| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.4.1.- |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.4.-.- |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#comment | "It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyzes spontaneously to form oxaloacetate."xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme is strictly specific for L-aspartate as substrate."xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC 2.5.1.72 preventing its hydrolysis and enabling the de novo biosynthesis of NAD(+)."xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2004/02/skos/core#prefLabel | "aspartate dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16731057 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17651440 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12496312 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/21468714 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/21821928 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22120624 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9819709 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2004/02/skos/core#altLabel | "NAD-dependent aspartate dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2004/02/skos/core#altLabel | "NADH2-dependent aspartate dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2004/02/skos/core#altLabel | "NADP(+)-dependent aspartate dehydrogenase"xsd:string |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.4.1.21#SIP080E68F182F0590B |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.4.1.21#SIP770875BD86742830 |
| http://purl.uniprot.org/enzyme/1.4.1.21 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.4.1.- |
| http://purl.uniprot.org/uniprot/A0A929KIU6 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.4.1.21 |
| http://purl.uniprot.org/uniprot/A0A8T5R4B9 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.4.1.21 |
| http://purl.uniprot.org/uniprot/A0A8I1TES4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.4.1.21 |