Reviews - 2we4 mentioned but not cited (1)
- Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets. Shi D, Caldovic L, Tuchman M. Biology (Basel) 7 E34 (2018)
Articles - 2we4 mentioned but not cited (1)
- Structural characterization of the enzymes composing the arginine deiminase pathway in Mycoplasma penetrans. Gallego P, Planell R, Benach J, Querol E, Perez-Pons JA, Reverter D. PLoS One 7 e47886 (2012)
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- Novel metabolic attributes of the genus cyanothece, comprising a group of unicellular nitrogen-fixing Cyanothece. Bandyopadhyay A, Elvitigala T, Welsh E, Stöckel J, Liberton M, Min H, Sherman LA, Pakrasi HB. mBio 2 e00214-11 (2011)
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- A novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris. Shi D, Li Y, Cabrera-Luque J, Jin Z, Yu X, Zhao G, Haskins N, Allewell NM, Tuchman M. PLoS One 6 e28825 (2011)
- Enzymology of the pathway for ATP production by arginine breakdown. Pols T, Singh S, Deelman-Driessen C, Gaastra BF, Poolman B. FEBS J 288 293-309 (2021)
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- Enhanced production of L-arginine by improving carbamoyl phosphate supply in metabolically engineered Corynebacterium crenatum. Wang Q, Jiang A, Tang J, Gao H, Zhang X, Yang T, Xu Z, Xu M, Rao Z. Appl Microbiol Biotechnol 105 3265-3276 (2021)
- E. coli allantoinase is activated by the downstream metabolic enzyme, glycerate kinase, and stabilizes the putative allantoin transporter by direct binding. Rodionova IA, Hosseinnia A, Kim S, Goodacre N, Zhang L, Zhang Z, Palsson B, Uetz P, Babu M, Saier MH. Sci Rep 13 7345 (2023)
Related citations provided by authors (2)
- Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.. Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V Protein Sci 8 934-40 (1999)
- The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.. Ramón-Maiques S, Marina A, Uriarte M, Fita I, Rubio V J Mol Biol 299 463-76 (2000)