullins, and Frank M. Raushel. "Role of Conserved Residues within the Carboxy Phosphate Domain of Carbamoyl Phosphate Synthetase†." Biochemistry 35, no. 45 (January 1996): 14352–61. http://dx.doi.org/10.1021/bi961183y.

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46

Krátký, Martin, Eva Novotná, Shalini Saxena, Perumal Yogeeswari, Dharmarajan Sriram, Markéta Švarcová, and Jarmila Vinšová. "Salicylanilide Diethyl Phosphates as Potential Inhibitors of Some Mycobacterial Enzymes." Scientific World Journal 2014 (2014): 1–6. http://dx.doi.org/10.1155/2014/703053.

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Antimycobacterially active salicylanilide diethyl phosphates were evaluated to identify their potential drug target(s) for the inhibition of several mycobacterial enzymes, including isocitrate lyase, L-alanine dehydrogenase (MtAlaDH), lysineε-aminotransferase, chorismate mutase, and pantothenate synthetase. The enzymes are related to the nongrowing state ofMycobacterium tuberculosis. Salicylanilide diethyl phosphates represent new candidates with significant inhibitory activity especially against L-alanine dehydrogenase. The most activeMtAlaDH inhibitor, 5-chloro-2-[(3-chlorophenyl)carbamoyl]phenyl diethyl phosphate, has an IC50of 4.96 µM and the best docking results. Other mycobacterial enzymes were mostly inhibited by some derivatives but at higher concentrations; isocitrate lyase showed the highest resistance to salicylanilide diethyl phosphates.

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47

Elgar, Greg, and J. Paul Schofield. "Carbamoyl phosphate synthetase (CPSase) in the PYR1-3 multigene ofDictyostelium discoideum." DNA Sequence 2, no. 4 (January 1992): 219–26. http://dx.doi.org/10.3109/10425179209020806.

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48

Wong, Lee-Jun C. "Postpartum Coma and Death due to Carbamoyl-Phosphate Synthetase I Deficiency." Annals of Internal Medicine 120, no. 3 (February 1, 1994): 216. http://dx.doi.org/10.7326/0003-4819-120-3-199402010-00007.

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Madan, A. "Carbamoyl Phosphate Synthetase Polymorphisms as a Risk Factor for Necrotizing Enterocolitis." Yearbook of Neonatal and Perinatal Medicine 2008 (January 2008): 220–21. http://dx.doi.org/10.1016/s8756-5005(08)79165-0.

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Martínez, Ana Isabel, Isabel Pérez-Arellano, Satu Pekkala, Belén Barcelona, and Javier Cervera. "Genetic, structural and biochemical basis of carbamoyl phosphate synthetase 1 deficiency." Molecular Genetics and Metabolism 101, no. 4 (December 2010): 311–23. http://dx.doi.org/10.1016/j.ymgme.2010.08.002.

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