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http://purl.uniprot.org/citations/20675472http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20675472http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20675472http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/20675472http://www.w3.org/2000/01/rdf-schema#comment"Long-chain and/or branched-chain polyamines are unique polycations found in thermophiles. Cytoplasmic polyamines were analyzed for cells cultivated at various growth temperatures in the hyperthermophilic archaeon Thermococcus kodakarensis. Spermidine [34] and N4-aminopropylspermine [3(3)43] were identified as major polyamines at 60°C, and the amounts of N4-aminopropylspermine [3(3)43] increased as the growth temperature rose. To identify genes involved in polyamine biosynthesis, a gene disruption study was performed. The open reading frames (ORFs) TK0240, TK0474, and TK0882, annotated as agmatine ureohydrolase genes, were disrupted. Only the TK0882 gene disruptant showed a growth defect at 85°C and 93°C, and the growth was partially retrieved by the addition of spermidine. In the TK0882 gene disruptant, agmatine and N1-aminopropylagmatine accumulated in the cytoplasm. Recombinant TK0882 was purified to homogeneity, and its ureohydrolase characteristics were examined. It possessed a 43-fold-higher kcat/Km value for N1-aminopropylagmatine than for agmatine, suggesting that TK0882 functions mainly as N1-aminopropylagmatine ureohydrolase to produce spermidine. TK0147, annotated as spermidine/spermine synthase, was also studied. The TK0147 gene disruptant showed a remarkable growth defect at 85°C and 93°C. Moreover, large amounts of agmatine but smaller amounts of putrescine accumulated in the disruptant. Purified recombinant TK0147 possessed a 78-fold-higher kcat/Km value for agmatine than for putrescine, suggesting that TK0147 functions primarily as an aminopropyl transferase to produce N1-aminopropylagmatine. In T. kodakarensis, spermidine is produced mainly from agmatine via N1-aminopropylagmatine. Furthermore, spermine and N4-aminopropylspermine were detected in the TK0147 disruptant, indicating that TK0147 does not function to produce spermine and long-chain polyamines."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.org/dc/terms/identifier"doi:10.1128/jb.00279-10"xsd:string
http://purl.uniprot.org/citations/20675472http://purl.org/dc/terms/identifier"doi:10.1128/jb.00279-10"xsd:string
http://purl.uniprot.org/citations/20675472http://purl.org/dc/terms/identifier"doi:10.1128/jb.00279-10"xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Fujiwara S."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Fujiwara S."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Imanaka T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Imanaka T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Masuda T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Masuda T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Oshima T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Oshima T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Nakajima N."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Nakajima N."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Terui Y."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Terui Y."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Kanai T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Kanai T."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Fukuda W."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Fukuda W."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Morimoto N."xsd:string
http://purl.uniprot.org/citations/20675472http://purl.uniprot.org/core/author"Morimoto N."xsd:string