| pubmed-article:14766011 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C0001022 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C0521033 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:14766011 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:14766011 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:14766011 | pubmed:dateCreated | 2004-5-10 | lld:pubmed |
| pubmed-article:14766011 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14766011 | pubmed:abstractText | Acetyl-CoA carboxylase (ACC) catalyses the first step in fatty-acid biosynthesis. Owing to its role in primary metabolism, ACC has been exploited as a commercial herbicide target and identified as a chemically validated fungicide target. In animals, ACC is also a key regulator of fat metabolism. This function has made ACC a prime target for the development of anti-obesity and anti-Type II diabetes therapeutics. Despite its economic importance, there is a lack of published information on recombinant expression of ACC. We report here the expression of enzymically active fungal (Ustilago maydis ) ACC in Escherichia coli. The recombinant enzyme exhibited Km values of 0.14+/-0.013 mM and 0.19+/-0.041 mM for acetyl-CoA and ATP respectively, which are comparable with those reported for the endogenous enzyme. The polyketide natural product soraphen is a potent inhibitor of the BC (biotin carboxylase) domain of endogenous fungal ACC. Similarly, recombinant ACC activity was inhibited by soraphen with a K(i) of 2.1+/-0.9 nM. A truncated BC domain that included amino acids 2-560 of the full-length protein was also expressed in E. coli. The isolated BC domain was expressed to higher levels, and was more stable than full-length ACC. Although incapable of enzymic turnover, the BC domain exhibited high-affinity soraphen binding (Kd 1.1+/-0.3 nM), demonstrating a native conformation. Additional BC domains from the phytopathogenic fungi Magnaporthe grisea and Phytophthora infestans were also cloned and expressed, and were shown to exhibit high-affinity soraphen binding. Together, these reagents will be useful for structural studies and assay development. | lld:pubmed |
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| pubmed-article:14766011 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14766011 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14766011 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14766011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14766011 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14766011 | pubmed:month | May | lld:pubmed |
| pubmed-article:14766011 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:14766011 | pubmed:author | pubmed-author:WeatherlyStep... | lld:pubmed |
| pubmed-article:14766011 | pubmed:author | pubmed-author:VolrathSandra... | lld:pubmed |
| pubmed-article:14766011 | pubmed:author | pubmed-author:ElichTedd DTD | lld:pubmed |
| pubmed-article:14766011 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:14766011 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:14766011 | pubmed:volume | 380 | lld:pubmed |
| pubmed-article:14766011 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14766011 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14766011 | pubmed:pagination | 105-10 | lld:pubmed |
| pubmed-article:14766011 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:14766011 | pubmed:meshHeading | pubmed-meshheading:14766011... | lld:pubmed |
| pubmed-article:14766011 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14766011 | pubmed:articleTitle | Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain. | lld:pubmed |
| pubmed-article:14766011 | pubmed:affiliation | Cropsolution, Inc., P.O. Box 14069, Research Triangle Park, NC 27560, USA. | lld:pubmed |
| pubmed-article:14766011 | pubmed:publicationType | Journal Article | lld:pubmed |
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