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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1998-2-18
|
| pubmed:abstractText |
During the screening for tyrosine phenol-lyase-producing thermophiles, we isolated an obligatory symbiotic thermophile, Symbiobacterium sp. SC-1, which grew only in coculture with Bacillus sp. SK-1. A gene encoding thermostable tyrosine phenol-lyase (TPL) was cloned from the genomic DNA of the Symbiobacterium sp. SC-1 and the nucleotide sequence of the TPL structural gene was determined. The gene consists of 1374 base pairs encoding a polypeptide of 458 amino acid residues; the molecular mass of the enzyme subunit is estimated to be 52,196 Da. The structural gene of TPL was amplified by PCR, blunt-ended, and ligated into the NcoI-HindIII site of plasmid pTrc99A to construct an expression vector for the overproduction of the thermostable TPL. The level of thermostable TPL production was about 15% of the total soluble proteins of Escherichia coli extract. The enzyme was purified to homogeneity from the E. coli extract with an overall yield of 48%.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
1046-5928
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
11
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
263-70
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:9425630-Amino Acid Sequence,
pubmed-meshheading:9425630-Bacillus,
pubmed-meshheading:9425630-Bacteria,
pubmed-meshheading:9425630-Base Sequence,
pubmed-meshheading:9425630-Cloning, Molecular,
pubmed-meshheading:9425630-Conserved Sequence,
pubmed-meshheading:9425630-Enzyme Stability,
pubmed-meshheading:9425630-Escherichia coli,
pubmed-meshheading:9425630-Genes, Bacterial,
pubmed-meshheading:9425630-Hot Temperature,
pubmed-meshheading:9425630-Kinetics,
pubmed-meshheading:9425630-Molecular Sequence Data,
pubmed-meshheading:9425630-Molecular Weight,
pubmed-meshheading:9425630-Plasmids,
pubmed-meshheading:9425630-Recombinant Proteins,
pubmed-meshheading:9425630-Restriction Mapping,
pubmed-meshheading:9425630-Sequence Alignment,
pubmed-meshheading:9425630-Sequence Homology, Amino Acid,
pubmed-meshheading:9425630-Thermodynamics,
pubmed-meshheading:9425630-Tyrosine Phenol-Lyase
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Thermostable tyrosine phenol-lyase of Symbiobacterium sp. SC-1: gene cloning, sequence determination, and overproduction in Escherichia coli.
|
| pubmed:affiliation |
Microbial Conversion RU, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Yusong, Taejon, Korea.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|