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Carbamoyl phosphate synthase II
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<h2 id="see-also">See also</h2> <ul><li><a href="/facts/Carbamoyl_phosphate_synthetase_I/VsVsvp2s">Carbamoyl phosphate synthetase I</a></li> <li>Carbamoyl phosphate synthetase III</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=Carbamoyl-Phosphate+Synthase+%28Glutamine-Hydrolyzing%29">Carbamoyl-Phosphate+Synthase+(Glutamine-Hydrolyzing)</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Anderson PM, Meister A (December 1965). "Evidence for an activated form of carbon dioxide in the reaction catalyzed by Escherichia coli carbamyl phosphate synthetase". Biochemistry. 4 (12): 2803–9. doi:10.1021/bi00888a034. PMID 5326356. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Kalman SM, Duffield PH, Brzozowski T (April 1966). "Purification and properties of a bacterial carbamyl phosphate synthetase". The Journal of Biological Chemistry. 241 (8): 1871–7. doi:10.1016/S0021-9258(18)96716-5. PMID 5329589. <a href="https://doi.org/10.1016%2FS0021-9258%2818%2996716-5" target="_blank">https://doi.org/10.1016%2FS0021-9258%2818%2996716-5</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Yip MC, Knox WE (May 1970). "Glutamine-dependent carbamyl phosphate synthetase. Properties and distribution in normal and neoplastic rat tissues". The Journal of Biological Chemistry. 245 (9): 2199–204. doi:10.1016/S0021-9258(18)63139-4. PMID 5442268. <a href="https://doi.org/10.1016%2FS0021-9258%2818%2963139-4" target="_blank">https://doi.org/10.1016%2FS0021-9258%2818%2963139-4</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Stapleton MA, Javid-Majd F, Harmon MF, Hanks BA, Grahmann JL, Mullins LS, Raushel FM (November 1996). "Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase". Biochemistry. 35 (45): 14352–61. doi:10.1021/bi961183y. PMID 8916922. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Holden HM, Thoden JB, Raushel FM (December 1998). "Carbamoyl phosphate synthetase: a tunnel runs through it". Current Opinion in Structural Biology. 8 (6): 679–85. doi:10.1016/s0959-440x(98)80086-9. PMID 9914247. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Raushel FM, Thoden JB, Reinhart GD, Holden HM (October 1998). "Carbamoyl phosphate synthetase: a crooked path from substrates to products". Current Opinion in Chemical Biology. 2 (5): 624–32. doi:10.1016/s1367-5931(98)80094-x. PMID 9818189. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Raushel FM, Thoden JB, Holden HM (June 1999). "The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia". Biochemistry. 38 (25): 7891–9. doi:10.1021/bi990871p. PMID 10387030. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Thoden JB, Huang X, Raushel FM, Holden HM (October 2002). "Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia". The Journal of Biological Chemistry. 277 (42): 39722–7. doi:10.1074/jbc.M206915200. PMID 12130656. <a href="https://doi.org/10.1074%2Fjbc.M206915200" target="_blank">https://doi.org/10.1074%2Fjbc.M206915200</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Inkling. "Unsupported Browser". Inkling. Retrieved 25 April 2018. <a href="https://www.inkling.com/read/illustrated-reviews-biochemistry-harvey-5th/chapter-22/pyrimidine-synthesis-and" target="_blank">https://www.inkling.com/read/illustrated-reviews-biochemistry-harvey-5th/chapter-22/pyrimidine-synthesis-and</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Engelking LR. Pyrimidine biosynthesis. Textbook of Veterinary Physiological Chemistry. 2015;:83–7. https://doi.org/10.1016/B978-0-12-391909-0.50014-1 Retrieved 1 April 2023 <a href="https://doi.org/10.1016/B978-0-12-391909-0.50014-1" target="_blank">https://doi.org/10.1016/B978-0-12-391909-0.50014-1</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Moreno-Morcillo M, Grande-García A, Ruiz-Ramos A, del Caño-Ochoa F, Boskovic J, Ramón-Maiques S (2017). "Structural Insight into the Core of CAD, the Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis". Structure. 25 (6): 912–923. doi:10.1016/j.str.2017.04.012. hdl:10261/166586. PMID 28591622. <a href="https://doi.org/10.1016%2Fj.str.2017.04.012" target="_blank">https://doi.org/10.1016%2Fj.str.2017.04.012</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> </ol>