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http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.-.-.-
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.4.1.-
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.4.-.-
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#comment"The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia."xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#comment"A pyridoxal 5'-phosphate protein."xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#comment"The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions."xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2000/01/rdf-schema#comment"While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases."xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#prefLabel"cysteine-S-conjugate beta-lyase"xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17191898
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/14209950
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12137566
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12504794
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16463021
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3782077
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4008484
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/721818
http://purl.uniprot.org/enzyme/4.4.1.13http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7612304
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#altLabel"cystathionine beta-lyase"xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#altLabel"L-cysteine-S-conjugate thiol-lyase (deaminating)"xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#altLabel"S-alkyl-L-cysteine lyase"xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#altLabel"S-alkyl-L-cysteine sulfoxide lyase"xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#altLabel"S-alkylcysteinase"xsd:string
http://purl.uniprot.org/enzyme/4.4.1.13http://www.w3.org/2004/02/skos/core#altLabel"S-alkylcysteine lyase"xsd:string