| http://purl.uniprot.org/citations/3038538 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3038538 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3038538 | http://www.w3.org/2000/01/rdf-schema#comment | "A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986) Gene 42, 31-36], was sequenced. The gene codes for a 314-amino-acid precursor, the N-terminal region of which has the characteristics of a signal peptide. The beta-lactamase as excreted by the host strain S. lividans PD6 has a ragged N-terminus, indicating either the presence of a leader peptidase of poor specificity or the action of an aminopeptidase. The primary structure (as deduced from the nucleotide sequence) was confirmed by amino acid sequencing of a 16-residue stretch at the amino terminus of the protein, a 12-residue stretch containing the active-site serine [De Meester et al. (1987) Biochem. J. 244, 427-432] and a 23-residue stretch obtained by trypsin digestion of the protein. The beta-lactamase belongs to class A, has three half-cystine residues (one of which occurs on the amino side of the active-site serine) and is inactivated by thiol reagents. Putative ribosome binding site and terminator region were identified."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1987.tb13521.x"xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1987.tb13521.x"xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Joris B."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Joris B."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "van Beeumen J."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "van Beeumen J."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "de Meester F."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "de Meester F."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Frere J.-M."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Frere J.-M."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Dusart J."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Dusart J."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Ghuysen J.-M."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Ghuysen J.-M."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Dehottay P."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Dehottay P."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Erpicum T."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/author | "Erpicum T."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/3038538 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |