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

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 ◽

Cited By ~ 13

Author(s):

Peter SUTER ◽

Jurg P. ROSENBUSCH

Keyword(s):

Escherichia Coli ◽

Binding Sites ◽

Pyridoxal Phosphate ◽

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 ◽

Cited By ~ 78

Author(s):

M. R. Bethell ◽

K. E. Smith ◽

J. S. White ◽

M. E. Jones

Keyword(s):

Escherichia Coli ◽

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 ◽

Cited By ~ 48

Author(s):

Jeffrey W. Stebbins ◽

Wei Xu ◽

Evan R. Kantrowitz

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Phosphate Binding ◽

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

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 ◽

Carbamyl Phosphate ◽

Fluorinated Analogs

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

10.1016/s0021-9258(17)38630-1 ◽

1985 ◽

Vol 260 (27) ◽

pp. 14712-14716 ◽

Cited By ~ 7

Author(s):

S F Nowlan ◽

E R Kantrowitz

Keyword(s):

Escherichia Coli ◽

Catalytic Subunit ◽

Pyrimidine Pathway ◽

Rapid Purification

A spectral probe near the subunit catalytic site of glutamine synthetase from Escherichia coli. Reduced pyridoxal 5'-phosphate.enzyme complexes.

10.1016/s0021-9258(17)38023-7 ◽

1978 ◽

Vol 253 (19) ◽

pp. 7017-7025 ◽

Cited By ~ 4

Author(s):

E.J. Whitley ◽

A. Ginsburg

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Catalytic Site

On the location and function of tyrosine beta 331 in the catalytic site of Escherichia coli F1-ATPase.

10.1016/s0021-9258(18)46004-8 ◽

1992 ◽

Vol 267 (3) ◽

pp. 1712-1718 ◽

Cited By ~ 5

Author(s):

J Weber ◽

R S Lee ◽

E Grell ◽

J G Wise ◽

A E Senior

Keyword(s):

Escherichia Coli ◽

Catalytic Site ◽

F1 Atpase ◽

And Function

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

10.1016/s0021-9258(19)41010-7 ◽

1975 ◽

Vol 250 (17) ◽

pp. 6852-6860 ◽

Cited By ~ 4

Author(s):

G R Jacobson ◽

G R Stark

Keyword(s):

Escherichia Coli ◽

Dicarboxylic Acids ◽

Aspartate Transcarbamylase

The role of the invariant glutamate 95 in the catalytic site of Complex I from Escherichia coli

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/j.bbabio.2008.11.002 ◽

2009 ◽

Vol 1787 (1) ◽

pp. 68-73 ◽

Cited By ~ 14

Author(s):

Liliya Euro ◽

Galina Belevich ◽

Dmitry A. Bloch ◽

Michael I. Verkhovsky ◽

Mårten Wikström ◽

...

Keyword(s):

Escherichia Coli ◽

Complex I ◽

Catalytic Site

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

10.1016/s0021-9258(19)41435-x ◽

1975 ◽

Vol 250 (10) ◽

pp. 3571-3583 ◽

Cited By ~ 2

Author(s):

DR Evans ◽

SC Pastra-Landis ◽

WN Lipscomb

Keyword(s):

Escherichia Coli ◽

Partial Dissociation