Source:http://linkedlifedata.com/resource/pubmed/id/20662933
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions |
umls-concept:C0007292,
umls-concept:C0017258,
umls-concept:C0017337,
umls-concept:C0071598,
umls-concept:C0118631,
umls-concept:C0220781,
umls-concept:C0443299,
umls-concept:C0597295,
umls-concept:C1004764,
umls-concept:C1314939,
umls-concept:C1514562,
umls-concept:C1706276,
umls-concept:C1708726,
umls-concept:C1826528,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
1
|
pubmed:dateCreated |
2010-8-11
|
pubmed:abstractText |
Galbonolides A and B are antifungal compounds, which are produced by Streptomyces galbus. A multimodular polyketide synthase (PKS) was predicted to catalyze their biosynthesis, and a methoxymalonyl-acyl carrier protein (methoxymalonyl-ACP) was expected to be involved in the biosynthesis of galbonolide A. Cloning of a methoxymalonyl-ACP biosynthesis locus (galGHIJK) and the flanking regions has revealed that the locus is colocalized with beta-ketoacyl synthase (KAS)-related genes (orf3, 4, and 5), but separated from any multimodular PKS gene cluster in S. galbus. A galI-disruption mutant (SK-galI-5) is unable to produce galbonolide A, but can synthesize galbonolide B, indicating that galGHIJK is involved in the biosynthesis of galbonolide A. A disruption mutant of orf4 is severely impaired in the production of both galbonolides A and B. These results indicate that galGHIJK and the KAS genes are involved in the biosynthesis of galbonolides, although they are not colocalized with a multimodular PKS gene cluster. We further propose that a single galbonolide PKS generates two discrete structures, galbonolides A and B, by alternatively incorporating methoxymalonate and methylmalonate, respectively.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Carrier Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Antifungal Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Lactones,
http://linkedlifedata.com/resource/pubmed/chemical/Polyketide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/neorustmicin A,
http://linkedlifedata.com/resource/pubmed/chemical/rustmicin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
1574-6968
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
1
|
pubmed:volume |
310
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
69-75
|
pubmed:meshHeading |
pubmed-meshheading:20662933-Acyl Carrier Protein,
pubmed-meshheading:20662933-Antifungal Agents,
pubmed-meshheading:20662933-Biosynthetic Pathways,
pubmed-meshheading:20662933-Cloning, Molecular,
pubmed-meshheading:20662933-Gene Deletion,
pubmed-meshheading:20662933-Gene Order,
pubmed-meshheading:20662933-Lactones,
pubmed-meshheading:20662933-Models, Biological,
pubmed-meshheading:20662933-Multigene Family,
pubmed-meshheading:20662933-Mutagenesis, Insertional,
pubmed-meshheading:20662933-Polyketide Synthases,
pubmed-meshheading:20662933-Streptomyces
|
pubmed:year |
2010
|
pubmed:articleTitle |
The methoxymalonyl-acyl carrier protein biosynthesis locus and the nearby gene with the beta-ketoacyl synthase domain are involved in the biosynthesis of galbonolides in Streptomyces galbus, but these loci are separate from the modular polyketide synthase gene cluster.
|
pubmed:affiliation |
Department of Biological Science, Division of Bioscience and Bioinformatics, Myongji University, San 38-2 Nam-dong, Yongin-si, Gyunggi-do, Korea.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|