| http://purl.uniprot.org/citations/7988883 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7988883 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7988883 | http://www.w3.org/2000/01/rdf-schema#comment | "Peptidase D of Escherichia coli was overproduced from a multicopy plasmid and purified to electrophoretic homogeneity. The pure enzyme was stable at 4 degrees C or -20 degrees C and had a pH optimum at pH 9, and a pI of 4.7; the temperature optimum was at 37 degrees C. As the enzyme was activated by Co2+ and Zn2+, and deactivated by metal chelators, it appears to be a metallopeptidase. By activity staining of native gels, 11 dipeptides which are preferentially cleaved by peptidase D were identified. Peptidase D activity required dipeptide substrates with an unblocked amino terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline were not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids were hydrolyzed. Km values of 2 to 5 mM indicate a relatively poor interaction of the enzyme with its substrates."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1574-6968.1994.tb07215.x"xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1574-6968.1994.tb07215.x"xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Henrich B."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Henrich B."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Plapp R."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Plapp R."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Schroeder U."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Schroeder U."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Fink J."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/author | "Fink J."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/name | "FEMS Microbiol. Lett."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/name | "FEMS Microbiol. Lett."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/pages | "153-159"xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/pages | "153-159"xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/title | "Peptidase D of Escherichia coli K-12, a metallopeptidase of low substrate specificity."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/title | "Peptidase D of Escherichia coli K-12, a metallopeptidase of low substrate specificity."xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/volume | "123"xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://purl.uniprot.org/core/volume | "123"xsd:string |
| http://purl.uniprot.org/citations/7988883 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7988883 |
| http://purl.uniprot.org/citations/7988883 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7988883 |