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http://purl.uniprot.org/citations/11501754http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11501754http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11501754http://www.w3.org/2000/01/rdf-schema#comment"The chlorophyll synthase gene from oat (Avena sativa) was cloned and expressed in Escherichia coli. The deduced amino acid sequence consists of 378 amino acids including a presequence of 46 amino acids. Deletion mutants show that a core protein comprising amino acid residues 88 to 377 is enzymatically active. The sequence of the mature protein shows 85% identity with the chlorophyll synthase of Arabidopsis thaliana and 62% identity with the chlorophyll synthase of Synechocystis PCC 6803. The gene is constitutively expressed as the same transcript level is found in dark-grown and in light-grown seedlings. The enzyme requires magnesium ions for activity; manganese ions can reconstitute only part of the activity. Diacetyl and N-phenylmaleimide (NPM) inhibit the enzyme activity. Site-directed mutagenesis reveals that, out of the 4 Arg residues present in the active core protein, Arg-91 and Arg-161 are essential for the activity. Five cysteine residues are present in the core protein, of which only Cys-109 is essential for the enzyme activity. Since the wild-type and all other Cys-mutants with the exception of the mutant C304A are inhibited by N-phenylmaleimide, we conclude that the inhibitor binds to a non-essential Cys residue to abolish activity. The role of the various Arg and Cys residues is discussed."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.org/dc/terms/identifier"doi:10.1515/bc.2001.112"xsd:string
http://purl.uniprot.org/citations/11501754http://purl.org/dc/terms/identifier"doi:10.1515/bc.2001.112"xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Ruediger W."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Ruediger W."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Oster U."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Oster U."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Koegel J."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Koegel J."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Lenz S."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Lenz S."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Schmid H.C."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/author"Schmid H.C."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/name"Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/name"Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/pages"903-911"xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/pages"903-911"xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/title"Cloning and characterisation of chlorophyll synthase from Avena sativa."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/title"Cloning and characterisation of chlorophyll synthase from Avena sativa."xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/volume"382"xsd:string
http://purl.uniprot.org/citations/11501754http://purl.uniprot.org/core/volume"382"xsd:string