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11. Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study. Stebbins JW, Robertson DE, Roberts MF, Stevens RC, Lipscomb WN, Kantrowitz ER. Protein Sci; 1992 Nov; 1(11):1435-46. PubMed ID: 1303763 [Abstract] [Full Text] [Related]
12. Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase. Eisenstein E, Markby DW, Schachman HK. Biochemistry; 1990 Apr 17; 29(15):3724-31. PubMed ID: 2187530 [Abstract] [Full Text] [Related]
14. The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity. Macol C, Dutta M, Stec B, Tsuruta H, Kantrowitz ER. Protein Sci; 1999 Jun 17; 8(6):1305-13. PubMed ID: 10386880 [Abstract] [Full Text] [Related]
15. Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme. Wales ME, Hoover TA, Wild JR. J Biol Chem; 1988 May 05; 263(13):6109-14. PubMed ID: 3283120 [Abstract] [Full Text] [Related]
17. Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP. Newell JO, Markby DW, Schachman HK. J Biol Chem; 1989 Feb 15; 264(5):2476-81. PubMed ID: 2644262 [Abstract] [Full Text] [Related]
18. T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition. Heng S, Stieglitz KA, Eldo J, Xia J, Cardia JP, Kantrowitz ER. Biochemistry; 2006 Aug 22; 45(33):10062-71. PubMed ID: 16906764 [Abstract] [Full Text] [Related]
19. 240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase. Alam N, Stieglitz KA, Caban MD, Gourinath S, Tsuruta H, Kantrowitz ER. J Biol Chem; 2004 May 28; 279(22):23302-10. PubMed ID: 15014067 [Abstract] [Full Text] [Related]