152 related articles for article (PubMed ID: 3283120)
1. 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; 263(13):6109-14. PubMed ID: 3283120
[TBL] [Abstract][Full Text] [Related]
2. Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.
Zhou BB; Schachman HK
Protein Sci; 1993 Jan; 2(1):103-12. PubMed ID: 8443583
[TBL] [Abstract][Full Text] [Related]
3. Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.
Peterson CB; Schachman HK
J Biol Chem; 1992 Feb; 267(4):2443-50. PubMed ID: 1733944
[TBL] [Abstract][Full Text] [Related]
4. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site.
Corder TS; Wild JR
J Biol Chem; 1989 May; 264(13):7425-30. PubMed ID: 2651439
[TBL] [Abstract][Full Text] [Related]
5. 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; 264(5):2476-81. PubMed ID: 2644262
[TBL] [Abstract][Full Text] [Related]
6. Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase.
Sakash JB; Chan RS; Tsuruta H; Kantrowitz ER
J Biol Chem; 2000 Jan; 275(2):752-8. PubMed ID: 10625604
[TBL] [Abstract][Full Text] [Related]
7. Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains.
Powers VM; Yang YR; Fogli MJ; Schachman HK
Protein Sci; 1993 Jun; 2(6):1001-12. PubMed ID: 8318885
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.
Dembowski NJ; Newton CJ; Kantrowitz ER
Biochemistry; 1990 Apr; 29(15):3716-23. PubMed ID: 2111165
[TBL] [Abstract][Full Text] [Related]
10. Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.
Newton CJ; Stevens RC; Kantrowitz ER
Biochemistry; 1992 Mar; 31(11):3026-32. PubMed ID: 1550826
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.
Baker DP; Fetler L; Vachette P; Kantrowitz ER
Protein Sci; 1996 Nov; 5(11):2276-86. PubMed ID: 8931146
[TBL] [Abstract][Full Text] [Related]
13. Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.
Stebbins JW; Zhang Y; Kantrowitz ER
Biochemistry; 1990 Apr; 29(16):3821-7. PubMed ID: 2191720
[TBL] [Abstract][Full Text] [Related]
14. Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase.
Xu W; Kantrowitz ER
Biochemistry; 1989 Dec; 28(26):9937-43. PubMed ID: 2515892
[TBL] [Abstract][Full Text] [Related]
15. 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]
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. Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.
Fetler L; Tauc P; Baker DP; Macol CP; Kantrowitz ER; Vachette P
Protein Sci; 2002 May; 11(5):1074-81. PubMed ID: 11967364
[TBL] [Abstract][Full Text] [Related]
18. Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
Endrizzi JA; Beernink PT; Alber T; Schachman HK
Proc Natl Acad Sci U S A; 2000 May; 97(10):5077-82. PubMed ID: 10805770
[TBL] [Abstract][Full Text] [Related]
19. Divergent allosteric patterns verify the regulatory paradigm for aspartate transcarbamylase.
Wales ME; Madison LL; Glaser SS; Wild JR
J Mol Biol; 1999 Dec; 294(5):1387-400. PubMed ID: 10600393
[TBL] [Abstract][Full Text] [Related]
20. Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase.
Williams MK; Kantrowitz ER
Biochim Biophys Acta; 1998 Dec; 1429(1):249-58. PubMed ID: 9920401
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
