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Specificity of the Ester Bond-Forming Condensation Enzyme SgcC5 in C-1027 Biosynthesis
[Image: see text] The SgcC5 condensation enzyme catalyzes the attachment of SgcC2-tethered (S)-3-chloro-5-hydroxy-β-tyrosine (2) to the enediyne core in C-1027 (1) biosynthesis. It is reported that SgcC5 (i) exhibits high stereospecificity towards the (S)-enantiomers of SgcC2-tethered β-tyrosine and...
Tallennettuna:
| Päätekijät: | , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2012
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3345089/ https://ncbi.nlm.nih.gov/pubmed/22519717 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ol300720s |
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