http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.2.-.- |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.2.1.- |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.-.-.- |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation."xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis."xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430."xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2000/01/rdf-schema#comment | "In humans, the enzyme is a primary target for the environmental toxin Pb."xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2004/02/skos/core#prefLabel | "porphobilinogen synthase"xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7819203 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8424649 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/13276347 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22037356 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22974111 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4998716 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/5773436 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9644976 |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2004/02/skos/core#altLabel | "delta-aminolevulinic acid dehydratase"xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2004/02/skos/core#altLabel | "aminolevulinate dehydratase"xsd:string |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/4.2.1.24#SIP6BE445B099E3F57A |
http://purl.uniprot.org/enzyme/4.2.1.24 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/4.2.1.- |
http://purl.uniprot.org/uniprot/A0A924G2V5 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.24 |
http://purl.uniprot.org/uniprot/A0A947FX20 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.24 |
http://purl.uniprot.org/uniprot/A0A7Y6NES1 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.24 |