http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.2.-.- |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.2.1.- |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#comment | "(S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde."xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate."xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#comment | "In many bacterial species, both activities are carried out by a single bifunctional enzyme."xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#comment | "NADP(+) can also act as acceptor, but with lower activity."xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme catalyzes the irreversible oxidation of glutamate-gamma-semialdehyde to glutamate as part of the proline degradation pathway."xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2004/02/skos/core#prefLabel | "L-glutamate gamma-semialdehyde dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1618807 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17554163 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12223682 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/13681370 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2004/02/skos/core#altLabel | "pyrroline-5-carboxylate dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2004/02/skos/core#altLabel | "1-pyrroline-5-carboxylate dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2004/02/skos/core#altLabel | "Delta(1)-pyrroline-5-carboxylate dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/1.5.1.12 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.2.1.88#SIP2A03C1C3D00FDA60 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.2.1.88#SIP1D8904EC556588F9 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.2.1.88#SIP94E8EAE22A2460C9 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.2.1.88#SIPC20E38239F74F063 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.2.1.88#SIPD1DDCF05D677DC45 |
http://purl.uniprot.org/enzyme/1.2.1.88 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.2.1.- |