| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.2.-.- |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.2.1.- |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157."xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine."xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria."xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "In contrast, different enzymes are involved in the first reaction."xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2000/01/rdf-schema#comment | "In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17."xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2004/02/skos/core#prefLabel | "betaine-aldehyde dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9792097 |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12466265 |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12604197 |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12736784 |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/13192104 |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2004/02/skos/core#altLabel | "betaine aldehyde dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2004/02/skos/core#altLabel | "BADH"xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2004/02/skos/core#altLabel | "betaine aldehyde oxidase"xsd:string |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.2.1.8#SIP68A93BF619F5C7DB |
| http://purl.uniprot.org/enzyme/1.2.1.8 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.2.1.- |
| http://purl.uniprot.org/uniprot/A0AA90GSV0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.2.1.8 |
| http://purl.uniprot.org/uniprot/A0A812GU10 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.2.1.8 |
| http://purl.uniprot.org/uniprot/A0A9W4PLM7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.2.1.8 |
| http://purl.uniprot.org/uniprot/A0A090GJ20 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.2.1.8 |