173 related articles for article (PubMed ID: 3146350)
1. Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.
Middleton SA; Kantrowitz ER
Biochemistry; 1988 Nov; 27(23):8653-60. PubMed ID: 3146350
[TBL] [Abstract][Full Text] [Related]
2. A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase.
Middleton SA; Stebbins JW; Kantrowitz ER
Biochemistry; 1989 Feb; 28(4):1617-26. PubMed ID: 2655696
[TBL] [Abstract][Full Text] [Related]
3. Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.
Newton CJ; Kantrowitz ER
Biochemistry; 1990 Feb; 29(6):1444-51. PubMed ID: 2185840
[TBL] [Abstract][Full Text] [Related]
4. Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase.
Ladjimi MM; Middleton SA; Kelleher KS; Kantrowitz ER
Biochemistry; 1988 Jan; 27(1):268-76. PubMed ID: 3280018
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. 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]
7. 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]
8. 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]
9. Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase.
Stebbins JW; Xu W; Kantrowitz ER
Biochemistry; 1989 Mar; 28(6):2592-600. PubMed ID: 2659074
[TBL] [Abstract][Full Text] [Related]
10. The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase.
Baker DP; Kantrowitz ER
Biochemistry; 1993 Sep; 32(38):10150-8. PubMed ID: 8104480
[TBL] [Abstract][Full Text] [Related]
11. The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain.
Newton CJ; Kantrowitz ER
Proc Natl Acad Sci U S A; 1990 Mar; 87(6):2309-13. PubMed ID: 2179954
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. 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]
14. Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase.
Xu W; Kantrowitz ER
Biochemistry; 1991 Mar; 30(9):2535-42. PubMed ID: 1900434
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interface.
Baker DP; Stebbins JW; DeSena E; Kantrowitz ER
J Biol Chem; 1994 Oct; 269(40):24608-14. PubMed ID: 7929132
[TBL] [Abstract][Full Text] [Related]
17. A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.
Ladjimi MM; Kantrowitz ER
Biochemistry; 1988 Jan; 27(1):276-83. PubMed ID: 3280019
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.
Macol CP; Tsuruta H; Kantrowitz ER
J Biol Chem; 2002 Jul; 277(30):26852-7. PubMed ID: 12016227
[TBL] [Abstract][Full Text] [Related]
20. Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
Tauc P; Vachette P; Middleton SA; Kantrowitz ER
J Mol Biol; 1990 Jul; 214(1):327-35. PubMed ID: 1973463
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
