| pubmed-article:12904561 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0086948 | lld:lifeskim |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0071598 | lld:lifeskim |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:12904561 | lifeskim:mentions | umls-concept:C0076464 | lld:lifeskim |
| pubmed-article:12904561 | pubmed:issue | Pt 8 | lld:pubmed |
| pubmed-article:12904561 | pubmed:dateCreated | 2003-8-7 | lld:pubmed |
| pubmed-article:12904561 | pubmed:abstractText | Bacterial modular polyketide synthase (PKS) genes are commonly associated with another gene that encodes a thioesterase II (TEII) believed to remove aberrantly loaded substrates from the PKS. Co-expression of the Saccharopolyspora erythraea ery-ORF5 TEII and eryA genes encoding 6-deoxyerythronolide B synthase (DEBS) in Streptomyces hosts eliminated or significantly lowered production of 8,8'-deoxyoleandolide [15-nor-6-deoxyerythronolide B (15-nor-6dEB)], which arises from an acetate instead of a propionate starter unit. Disruption of the TEII gene in an industrial Sac. erythraea strain caused a notable amount of 15-norerythromycins to be produced by utilization of an acetate instead of a propionate starter unit and also resulted in moderately lowered production of erythromycin compared with the amount produced by the parental strain. A similar behaviour of the TEII gene was observed in Escherichia coli strains that produce 6dEB and 15-methyl-6dEB. Direct biochemical analysis showed that the ery-ORF5 TEII enzyme favours hydrolysis of acetyl groups bound to the loading acyl carrier protein domain (ACP(L)) of DEBS. These results point to a clear role of the TEII enzyme, i.e. removal of a specific type of acyl group from the ACP(L) domain of the DEBS1 loading module. | lld:pubmed |
| pubmed-article:12904561 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12904561 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12904561 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12904561 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12904561 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12904561 | pubmed:issn | 1350-0872 | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:AshleyGaryG | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:KhoslaChaitan... | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:CarneyJohn... | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:ChaoElizabeth... | lld:pubmed |
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| pubmed-article:12904561 | pubmed:author | pubmed-author:HutchinsonC... | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:HuZhihaoZ | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:MurliSumatiS | lld:pubmed |
| pubmed-article:12904561 | pubmed:author | pubmed-author:KealeyJimJ | lld:pubmed |
| pubmed-article:12904561 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12904561 | pubmed:volume | 149 | lld:pubmed |
| pubmed-article:12904561 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12904561 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12904561 | pubmed:pagination | 2213-25 | lld:pubmed |
| pubmed-article:12904561 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12904561 | pubmed:meshHeading | pubmed-meshheading:12904561... | lld:pubmed |
| pubmed-article:12904561 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12904561 | pubmed:articleTitle | A specific role of the Saccharopolyspora erythraea thioesterase II gene in the function of modular polyketide synthases. | lld:pubmed |
| pubmed-article:12904561 | pubmed:affiliation | Kosan Biosciences, Hayward, CA 94545, USA. hu@kosan.com | lld:pubmed |
| pubmed-article:12904561 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12904561 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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