| http://purl.uniprot.org/citations/7035170 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7035170 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7035170 | http://www.w3.org/2000/01/rdf-schema#comment | "Glutamate-semialdehyde dehydrogenase, catalysing the reduction in vivo of gamma-glutamyl phosphate to glutamate 5-semialdehyde in the pathway of proline biosynthesis in Escherichia coli, has been purified to homogeneity. High initial levels of the enzyme were achieved by using a multicopy ColEl-pro A, B hybrid plasmid. The protein has a molecular weight of 1.89 X 10(5) and consists of four identical subunits of molecular weight 4.7 X 10(4) each. The pH optimum is 7.0 and the protein is stable for at least 10 min between pH 6.0-9.0 and for long periods at pH 7.0 It is rapidly inactivated at temperatures greater than 50 degrees C. The enzyme is very sensitive to inhibition by p-chloro-mercuribenzoate, copper and nickel ions."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1982.tb05823.x"xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1982.tb05823.x"xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/author | "Leisinger T."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/author | "Leisinger T."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/author | "Hayzer D.J."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/author | "Hayzer D.J."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/date | "1982"xsd:gYear |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/date | "1982"xsd:gYear |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/pages | "561-565"xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/pages | "561-565"xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/title | "Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/title | "Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase."xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/volume | "121"xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://purl.uniprot.org/core/volume | "121"xsd:string |
| http://purl.uniprot.org/citations/7035170 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7035170 |
| http://purl.uniprot.org/citations/7035170 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7035170 |
| http://purl.uniprot.org/citations/7035170 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7035170 |
| http://purl.uniprot.org/citations/7035170 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7035170 |
| http://purl.uniprot.org/uniprot/P07004 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7035170 |
| http://purl.uniprot.org/uniprot/P07004#attribution-3E0E89064800F70DEC1F60E70D068C3D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7035170 |