| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/2000/01/rdf-schema#comment | "alpha-Lytic protease is a 19.8-kDa protein secreted from the Gram-negative bacterium Lysobacter enzymogenes. We have cloned and sequenced the gene for this serine protease. The nucleotide sequence contains an open reading frame which codes for the 198-residue mature enzyme and a potential prepro-peptide, also of 198 residues. The COOH-terminal 49 residues of the pro-peptide are significantly homologous to the propeptides of Streptomyces griseus proteases A and B. We suggest that this pro-peptide region facilitates formation of the active enzyme. A region bridging the NH2-terminal pre- and pro-peptides is homologous to a maize inhibitor of serine proteases. We speculate that this region inhibits enzymatic activity of the prepro-enzyme."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)37430-1"xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)37430-1"xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/author | "Wensink P.C."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/author | "Wensink P.C."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/author | "Epstein D.M."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/author | "Epstein D.M."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/pages | "16586-16590"xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/pages | "16586-16590"xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/title | "The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/title | "The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes."xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/volume | "263"xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://purl.uniprot.org/core/volume | "263"xsd:string |
| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3053694 |
| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3053694 |
| http://purl.uniprot.org/citations/3053694 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3053694 |
| http://purl.uniprot.org/citations/3053694 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3053694 |
| http://purl.uniprot.org/citations/3053694 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3053694 |