Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1992-5-20
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64743,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97581,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97582,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97583,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97584,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97585,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97586,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97587,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97588,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M97589
|
pubmed:abstractText |
The structural gene for a subtilisin J from Bacillus stearothermophilus NCIMB10278 was cloned in Bacillus subtilis using pZ124 as a vector, and its nucleotide sequence was determined. The nucleotide sequence revealed only one large open reading frame, composed of 1,143 base pairs and 381 amino acid residues. A Shine-Dalgarno sequence was found 8 bp upstream from the translation start site (GTG). The deduced amino acid sequence revealed an N-terminal signal peptide and pro-peptide of 106 residues followed by the mature protein comprised of 275 residues. The productivity of subtilisin in the culture broth of the Bacillus subtilis was about 46-fold higher than that of the Bacillus stearothermophilus. The amino acid sequence of the extracellular alkaline protease subtilisin J is highly homologous to that of subtilisin E and it shows 69% identity with subtilisin Carlsberg, 89% with subtilisin BPN' and 70% with subtilisin DY. Some properties of the subtilisin J that had been purified from the Bacillus subtilis were examined. The subtilisin J has alkaline pH characteristics and a molecular weight of 27,500. It retains about 50% of its activity even after treatment at 60 degrees C for 30 min in the presence of 2 mM calcium chloride.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
184
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
277-82
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:1567435-Amino Acid Sequence,
pubmed-meshheading:1567435-Bacillus subtilis,
pubmed-meshheading:1567435-Base Sequence,
pubmed-meshheading:1567435-Cloning, Molecular,
pubmed-meshheading:1567435-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1567435-Genes, Bacterial,
pubmed-meshheading:1567435-Geobacillus stearothermophilus,
pubmed-meshheading:1567435-Molecular Sequence Data,
pubmed-meshheading:1567435-Molecular Weight,
pubmed-meshheading:1567435-Oligopeptides,
pubmed-meshheading:1567435-Recombinant Proteins,
pubmed-meshheading:1567435-Restriction Mapping,
pubmed-meshheading:1567435-Subtilisins
|
pubmed:year |
1992
|
pubmed:articleTitle |
Molecular cloning of a subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis.
|
pubmed:affiliation |
Department of Life Science, Korea Advanced Institute of Science and Technology, Taejon.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|