Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli.

Faculty Opinions recommendation of Time evolution of the quaternary structure of Escherichia coli aspartate transcarbamoylase upon reaction with the natural substrates and a slow, tight-binding inhibitor.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.12818969.14100069 ◽

2011 ◽

Author(s):

Jean-Pierre Changeux

Keyword(s):

Escherichia Coli ◽

Time Evolution ◽

Quaternary Structure ◽

Tight Binding ◽

Crystallization and preliminary X-ray diffraction studies of an inactive mutant aspartate transcarbamoylase from Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)69302-6 ◽

1981 ◽

Vol 256 (10) ◽

pp. 4691-4692

Author(s):

R. Kim ◽

T.S. Young ◽

H.K. Schachman ◽

S.H. Kim

Keyword(s):

Escherichia Coli ◽

X Ray Diffraction ◽

X Ray

Proteolytic Cleavage of the Multienzyme Polypeptide CAD to Release the Mammalian Aspartate Transcarbamoylase. Biochemical Comparison with the Homologous Escherichia Coli Catalytic Subunit

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1994.0845b.x ◽

1994 ◽

Vol 225 (3) ◽

pp. 845-853 ◽

Cited By ~ 7

Author(s):

Benjamin Hemmens ◽

Elizabeth A. Carrey

Keyword(s):

Escherichia Coli ◽

Proteolytic Cleavage ◽

Catalytic Subunit ◽

Biochemical Comparison

Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase

Biochemistry ◽

10.1021/bi00126a026 ◽

1992 ◽

Vol 31 (11) ◽

pp. 3026-3032 ◽

Cited By ~ 7

Author(s):

Colin J. Newton ◽

Raymond C. Stevens ◽

Evan R. Kantrowitz

Keyword(s):

Escherichia Coli ◽

Conserved Residue

Ligand interactions at the active site of aspartate transcarbamoylase from Escherichia coli

Biochemistry ◽

10.1021/bi00355a023 ◽

1986 ◽

Vol 25 (7) ◽

pp. 1605-1611 ◽

Cited By ~ 4

Author(s):

Paul R. Dennis ◽

M. Vijaya Krishna ◽

Maria Di Gregorio ◽

William W. C. Chan

Keyword(s):

Escherichia Coli ◽

Active Site ◽

Ligand Interactions

Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase

Biochemistry ◽

10.1021/bi00223a034 ◽

1991 ◽

Vol 30 (9) ◽

pp. 2535-2542 ◽

Cited By ~ 8

Author(s):

Wei Xu ◽

Evan R. Kantrowitz

Keyword(s):

Escherichia Coli ◽

Catalytic Mechanism ◽

A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition

Journal of Molecular Biology ◽

10.1016/j.jmb.2005.03.073 ◽

2005 ◽

Vol 349 (2) ◽

pp. 413-423 ◽

Cited By ~ 6

Author(s):

Kimberly A. Stieglitz ◽

Styliani C. Pastra-Landis ◽

Jiarong Xia ◽

Hiro Tsuruta ◽

Evan R. Kantrowitz

Keyword(s):

Escherichia Coli ◽

Amino Acid ◽

Amino Acid Substitution ◽

Active Site ◽

Single Amino Acid Substitution ◽

Single Amino Acid ◽

Allosteric Transition

Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis

Biochemistry ◽

10.1021/bi00118a022 ◽

1992 ◽

Vol 31 (3) ◽

pp. 792-798 ◽

Cited By ~ 18

Author(s):

Yang Zhang ◽

Evan R. Kantrowitz

Keyword(s):

Escherichia Coli ◽

Regulatory Site ◽

Site Specific

On the Mechanism of Assembly of the Aspartate Transcarbamoylase from Escherichia coli

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1978.tb12600.x ◽

1978 ◽

Vol 90 (2) ◽

pp. 271-281 ◽

Cited By ~ 7

Author(s):

William W.-C. CHAN

Keyword(s):

Escherichia Coli ◽

Aspartate Transcarbamoylase from Escherichia coli: Electron Density at 5.5 A Resolution

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.70.4.1117 ◽

1973 ◽

Vol 70 (4) ◽

pp. 1117-1121 ◽

Cited By ~ 32

Author(s):

S. G. Warren ◽

B. F. P. Edwards ◽

D. R. Evans ◽

D. C. Wiley ◽

W. N. Lipscomb

Keyword(s):

Escherichia Coli ◽

Electron Density ◽