Nucleotide sequence of the pyrimidine specific carbamoyl phosphate synthetase, a part of the yeast multifunctional protein encoded by the URA2 gene

1987 ◽  
Vol 207 (2-3) ◽  
pp. 314-319 ◽  
Author(s):  
Jean-Luc Souciet ◽  
Serge Potier ◽  
Jean-Claude Hubert ◽  
François Lacroute
Keyword(s):  
Nucleotide Sequence ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Multifunctional Protein

scholarly journals Organization of a multifunctional protein in pyrimidine biosynthesis. A domain hypersensitive to proteolysis

1984 ◽  
Vol 217 (2) ◽  
pp. 435-440 ◽  
Author(s):  
P C Rumsby ◽  
P C Campbell ◽  
L A Niswander ◽  
J N Davidson
Keyword(s):  
Pyrimidine Biosynthesis ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Multifunctional Protein ◽  
Aggregation Site ◽  
Aspartate Carbamoyltransferase ◽  
Low Concentrations ◽  
Proteinase A

When the multifunctional protein that catalyses the first three steps of pyrimidine biosynthesis in hamster cells is treated with staphylococcal V8 proteinase, a single cleavage takes place. The activities of carbamoyl-phosphate synthetase (EC 6.3.5.5), aspartate carbamoyltransferase (EC 2.1.3.2) and dihydro-orotase (EC 3.5.2.3) and the allosteric inhibition by UTP are unaffected. One fragment, of Mr 182000, has the first and third enzyme activities, whereas the other fragment, of Mr 42000, has aspartate carbamoyltransferase activity and an aggregation site. A similar small fragment is observed in protein digested with low concentrations of trypsin. A similar large fragment is seen after digestion with trypsin and as the predominating form of this protein in certain mutants defective in pyrimidine biosynthesis. These results indicate that a region located adjacent to the aspartate carbamoyltransferase domain is hypersensitive to proteinase action in vitro and may also be sensitive to proteolysis in vivo.

scholarly journals Pyrimidine Biosynthetic Enzyme CAD: Its Function, Regulation, and Diagnostic Potential

2021 ◽  
Vol 22 (19) ◽  
pp. 10253
Author(s):  
Guanya Li ◽  
Dunhui Li ◽  
Tao Wang ◽  
Shanping He
Keyword(s):  
Metabolic Diseases ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Nucleotide Synthesis ◽  
Multifunctional Protein ◽  
The Past ◽  
Pyrimidine Nucleotide ◽  
Diagnostic Potential ◽  
Active Intermediates

CAD (Carbamoyl-phosphate synthetase 2, Aspartate transcarbamoylase, and Dihydroorotase) is a multifunctional protein that participates in the initial three speed-limiting steps of pyrimidine nucleotide synthesis. Over the past two decades, extensive investigations have been conducted to unmask CAD as a central player for the synthesis of nucleic acids, active intermediates, and cell membranes. Meanwhile, the important role of CAD in various physiopathological processes has also been emphasized. Deregulation of CAD-related pathways or CAD mutations cause cancer, neurological disorders, and inherited metabolic diseases. Here, we review the structure, function, and regulation of CAD in mammalian physiology as well as human diseases, and provide insights into the potential to target CAD in future clinical applications.

scholarly journals Product inhibition studies on bovine liver carbamoyl phosphate synthetase

1974 ◽  
Vol 141 (3) ◽  
pp. 817-824 ◽  
Author(s):  
Keith R. F. Elliott ◽  
Keith F. Tipton
Keyword(s):  
Inorganic Phosphate ◽  
Substrate Binding ◽  
Inorganic Ions ◽  
Bovine Liver ◽  
Product Inhibition ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Product Release ◽  
Proposed Model ◽  
Inhibition Studies

A study of the product-inhibition patterns of carbamoyl phosphate synthetase from bovine liver is reported. Inhibition by adenosine, AMP and inorganic ions is also reported. The results are in agreement with the previously proposed model in which the order of substrate binding is ATPMg, followed by HCO3−, ATPMg and NH4+. The order of product release on the basis of the reported results is carbamoyl phosphate, followed by ADPMg, ADPMg and inorganic phosphate.

Inactivation by acivicin of carbamoyl-phosphate synthetase II of human colon carcinoma

1985 ◽  
Vol 34 (1) ◽  
pp. 97-100 ◽  
Author(s):  
Judith S. Sebolt ◽  
Takashi Aoki ◽  
John N. Eble ◽  
John L Glover ◽  
George Weber
Keyword(s):  
Colon Carcinoma ◽  
Human Colon ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Human Colon Carcinoma

Spatial relationships among the active and allosteric sites of carbamoyl-phosphate synthetase

1985 ◽  
Vol 13 (2) ◽  
pp. 98-109 ◽  
Author(s):  
Philip G. Kasprzyk ◽  
Eric Whalen-Pederson ◽  
Paul M. Anderson ◽  
Joseph J. Villafranca
Keyword(s):  
Spatial Relationships ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Allosteric Sites
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