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http://purl.uniprot.org/citations/4908780http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/4908780http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/4908780http://www.w3.org/2000/01/rdf-schema#comment"A mutant of Escherichia coli is described which is defective in the conversion of arginine to putrescine. The activity of the enzyme agmatine ureohydrolase is greatly reduced, whereas the activity of the other two enzymes of the pathway, the constitutive arginine decarboxylase and the inducible arginine decarboxylase, are within the normal range. The growth behavior of the mutant reflects the enzymatic block. It grows well in the absence of arginine, but only poorly in the presence of arginine. Under the former conditions, putrescine can be formed from ornithine as well as arginine, whereas under the latter conditions, because of feedback control, it can be formed only from arginine."xsd:string
http://purl.uniprot.org/citations/4908780http://purl.org/dc/terms/identifier"doi:10.1128/jb.101.3.725-730.1970"xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/author"Maas W.K."xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/author"Hirshfield I.N."xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/author"Leifer Z."xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/author"Rosenfeld H.J."xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/date"1970"xsd:gYear
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/name"J Bacteriol"xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/pages"725-730"xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/title"Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine."xsd:string
http://purl.uniprot.org/citations/4908780http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/4908780http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/4908780
http://purl.uniprot.org/citations/4908780http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/4908780
http://purl.uniprot.org/citations/4908780http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/4908780
http://purl.uniprot.org/citations/4908780http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/4908780
http://purl.uniprot.org/enzyme/3.5.3.11http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4908780
http://purl.uniprot.org/uniprot/P60651#attribution-FC3057FC68A76330713B9878B64827D6http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/4908780