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http://purl.uniprot.org/citations/206652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/206652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/206652http://www.w3.org/2000/01/rdf-schema#comment"The arginine-specific carbamoyl-phosphate synthase of yeast was stabilized sufficiently to allow partial purification of the enzyme (30-to 40-fold). The synthase (mol. wt 115000) comprised two unequal subunits: a heavy subunit (mol. wt 80000) capable of catalysing synthesis of carbamoyl phosphate with ammonia as a nitrogen donor and a light subunit conferring upon the holoenzyme the ability to utilize glutamine. The enzyme had unusually high affinity for ATP (Km = 0.2 mM) and atypical negative cooperativity for glutamine binding ([S]0.5 = 0.25 mM). Glutamine activity was not modulated by possible effectors such as arginine, ornithine or N-acetylglutamate. Thus, although the yeast arginine enzyme physically and functionally resembles the single enteric synthase, the systems differ substantially both in kinetic properties and in regulation of activity."xsd:string
http://purl.uniprot.org/citations/206652http://purl.org/dc/terms/identifier"doi:10.1099/00221287-106-1-145"xsd:string
http://purl.uniprot.org/citations/206652http://purl.org/dc/terms/identifier"doi:10.1099/00221287-106-1-145"xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/author"Price C.W."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/author"Price C.W."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/author"Abdelal A.T."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/author"Abdelal A.T."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/author"Holwell J.H."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/author"Holwell J.H."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/date"1978"xsd:gYear
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/date"1978"xsd:gYear
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/name"J. Gen. Microbiol."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/name"J. Gen. Microbiol."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/pages"145-151"xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/pages"145-151"xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/title"Purification and properties of the arginine-specific carbamoyl-phosphate synthase from Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/title"Purification and properties of the arginine-specific carbamoyl-phosphate synthase from Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/volume"106"xsd:string
http://purl.uniprot.org/citations/206652http://purl.uniprot.org/core/volume"106"xsd:string
http://purl.uniprot.org/citations/206652http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/206652
http://purl.uniprot.org/citations/206652http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/206652
http://purl.uniprot.org/citations/206652http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/206652
http://purl.uniprot.org/citations/206652http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/206652