pubmed-article:2341042 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0995737 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C1522642 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0004793 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C1704222 | lld:lifeskim |
pubmed-article:2341042 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:2341042 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2341042 | pubmed:dateCreated | 1990-6-26 | lld:pubmed |
pubmed-article:2341042 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2341042 | pubmed:abstractText | The gene (npr) encoding an extracellular neutral metalloprotease (Npr) from Streptomyces cacaoi YM15 was cloned in Streptomyces lividans using pIJ702 as a vector. The nucleotide (nt) sequence of npr was determined. The deduced open reading frame encoded 550 amino acids (aa) (60 kDa) with a putative signal sequence of 34 aa at the N terminus. High-resolution S1 mapping identified the transcriptional start point at about 132-134 nt upstream from the start codon. The nt sequences at both -10 and -35 regions resemble the consensus sequence of typical Escherichia coli promoters and a fragment containing the promoter was functional in an E. coli promoter probe plasmid. In vitro transcription and translation of the cloned npr sequence revealed a 60-kDa protein product, correlated with the sequence data but not with the size (35 kDa) of the extracellular Npr. The N-terminal aa sequence in conjunction with the aa composition analyses on the purified mature Npr led to the conclusion that it was processed from the 60-kDa pre-proenzyme form encoded by npr. The Npr protease contained putative zinc ligand-binding regions and two repeated motifs, Asp-Ser-Gly, similar to the active site residues of the aspartic acid and retroviral proteases. | lld:pubmed |
pubmed-article:2341042 | pubmed:language | eng | lld:pubmed |
pubmed-article:2341042 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2341042 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2341042 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2341042 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2341042 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2341042 | pubmed:month | Mar | lld:pubmed |
pubmed-article:2341042 | pubmed:issn | 0378-1119 | lld:pubmed |
pubmed-article:2341042 | pubmed:author | pubmed-author:YenL CLC | lld:pubmed |
pubmed-article:2341042 | pubmed:author | pubmed-author:TsugitaAA | lld:pubmed |
pubmed-article:2341042 | pubmed:author | pubmed-author:ChangP CPC | lld:pubmed |
pubmed-article:2341042 | pubmed:author | pubmed-author:KuoT CTC | lld:pubmed |
pubmed-article:2341042 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2341042 | pubmed:day | 30 | lld:pubmed |
pubmed-article:2341042 | pubmed:volume | 88 | lld:pubmed |
pubmed-article:2341042 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2341042 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2341042 | pubmed:pagination | 87-95 | lld:pubmed |
pubmed-article:2341042 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:2341042 | pubmed:meshHeading | pubmed-meshheading:2341042-... | lld:pubmed |
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pubmed-article:2341042 | pubmed:meshHeading | pubmed-meshheading:2341042-... | lld:pubmed |
pubmed-article:2341042 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2341042 | pubmed:articleTitle | Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product. | lld:pubmed |
pubmed-article:2341042 | pubmed:affiliation | Institute of Biochemistry, National Yang-Ming Medical College, Taipei, Taiwan. | lld:pubmed |
pubmed-article:2341042 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2341042 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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