| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.2.-.- |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.2.1.- |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.-.-.- |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#comment | "The alpha-subunit catalyzes the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was listed formerly as EC 4.1.2.8)."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#comment | "In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122)."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#comment | "That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#comment | "The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2000/01/rdf-schema#comment | "In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18, EC 4.1.1.48, EC 4.1.3.27 and EC 5.3.1.24."xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2004/02/skos/core#prefLabel | "tryptophan synthase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16526091 |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3053720 |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10353823 |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16590328 |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2004/02/skos/core#altLabel | "tryptophan synthetase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2004/02/skos/core#altLabel | "indoleglycerol phosphate aldolase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2004/02/skos/core#altLabel | "L-tryptophan synthetase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2004/02/skos/core#altLabel | "tryptophan desmolase"xsd:string |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/4.2.1.20#SIPA479678F2AC955CE |
| http://purl.uniprot.org/enzyme/4.2.1.20 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/4.2.1.- |
| http://purl.uniprot.org/uniprot/A0A925BNT7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.20 |
| http://purl.uniprot.org/uniprot/A0A0C2X6L0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.20 |
| http://purl.uniprot.org/uniprot/A0A975XU93 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.20 |
| http://purl.uniprot.org/uniprot/A0A964LLF7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.2.1.20 |