865 related articles for article (PubMed ID: 16906764)
1. 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; 45(33):10062-71. PubMed ID: 16906764
[TBL] [Abstract][Full Text] [Related]
2. Use of L-asparagine and N-phosphonacetyl-L-asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbomoylase.
Cardia JP; Eldo J; Xia J; O'Day EM; Tsuruta H; Gryncel KR; Kantrowitz ER
Proteins; 2008 May; 71(3):1088-96. PubMed ID: 18004787
[TBL] [Abstract][Full Text] [Related]
3. A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.
Stieglitz KA; Pastra-Landis SC; Xia J; Tsuruta H; Kantrowitz ER
J Mol Biol; 2005 Jun; 349(2):413-23. PubMed ID: 15890205
[TBL] [Abstract][Full Text] [Related]
4. Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states.
Stieglitz K; Stec B; Baker DP; Kantrowitz ER
J Mol Biol; 2004 Aug; 341(3):853-68. PubMed ID: 15288791
[TBL] [Abstract][Full Text] [Related]
5. T-state active site of aspartate transcarbamylase: crystal structure of the carbamyl phosphate and L-alanosine ligated enzyme.
Huang J; Lipscomb WN
Biochemistry; 2006 Jan; 45(2):346-52. PubMed ID: 16401065
[TBL] [Abstract][Full Text] [Related]
6. Direct observation of an altered quaternary-structure transition in a mutant aspartate transcarbamoylase.
Tsuruta H; Vachette P; Kantrowitz ER
Proteins; 1998 Jun; 31(4):383-90. PubMed ID: 9626698
[TBL] [Abstract][Full Text] [Related]
7. 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
[TBL] [Abstract][Full Text] [Related]
8. Cooperativity and high pressure: stabilization of the R conformation of the allosteric aspartate transcarbamylase under the influence of pressure.
Hervé G; Schmitt B; Serre V
Cell Mol Biol (Noisy-le-grand); 2004 Jun; 50(4):347-52. PubMed ID: 15529744
[TBL] [Abstract][Full Text] [Related]
9. Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?
Foote J; Schachman HK
J Mol Biol; 1985 Nov; 186(1):175-84. PubMed ID: 3908690
[TBL] [Abstract][Full Text] [Related]
10. Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi. Insights into cooperative and allosteric mechanisms.
Van Boxstael S; Maes D; Cunin R
FEBS J; 2005 Jun; 272(11):2670-83. PubMed ID: 15943802
[TBL] [Abstract][Full Text] [Related]
11. Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase.
Macol CP; Tsuruta H; Stec B; Kantrowitz ER
Nat Struct Biol; 2001 May; 8(5):423-6. PubMed ID: 11323717
[TBL] [Abstract][Full Text] [Related]
12. The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects.
Sakash JB; Kantrowitz ER
Biochemistry; 1998 Jan; 37(1):281-8. PubMed ID: 9425049
[TBL] [Abstract][Full Text] [Related]
13. A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure.
Williams MK; Stec B; Kantrowitz ER
J Mol Biol; 1998 Aug; 281(1):121-34. PubMed ID: 9680480
[TBL] [Abstract][Full Text] [Related]
14. Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle.
Stieglitz KA; Dusinberre KJ; Cardia JP; Tsuruta H; Kantrowitz ER
J Mol Biol; 2005 Sep; 352(2):478-86. PubMed ID: 16120448
[TBL] [Abstract][Full Text] [Related]
15. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.
Jin L; Stec B; Lipscomb WN; Kantrowitz ER
Proteins; 1999 Dec; 37(4):729-42. PubMed ID: 10651286
[TBL] [Abstract][Full Text] [Related]
16. Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
Baker DP; Fetler L; Keiser RT; Vachette P; Kantrowitz ER
Protein Sci; 1995 Feb; 4(2):258-67. PubMed ID: 7757014
[TBL] [Abstract][Full Text] [Related]
17. Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP.
De Vos D; Xu Y; Aerts T; Van Petegem F; Van Beeumen JJ
Biochem Biophys Res Commun; 2008 Jul; 372(1):40-4. PubMed ID: 18477471
[TBL] [Abstract][Full Text] [Related]
18. Intramolecular signal transmission in enterobacterial aspartate transcarbamylases II. Engineering co-operativity and allosteric regulation in the aspartate transcarbamylase of Erwinia herbicola.
Cunin R; Rani CS; Van Vliet F; Wild JR; Wales M
J Mol Biol; 1999 Dec; 294(5):1401-11. PubMed ID: 10600394
[TBL] [Abstract][Full Text] [Related]
19. The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T<-->R equilibrium.
Fetler L; Vachette P
J Mol Biol; 2001 Jun; 309(3):817-32. PubMed ID: 11397099
[TBL] [Abstract][Full Text] [Related]
20. 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; 8(6):1305-13. PubMed ID: 10386880
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
