Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.60.4.1442 ◽

1968 ◽

Vol 60 (4) ◽

pp. 1442-1449 ◽

Author(s):

M. R. Bethell ◽

K. E. Smith ◽

J. S. White ◽

M. E. Jones

Keyword(s):

Escherichia Coli ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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Topology of Binding Sites for Carbamyl Phosphate in Aspartate Transcarbamylase from Escherichia coli. The Use of Pyridoxal Phosphate as Covalent Probe

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1975.tb04139.x ◽

1975 ◽

Vol 54 (1) ◽

pp. 293-299 ◽

Author(s):

Peter SUTER ◽

Jurg P. ROSENBUSCH

Keyword(s):

Escherichia Coli ◽

Binding Sites ◽

Pyridoxal Phosphate ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate

Biochemistry ◽

10.1021/bi00488a041 ◽

1990 ◽

Vol 29 (36) ◽

pp. 8491-8498 ◽

Author(s):

Xu Guang Xi ◽

Francoise Van Vliet ◽

Moncef M. Ladjimi ◽

Raymond Cunin ◽

Guy Herve

Keyword(s):

Escherichia Coli ◽

Carbonyl Group ◽

Catalytic Site ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase

Biochemistry ◽

10.1021/bi00432a037 ◽

1989 ◽

Vol 28 (6) ◽

pp. 2592-2600 ◽

Author(s):

Jeffrey W. Stebbins ◽

Wei Xu ◽

Evan R. Kantrowitz

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Phosphate Binding ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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Aspartate transcarbamylase of Escherichia coli. Heterogeneity of binding sites for carbamyl phosphate and fluorinated analogs of carbamyl phosphate.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)33046-6 ◽

1976 ◽

Vol 251 (19) ◽

pp. 5966-5975

Author(s):

J A Ridge ◽

F Roberts ◽

M H Schaffer ◽

G R Stark

Keyword(s):

Escherichia Coli ◽

Binding Sites ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate ◽

Fluorinated Analogs

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Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)38630-1 ◽

1985 ◽

Vol 260 (27) ◽

pp. 14712-14716 ◽

Author(s):

S F Nowlan ◽

E R Kantrowitz

Keyword(s):

Escherichia Coli ◽

Catalytic Subunit ◽

Aspartate Transcarbamylase ◽

Pyrimidine Pathway ◽

Rapid Purification

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Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)41010-7 ◽

1975 ◽

Vol 250 (17) ◽

pp. 6852-6860 ◽

Author(s):

G R Jacobson ◽

G R Stark

Keyword(s):

Escherichia Coli ◽

Dicarboxylic Acids ◽

Aspartate Transcarbamylase

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Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)41435-x ◽

1975 ◽

Vol 250 (10) ◽

pp. 3571-3583 ◽

Author(s):

DR Evans ◽

SC Pastra-Landis ◽

WN Lipscomb

Keyword(s):

Escherichia Coli ◽

Aspartate Transcarbamylase ◽

Partial Dissociation

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Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.78.11.6759 ◽

1981 ◽

Vol 78 (11) ◽

pp. 6759-6763 ◽

Author(s):

M. Lennick ◽

N. M. Allewell

Keyword(s):

Escherichia Coli ◽

Hydrogen Exchange ◽

Aspartate Transcarbamylase ◽

Exchange Kinetics ◽

Kinetics Of ◽

Effector Binding

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Acetyl and carbamyl phosphate utilization with aspartate transcarbamylase and carbamate kinase

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(63)90031-7 ◽

1963 ◽

Vol 11 (1) ◽

pp. 75-78 ◽

Author(s):

S. Grisolia ◽

R. Amelunxen ◽

L. Raijman

Keyword(s):

Aspartate Transcarbamylase ◽

Carbamyl Phosphate ◽

Carbamate Kinase

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Bicarbonate-Dependent Cleavage of Adenosine Triphosphate and Other Reactions Catalyzed by Escherichia coli Carbamyl Phosphate Synthetase*

Biochemistry ◽

10.1021/bi00874a012 ◽

1966 ◽

Vol 5 (10) ◽

pp. 3157-3163 ◽

Author(s):

Paul M. Anderson ◽

Alton Meister

Keyword(s):

Escherichia Coli ◽

Adenosine Triphosphate ◽

Carbamyl Phosphate ◽

Carbamyl Phosphate Synthetase

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