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http://purl.uniprot.org/citations/7957167http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7957167http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7957167http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/7957167http://www.w3.org/2000/01/rdf-schema#comment"5-Aminolevulinic acid for chlorophyll synthesis in greening barley is formed from glutamate. One of the steps involved in the conversion of glutamate to 5-aminolevulinic acid involves a reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde and tRNA(Glu). An enzyme catalysing this reduction was purified from the stroma of greening barley chloroplasts. An approximately 270-kDa protein composed of 54-kDa identical subunits was identified as the barley glutamyl-tRNA(Glu) reductase after purification by Sephacryl S-300, Cibacron Blue-Sepharose, 2'-5'-ADP-Sepharose, Mono S, Mini Q and Superose 12 chromatography. The sequence of 18 amino acids from the N-terminus of the reductase is 50% identical to a cDNA-deduced domain of the Arabidopsis thaliana hemA protein and encoded in a barley hemA cDNA sequence. This is an unequivocal demonstration that the glutamyl-tRNA(Glu) reductase subunit of higher plants is encoded in a hemA gene of the nuclear genome. Heme at 4 microM concentration or glutamate 1-semialdehyde at 200 microM caused a 50% inhibition of the reductase activity. Micromolar concentrations of Zn2+, Cu2+ and Cd2+ also inhibited barley glutamyl-tRNA(Glu) reductase."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1994.00529.x"xsd:string
http://purl.uniprot.org/citations/7957167http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1994.00529.x"xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/author"Kannangara C.G."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/author"Kannangara C.G."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/author"Pontoppidan B."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/author"Pontoppidan B."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/pages"529-537"xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/pages"529-537"xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/title"Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/title"Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis."xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/volume"225"xsd:string
http://purl.uniprot.org/citations/7957167http://purl.uniprot.org/core/volume"225"xsd:string
http://purl.uniprot.org/citations/7957167http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7957167
http://purl.uniprot.org/citations/7957167http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7957167
http://purl.uniprot.org/citations/7957167http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7957167
http://purl.uniprot.org/citations/7957167http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7957167
http://purl.uniprot.org/citations/7957167http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7957167