| http://purl.uniprot.org/citations/35347 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/35347 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/35347 | http://www.w3.org/2000/01/rdf-schema#comment | "Yeast argininosuccinate synthetase has been purified to homogeneity. The enzyme was found to have a molecular weight of 228,000 as determined by gel sieving. It is composed of identical subunits of Mr 49,000 as shown by gel electrophoresis. The quaternary structure as determined by cross-linking of the subunits with glutaraldehyde, followed by gel electrophoresis with dodecylsulfate, is tetrameric. The saturation functions by citrulline and aspartate are hyperbolic; with MgATP as the variable substrate a sigmoid character, dependent on the concentration of citrulline, aspartate, argininosuccinate and arginine, was observed. The positive cooperativity is reduced by increasing concentrations of citrulline and aspartate; it is increased by argininosuccinate and arginine. Kinetic analysis provided evidence for a random addition of substrates. Initial velocity studies as well as product and dead-end inhibition studies comply with a rapid-equilibrium random model, except for the interconversion of the central quaternary complexes; the different kinetic constants have been established on the basis. Yeast argininosuccinate synthetase has a double metabolic function: anabolic in the biosynthesis of arginine, catabolic as the first enzyme of citrulline utilization as nitrogen source. The kinetic properties of the enzyme point to a physiologically well-adjusted activity for both roles and to an economic and efficient utilization of ATP."xsd:string |
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| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/author | "Stalon V."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/author | "Stalon V."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/author | "Hilger F."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/author | "Hilger F."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/author | "Simon J.-P."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/author | "Simon J.-P."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/date | "1979"xsd:gYear |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/date | "1979"xsd:gYear |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/pages | "153-163"xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/pages | "153-163"xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/title | "Yeast argininosuccinate synthetase. Purification; structural and kinetic properties."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/title | "Yeast argininosuccinate synthetase. Purification; structural and kinetic properties."xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/volume | "94"xsd:string |
| http://purl.uniprot.org/citations/35347 | http://purl.uniprot.org/core/volume | "94"xsd:string |
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