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Items: 1 to 20 of 41

1.
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.
J. W. Stebbins, D. E. Robertson, M. F. Roberts, R. C. Stevens, W. N. Lipscomb, E. R. Kantrowitz
Protein Sci. 1992 Nov; 1(11): 1435–1446. doi: 10.1002/pro.5560011105
PMCID:
PMC2142124
SummaryPDF–1.1M
2.
Metal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase
Gregory M. Cockrell, Evan R. Kantrowitz
Biochemistry. Author manuscript; available in PMC 2013 Sep 11.
Published in final edited form as: Biochemistry. 2012 Sep 11; 51(36): 7128–7137. Published online 2012 Aug 24. doi: 10.1021/bi300920m
PMCID:
PMC3461825
ArticlePDF–2.9M
3.
Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase
Wenyue Guo, Jay M. West, Andrew S. Dutton, Hiro Tsuruta, Evan R. Kantrowitz
Proc Natl Acad Sci U S A. 2012 May 15; 109(20): 7741–7746. Published online 2012 Apr 30. doi: 10.1073/pnas.1119683109
PMCID:
PMC3356622
ArticlePDF–999K
4.
Allosteric Signal Transmission Involves Synergy between Discrete Structural Units of the Regulatory Subunit of Aspartate Transcarbamoylase
Leyuan Liu, Melinda E. Wales, James R. Wild
Arch Biochem Biophys. Author manuscript; available in PMC 2011 Dec 18.
Published in final edited form as: Arch Biochem Biophys. 2000 Jan 15; 373(2): 352–360. doi: 10.1006/abbi.1999.1570
PMCID:
PMC3241997
ArticlePDF–1.6M
5.
The First High pH Structure of Escherichia coli Aspartate Transcarbamoylase
Kimberly A. Stieglitz, Jiarong Xia, Evan Kantrowitz
Proteins. Author manuscript; available in PMC 2010 Aug 11.
Published in final edited form as: Proteins. 2009 Feb 1; 74(2): 318–327. doi: 10.1002/prot.22162
PMCID:
PMC2920061
ArticlePDF–3.2M
6.
Synthesis and In Vitro Evaluation of Aspartate Transcarbamoylase Inhibitors
Laëtitia Coudray, Anne F. Pennebaker, Jean-Luc Montchamp
Bioorg Med Chem. Author manuscript; available in PMC 2010 Nov 15.
Published in final edited form as: Bioorg Med Chem. 2009 Nov 15; 17(22): 7680–7689. Published online 2009 Sep 30. doi: 10.1016/j.bmc.2009.09.045
PMCID:
PMC2783949
ArticlePDF–1.2M
7.
Submicromolar Phosphinic Inhibitors of E. coli Aspartate Transcarbamoylase
Laëtitia Coudray, Evan R. Kantrowitz, Jean-Luc Montchamp
Bioorg Med Chem Lett. Author manuscript; available in PMC 2010 Feb 1.
Published in final edited form as: Bioorg Med Chem Lett. 2009 Feb 1; 19(3): 900–902. Published online 2008 Dec 6. doi: 10.1016/j.bmcl.2008.11.115
PMCID:
PMC2743340
ArticlePDF–319K
8.
Dissecting Enzyme Regulation by Multiple Allosteric Effectors: Nucleotide Regulation of Aspartate Transcarbamoylase
Joshua D. Rabinowitz, Jennifer J. Hsiao, Kimberly R. Gryncel, Evan R. Kantrowitz, Xiao-Jiang Feng, Genyuan Li, Herschel Rabitz
Biochemistry. Author manuscript; available in PMC 2009 Aug 26.
Published in final edited form as: Biochemistry. 2008 May 27; 47(21): 5881–5888. Published online 2008 May 3. doi: 10.1021/bi8000566
PMCID:
PMC2732338
ArticlePDF–673K
9.
Structural Model of the R State of Escherichia coli Aspartate Transcarbamoylase with Substrates Bound
Jie Wang, Joby Eldo, Evan R. Kantrowitz
J Mol Biol. Author manuscript; available in PMC 2009 Aug 3.
Published in final edited form as: J Mol Biol. 2007 Aug 31; 371(5): 1261–1273. Published online 2007 Jun 9. doi: 10.1016/j.jmb.2007.06.011
PMCID:
PMC2720131
ArticlePDF–2.0M
10.
Time Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow Tight Binding Inhibitor
Jay M. West, Jiarong Xia, Hiro Tsuruta, Wenyue Guo, Elizabeth M. O’Day, Evan R. Kantrowitz
J Mol Biol. Author manuscript; available in PMC 2009 Dec 5.
Published in final edited form as: J Mol Biol. 2008 Dec 5; 384(1): 206–218. Published online 2008 Sep 16. doi: 10.1016/j.jmb.2008.09.022
PMCID:
PMC2656920
ArticlePDF–1.0M
11.
N-phosphonacetyl-L-isoasparagine a Potent and Specific Inhibitor of E. coli Aspartate Transcarbamoylase
Joby Eldo, James P. Cardia, Elizabeth M. O’Day, Jiarong Xia, Hiro Tsurata, Evan R. Kantrowitz
J Med Chem. Author manuscript; available in PMC 2008 Sep 16.
Published in final edited form as: J Med Chem. 2006 Oct 5; 49(20): 5932–5938. doi: 10.1021/jm0607294
PMCID:
PMC2538380
ArticlePDF–1.0M
12.
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
L. Fetler, P. Tauc, D.P. Baker, C.P. Macol, E.R. Kantrowitz, P. Vachette
Protein Sci. 2002 May; 11(5): 1074–1081. doi: 10.1110/ps.4500102
PMCID:
PMC2373563
ArticlePDF–125K
13.
The use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase.
J. B. Sakash, A. Tsen, E. R. Kantrowitz
Protein Sci. 2000 Jan; 9(1): 53–63. doi: 10.1110/ps.9.1.53
PMCID:
PMC2144450
SummaryPDF–1.8M
14.
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.
C. Macol, M. Dutta, B. Stec, H. Tsuruta, E. R. Kantrowitz
Protein Sci. 1999 Jun; 8(6): 1305–1313. doi: 10.1110/ps.8.6.1305
PMCID:
PMC2144362
SummaryPDF–204K
15.
The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.
D. P. Baker, L. Fetler, P. Vachette, E. R. Kantrowitz
Protein Sci. 1996 Nov; 5(11): 2276–2286. doi: 10.1002/pro.5560051114
PMCID:
PMC2143294
SummaryPDF–960K
16.
Ligation alters the pathway of urea-induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase.
S. Bromberg, V. J. LiCata, D. Mallikarachchi, N. M. Allewell
Protein Sci. 1994 Aug; 3(8): 1236–1244. doi: 10.1002/pro.5560030809
PMCID:
PMC2142926
SummaryPDF–1.8M
17.
Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.
C. B. Peterson, B. B. Zhou, D. Hsieh, A. N. Creager, H. K. Schachman
Protein Sci. 1994 Jun; 3(6): 960–966. doi: 10.1002/pro.5560030611
PMCID:
PMC2142879
SummaryPDF–781K
18.
A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
B. B. Zhou, G. L. Waldrop, L. Lum, H. K. Schachman
Protein Sci. 1994 Jun; 3(6): 967–974. doi: 10.1002/pro.5560030612
PMCID:
PMC2142877
SummaryPDF–866K
19.
A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition
Kimberly A. Stieglitz, Styliani C. Pastra-Landis, Jiarong Xia, Hiro Tsuruta, Evan R. Kantrowitz
J Mol Biol. Author manuscript; available in PMC 2006 Jun 15.
Published in final edited form as: J Mol Biol. 2005 Jun 3; 349(2): 413–423. Published online 2005 Apr 9. doi: 10.1016/j.jmb.2005.03.073
PMCID:
PMC1479453
ArticlePDF–1.0M
20.
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase
Jie Wang, Kimberly A. Stieglitz, James P. Cardia, Evan R. Kantrowitz
Proc Natl Acad Sci U S A. 2005 Jun 21; 102(25): 8881–8886. Published online 2005 Jun 10. doi: 10.1073/pnas.0503742102
PMCID:
PMC1157055
ArticlePDF–603K

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