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J. Staunton

Researcher at University of Cambridge

Publications -  6
Citations -  300

J. Staunton is an academic researcher from University of Cambridge. The author has contributed to research in topics: Polyketide synthase & Saccharopolyspora erythraea. The author has an hindex of 6, co-authored 6 publications receiving 289 citations.

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Active-site residue, domain and module swaps in modular polyketide synthases

TL;DR: A cassette system for convenient construction of hybrid modular PKSs based on the tylosin PKS in Streptomyces fradiae is described and its use in domain and module swaps is demonstrated.
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Engineering of complex polyketide biosynthesis — insights from sequencing of the monensin biosynthetic gene cluster

TL;DR: The sequencing of the genes for the biosynthesis of monensin A, a typical polyether ionophore polyketide, provided the first genetic evidence for the mechanism of oxidative cyclisation through which polyethers such as monens in are formed from the uncyclised products of the PKS.
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Engineering of a minimal modular polyketide synthase, and targeted alteration of the stereospecificity of polyketide chain extension

TL;DR: These results demonstrate that, as predicted, even a single-module PKS is catalytically active in the absence of other DEBS proteins, and indicates how targeted alteration of stereospecificity can be achieved on a modular PKS.
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Purification and separation of holo- and apo-forms of Saccharopolyspora erythraea acyl-carrier protein released from recombinant Escherichia coli by freezing and thawing

TL;DR: Electrospray mass spectrometry was used to confirm that the recombinant S. erythraea acyl-carrier protein over-expressed in E. coli can be selectively released from the cells in near-quantitative yield by a single cycle of freezing and thawing in a neutral buffer.
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Mutagenesis of the dehydratase active site in the erythromycin-producing polyketide synthase

TL;DR: It is proposed that during macrolactone biosynthesis a different set of activities is requid to cany out each of the six cycles of chain extension and (where appropriate) reduction, with each polypeptide housing the activities necessary for 2 cycles of polyketide chain extension.