Source:http://linkedlifedata.com/resource/pubmed/id/21456513
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2011-4-29
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pubmed:abstractText |
TrdL, encoding a flavin-dependent oxidoreductase in the tirandamycin gene cluster, was inactivated to afford a ?trdL mutant, the fermentation of which yielded a new intermediate, tirandamycin E (5), and an additional early intermediate, tirandamycin F (6), if XAD-16 resin was introduced. TrdL was overexpressed in E. coli, and the protein was shown to efficiently catalyze the transformations from 5 to tirandamycin A (1) and from 6 to tirandamycin D (4), demonstrating its function as a 10-hydroxy dehydrogenase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1523-7052
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
6
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2212-5
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pubmed:meshHeading |
pubmed-meshheading:21456513-Aminoglycosides,
pubmed-meshheading:21456513-Biocatalysis,
pubmed-meshheading:21456513-Molecular Structure,
pubmed-meshheading:21456513-Mutation,
pubmed-meshheading:21456513-Oxidoreductases,
pubmed-meshheading:21456513-Streptomyces,
pubmed-meshheading:21456513-Substrate Specificity
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pubmed:year |
2011
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pubmed:articleTitle |
Characterization of TrdL as a 10-hydroxy dehydrogenase and generation of new analogues from a tirandamycin biosynthetic pathway.
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pubmed:affiliation |
CAS Key Laboratory of Marine Bio-resources Sustainable Utilization, RNAM Center for Marine Microbiology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, 164 West Xingang Road, Guangzhou 510301, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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