| pubmed-article:8920189 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0995754 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0079429 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0038599 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:8920189 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:8920189 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:8920189 | pubmed:dateCreated | 1997-1-2 | lld:pubmed |
| pubmed-article:8920189 | pubmed:abstractText | Amino-terminal degradation has been observed for many of the secreted heterologous proteins produced by S. lividans 66. We, therefore, set out to characterize the relevant proteinases and their genes. A tripeptide chromogenic substrate was used to identify a gene that was shown to encode a secreted protein which removed tripeptides from the amino terminus of extracellular proteins (tripeptidyl aminopeptidase, Tap; Butler et al. 1995). This activity was removed by a homologous gene deletion replacement and the ability of the S. lividans strain to remove N-terminal tripeptides was greatly reduced, but still significant. When the tap-deleted strain was used as a host for the rescreening of a S. lividans 66 genomic DNA library, a number of other genes encoding proteases with aminopeptidase activities were discovered. One clone (P5-4) produced a 45-kDa secreted protein (Ssp), which showed activity against Ala-Pro-Ala-beta-naphthylamide (APA-beta NH-Nap) substrate. Further analysis of the cloned DNA showed an open-reading frame encoding a protein larger than 45 kDa. Direct Edman degradation of the secreted protein confirmed that it was encoded within the cloned DNA and probably processed from a larger precursor. Protein sequence analysis revealed a striking homology to subtilisin BPN' in three regions around the active-site residues suggesting that the protein is a serine protease. As expected, the protease activity was inhibited by phenylmethylsulphonyl fluoride. Mutant strains with most of the ssp gene deleted exhibited reduced activity against APA-beta NH-Nap substrate compared to their non-deleted parental strains. | lld:pubmed |
| pubmed-article:8920189 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8920189 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920189 | pubmed:citationSubset | B | lld:pubmed |
| pubmed-article:8920189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8920189 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8920189 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8920189 | pubmed:issn | 0175-7598 | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:SolterDD | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:MalekL TLT | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:ButlerM JMJ | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:BinnieCC | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:WalczykEE | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:KrygsmanPP | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:AphaleJ SJS | lld:pubmed |
| pubmed-article:8920189 | pubmed:author | pubmed-author:DiZonnoM AMA | lld:pubmed |
| pubmed-article:8920189 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8920189 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:8920189 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8920189 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8920189 | pubmed:pagination | 141-7 | lld:pubmed |
| pubmed-article:8920189 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:meshHeading | pubmed-meshheading:8920189-... | lld:pubmed |
| pubmed-article:8920189 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8920189 | pubmed:articleTitle | Cloning and analysis of a gene from Streptomyces lividans 66 encoding a novel secreted protease exhibiting homology to subtilisin BPN'. | lld:pubmed |
| pubmed-article:8920189 | pubmed:affiliation | Cangene Corporation, Mississauga, Ontario, Canada. | lld:pubmed |
| pubmed-article:8920189 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8920189 | pubmed:publicationType | Comparative Study | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8920189 | lld:pubmed |
