Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate

Gordon G. Hammes; Robert W. Porter; George R. Stark

doi:10.1021/bi00782a017

Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate

Biochemistry ◽

10.1021/bi00782a017 ◽

1971 ◽

Vol 10 (6) ◽

pp. 1046-1050 ◽

Cited By ~ 44

Author(s):

Gordon G. Hammes ◽

Robert W. Porter ◽

George R. Stark

Keyword(s):

Catalytic Subunit ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate ◽

Relaxation Spectra

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Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate

Biochemistry ◽

10.1021/bi00787a030 ◽

1971 ◽

Vol 10 (11) ◽

pp. 2150-2156 ◽

Cited By ~ 18

Author(s):

Gordon G. Hammes ◽

Cheng-Wen Wu

Keyword(s):

Native Enzyme ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate ◽

Relaxation Spectra

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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 ◽

Cited By ~ 7

Author(s):

S F Nowlan ◽

E R Kantrowitz

Keyword(s):

Escherichia Coli ◽

Catalytic Subunit ◽

Aspartate Transcarbamylase ◽

Pyrimidine Pathway ◽

Rapid Purification

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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 ◽

Cited By ~ 13

Author(s):

Peter SUTER ◽

Jurg P. ROSENBUSCH

Keyword(s):

Escherichia Coli ◽

Binding Sites ◽

Pyridoxal Phosphate ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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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 ◽

Cited By ~ 7

Author(s):

S. Grisolia ◽

R. Amelunxen ◽

L. Raijman

Keyword(s):

Aspartate Transcarbamylase ◽

Carbamyl Phosphate ◽

Carbamate Kinase

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Response to the adenylate energy charge by Escherichia coli aspartate transcarbamylase and its catalytic subunit

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(69)90575-0 ◽

1969 ◽

Vol 36 (3) ◽

pp. 381-386 ◽

Cited By ~ 12

Author(s):

William N. Bigler ◽

Daniel E. Atkinson

Keyword(s):

Escherichia Coli ◽

Energy Charge ◽

Catalytic Subunit ◽

Adenylate Energy Charge ◽

Aspartate Transcarbamylase

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Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit

Biochemistry ◽

10.1021/bi00819a010 ◽

1970 ◽

Vol 9 (17) ◽

pp. 3353-3362 ◽

Cited By ~ 37

Author(s):

John Eckfeldt ◽

Gordon G. Hammes ◽

Scott C. Mohr ◽

Cheng-Wen Wu

Keyword(s):

Native Enzyme ◽

Regulatory Subunit ◽

Aspartate Transcarbamylase ◽

Relaxation Spectra

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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 ◽

Aspartate Transcarbamylase ◽

Carbamyl Phosphate

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Mechanism of the reaction catalyzed by the catalytic subunit of aspartate transcarbamylase. Kinetic studies with acetyl phosphate as substrate

Biochemistry ◽

10.1021/bi00747a027 ◽

1973 ◽

Vol 12 (23) ◽

pp. 4727-4732 ◽

Cited By ~ 10

Author(s):

Elizabeth Heyde ◽

J. F. Morrison

Keyword(s):

Kinetic Studies ◽

Catalytic Subunit ◽

Acetyl Phosphate ◽

Aspartate Transcarbamylase ◽

Mechanism Of The Reaction

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Carbamyl-phosphate synthetase domain of the yeast multifunctional protein Ura2 is necessary for aspartate transcarbamylase inhibition by UTP

FEBS Letters ◽

10.1016/s0014-5793(98)00010-6 ◽

1998 ◽

Vol 422 (2) ◽

pp. 170-174 ◽

Cited By ~ 5

Author(s):

Richard Antonelli ◽

Laurence Estevez ◽

Michèle Denis-Duphil

Keyword(s):

Aspartate Transcarbamylase ◽

Carbamyl Phosphate ◽

Multifunctional Protein ◽

Carbamyl Phosphate Synthetase

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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 ◽

Cited By ~ 11

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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