| http://purl.uniprot.org/citations/14766011 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14766011 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20031960"xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/author | "Elich T.D."xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/author | "Volrath S.L."xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/author | "Weatherly S.C."xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/pages | "105-110"xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/title | "Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain."xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://purl.uniprot.org/core/volume | "380"xsd:string |
| http://purl.uniprot.org/citations/14766011 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14766011 |
| http://purl.uniprot.org/citations/14766011 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14766011 |
| http://purl.uniprot.org/uniprot/#_Q13085-mappedCitation-14766011 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14766011 |
| http://purl.uniprot.org/uniprot/#_P50747-mappedCitation-14766011 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14766011 |
| http://purl.uniprot.org/uniprot/#_O00763-mappedCitation-14766011 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14766011 |
| http://purl.uniprot.org/uniprot/O00763 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14766011 |
| http://purl.uniprot.org/uniprot/Q13085 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14766011 |
| http://purl.uniprot.org/uniprot/P50747 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14766011 |