Source:http://linkedlifedata.com/resource/pubmed/id/16337147
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
2005-12-19
|
pubmed:abstractText |
The amino acid residues serine at position 213 (S213) and lysine at position 218 (K218), which are present in close proximity to the histidine-rich motif II of Mucor rouxii fatty acid Delta(6)-desaturase isoform II, were targeted for studying structure-function relationships using site-directed mutagenesis. The mutants were functionally characterized in a heterologous host, Saccharomyces cerevisiae. Substrate specificity and preference studies revealed that S213 and K218 are involved in substrate recognition. K218 plays a role in substrate preference by involvement in the binding of substrates, particularly C15-C18 monoene fatty acids. Modification of the M. rouxii Delta(6)-desaturase therefore has potential in specifically altering substrate utilization for production of desired fatty acids.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
339
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1029-34
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:16337147-Amino Acid Sequence,
pubmed-meshheading:16337147-Amino Acid Substitution,
pubmed-meshheading:16337147-Computer Simulation,
pubmed-meshheading:16337147-Enzyme Activation,
pubmed-meshheading:16337147-Fatty Acids,
pubmed-meshheading:16337147-Gene Targeting,
pubmed-meshheading:16337147-Histidine,
pubmed-meshheading:16337147-Linoleoyl-CoA Desaturase,
pubmed-meshheading:16337147-Models, Molecular,
pubmed-meshheading:16337147-Molecular Sequence Data,
pubmed-meshheading:16337147-Mucor,
pubmed-meshheading:16337147-Mutagenesis, Site-Directed,
pubmed-meshheading:16337147-Recombinant Proteins,
pubmed-meshheading:16337147-Saccharomyces cerevisiae,
pubmed-meshheading:16337147-Sequence Homology, Amino Acid,
pubmed-meshheading:16337147-Structure-Activity Relationship,
pubmed-meshheading:16337147-Substrate Specificity
|
pubmed:year |
2006
|
pubmed:articleTitle |
Targeted mutagenesis of a fatty acid Delta6-desaturase from Mucor rouxii: role of amino acid residues adjacent to histidine-rich motif II.
|
pubmed:affiliation |
School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|