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Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases.
Abstract : Cyclodipeptide synthases form cyclodipeptides from two aminoacyl transfer RNAs. They use a ping-pong mechanism that begins with transfer of the aminoacyl moiety of the first aminoacyl tRNA onto a conserved serine, yielding an aminoacyl enzyme. Combining X-ray crystallography, site-directed mutagenesis and affinity labelling of the cyclodipeptide synthase AlbC, we demonstrate that the covalent intermediate reacts with the aminoacyl moiety of the second aminoacyl tRNA, forming a dipeptidyl enzyme, and identify the aminoacyl-binding sites of the aminoacyl tRNAs.
Cited literature [29 references]
https://hal-polytechnique.archives-ouvertes.fr/hal-01098814
Contributor : Denis Roura <>
Submitted on : Monday, November 2, 2015 - 5:27:13 PM
Last modification on : Wednesday, July 29, 2020 - 4:10:05 PM
Long-term archiving on: : Friday, April 28, 2017 - 6:10:54 AM
Contributor : Denis Roura <>
Submitted on : Monday, November 2, 2015 - 5:27:13 PM
Last modification on : Wednesday, July 29, 2020 - 4:10:05 PM
Long-term archiving on: : Friday, April 28, 2017 - 6:10:54 AM
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