| pubmed-article:10930733 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C1081565 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0005740 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0039859 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:10930733 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10930733 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10930733 | pubmed:dateCreated | 2000-9-12 | lld:pubmed |
| pubmed-article:10930733 | pubmed:abstractText | We have previously proposed that the BlmIV and BlmIII non-ribosomal peptide synthetases are involved in the formation of the bithiazole moiety of the anti-tumor drug bleomycin in Streptomyces verticillus ATCC15003. We report here the identification and characterization of an oxidation domain in BlmIII. The oxidation domain shows local homology to a family of oxidoreductases and is present in all thiazole-forming non-ribosomal peptide synthetase modules known to date. Both the blmIII-Ox domain and blmIII gene were expressed in Escherichia coli, and the resulting BlmIII-Ox and BlmIII proteins were purified to homogeneity. The oxidation domain contains one molar equivalent of non-covalently bound FMN as a prosthetic group. These results provide experimental evidence for an oxidation domain within non-ribosomal peptide synthetases, suggesting that BlmIII-Ox probably catalyzes the thiazoline to thiazole oxidation in bleomycin biosynthesis. | lld:pubmed |
| pubmed-article:10930733 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10930733 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10930733 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10930733 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10930733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10930733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10930733 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10930733 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10930733 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10930733 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:10930733 | pubmed:author | pubmed-author:ChenMM | lld:pubmed |
| pubmed-article:10930733 | pubmed:author | pubmed-author:SánchezCC | lld:pubmed |
| pubmed-article:10930733 | pubmed:author | pubmed-author:SheaMM | lld:pubmed |
| pubmed-article:10930733 | pubmed:author | pubmed-author:FRYJ FJF | lld:pubmed |
| pubmed-article:10930733 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10930733 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10930733 | pubmed:volume | 189 | lld:pubmed |
| pubmed-article:10930733 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10930733 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10930733 | pubmed:pagination | 171-5 | lld:pubmed |
| pubmed-article:10930733 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:meshHeading | pubmed-meshheading:10930733... | lld:pubmed |
| pubmed-article:10930733 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10930733 | pubmed:articleTitle | An oxidation domain in the BlmIII non-ribosomal peptide synthetase probably catalyzing thiazole formation in the biosynthesis of the anti-tumor drug bleomycin in Streptomyces verticillus ATCC15003. | lld:pubmed |
| pubmed-article:10930733 | pubmed:affiliation | Department of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA. | lld:pubmed |
| pubmed-article:10930733 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10930733 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10930733 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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