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Aspartate Carbamoyltransferase
Known as:
Carbamoyl-phosphate:L-aspartate carbamoyltransferase
, Carbamoyltransferase, Aspartate
, Aspartate Carbamoyltransferase [Chemical/Ingredient]
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An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (From Enzyme…
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National Institutes of Health
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Related topics
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9 relations
Narrower (2)
CAD trifunctional enzyme
carbamoyl phosphate synthase-aspartatecarbamoyl transferase complex
In Blood
Process of secretion
antagonists & inhibitors
aspects of radiation effects
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1985
Highly Cited
1985
Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.
S. Nowlan
,
E. Kantrowitz
Journal of Biological Chemistry
1985
Corpus ID: 25128437
Highly Cited
1985
Highly Cited
1985
Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.
K. Krause
,
K. Volź
,
W. Lipscomb
Proceedings of the National Academy of Sciences…
1985
Corpus ID: 31974392
In an x-ray diffraction study by the isomorphous replacement method, the structure of the complex of aspartate…
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Highly Cited
1979
Highly Cited
1979
Changes in the x-ray solution scattering of aspartate transcarbamylase following the allosteric transition.
M. F. Moody
,
P. Vachette
,
A. Foote
Journal of Molecular Biology
1979
Corpus ID: 34659959
Highly Cited
1975
Highly Cited
1975
A complex genetic locus that controls the first three steps of pyrimidine biosynthesis in Drosophila
J. Rawls
,
J. Fristrom
Nature
1975
Corpus ID: 4222639
IN eukaryotes, the initial steps in the de novo synthesis of pyrimidines are performed by multienzyme complexes consisting of the…
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Highly Cited
1974
Highly Cited
1974
N-(phosphonacetyl)-L-aspartate, a potent transition state analog inhibitor of aspartate transcarbamylase, blocks proliferation of mammalian cells in culture.
E. A. Swyryd
,
S. Seaver
,
G. Stark
Journal of Biological Chemistry
1974
Corpus ID: 23845172
Highly Cited
1971
Highly Cited
1971
Subunit structure of aspartate transcarbamylase from Escherichia coli.
J. Rosenbusch
,
K. Weber
Journal of Biological Chemistry
1971
Corpus ID: 710513
Highly Cited
1970
Highly Cited
1970
Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins.
G. Davies
,
G. Stark
Proceedings of the National Academy of Sciences…
1970
Corpus ID: 8441907
Amidination of aldolase, glyceraldehyde-3-phosphate dehydrogenase, tryptophan synthetase B protein, L-arabinose isomerase, and…
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Highly Cited
1970
Highly Cited
1970
A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying…
Thomas C. Vanaman
,
George R. Stark
Journal of Biological Chemistry
1970
Corpus ID: 37789227
Highly Cited
1967
Highly Cited
1967
The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits.
J. Gerhart
,
H. Holoubek
Journal of Biological Chemistry
1967
Corpus ID: 30527549
Highly Cited
1964
Highly Cited
1964
ENZYMES OF ARGININE METABOLISM IN MAMMALIAN CELL CULTURE. I. REPRESSION OF ARGININOSUCCINATE SYNTHETASE AND ARGININOSUCCINASE.
R. Schimke
Journal of Biological Chemistry
1964
Corpus ID: 38560939
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