Abstract
This communication explores prenyltransferase substrate binding pocket flexibility to tag and enrich isoprenoids using affinity-based purification for metabolomic studies.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / metabolism
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Binding Sites
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Dimethylallyltranstransferase / chemistry
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Dimethylallyltranstransferase / metabolism*
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Diphosphates / metabolism
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Diterpenes / metabolism
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Kinetics
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Metabolomics / methods*
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Naphthoquinones / metabolism
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Pliability
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Prenylation
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Protein Binding
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Reproducibility of Results
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Streptomyces / enzymology
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Terpenes / metabolism*
Substances
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Bacterial Proteins
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Diphosphates
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Diterpenes
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Naphthoquinones
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Terpenes
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geranyl diphosphate
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naphterpin B
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Dimethylallyltranstransferase