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http://purl.uniprot.org/citations/10594185http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10594185http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10594185http://www.w3.org/2000/01/rdf-schema#comment"The most comprehensive studies on a plant lysozyme (EC 3.2.1.17) are those on the enzyme from papaya (Carica papaya) latex, published in 1967 and 1969. However, the N-terminal amino acid sequence of five amino acid sequence of this enzyme, determined by manual Edman degradation, did not allow assignment to any of the much later-classified families of glycosyl hydrolases. N-Terminal sequence analysis of 22 residues of papaya lysozyme now shows unambiguously that the enzyme belongs to the family 19 chitinases. It has properties similar to those of basic class I chitinases with lysozyme activity, such as cleavage specificity at the C-1 of N-acetylmuramic acid with inversion of configuration, but as it lacks an N-terminal hevein domain, it should be classified as a class II chitinase."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.org/dc/terms/identifier"doi:10.1007/pl00000075"xsd:string
http://purl.uniprot.org/citations/10594185http://purl.org/dc/terms/identifier"doi:10.1007/pl00000075"xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/author"Beintema J.J."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/author"Beintema J.J."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/author"Subroto T."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/author"Subroto T."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/author"Sufiati S."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/author"Sufiati S."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/name"J. Mol. Evol."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/name"J. Mol. Evol."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/pages"819-821"xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/pages"819-821"xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/title"Papaya (Carica papaya) lysozyme is a member of the family 19 (basic, class II) chitinases."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/title"Papaya (Carica papaya) lysozyme is a member of the family 19 (basic, class II) chitinases."xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/volume"49"xsd:string
http://purl.uniprot.org/citations/10594185http://purl.uniprot.org/core/volume"49"xsd:string
http://purl.uniprot.org/citations/10594185http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10594185
http://purl.uniprot.org/citations/10594185http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10594185
http://purl.uniprot.org/citations/10594185http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10594185
http://purl.uniprot.org/citations/10594185http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10594185