G
Gareth A. Roberts
Researcher at University of Cambridge
Publications - 9
Citations - 1278
Gareth A. Roberts is an academic researcher from University of Cambridge. The author has contributed to research in topics: Saccharopolyspora erythraea & Polyketide synthase. The author has an hindex of 8, co-authored 9 publications receiving 1262 citations. Previous affiliations of Gareth A. Roberts include National Institute for Medical Research.
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Journal ArticleDOI
An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea.
TL;DR: A novel organization of the erythromycin-producing polyketide synthase is revealed, which provides further insight into the mechanism of chain assembly.
Journal ArticleDOI
Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage
Jesus Cortes,Kirsten E. H. Wiesmann,Gareth A. Roberts,Murray J. B. Brown,James Staunton,Peter F. Leadlay +5 more
TL;DR: The 6-deoxyerythronolide B synthase of Saccharopolyspora erythraea has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain extension.
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Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases.
Stephen F. Haydock,James A. Dowson,Namrita Dhillon,Gareth A. Roberts,Jesus Cortes,Peter F. Leadlay +5 more
TL;DR: Comparison of the amino acid sequence of EryG with the sequence of other S-adenosylmethionine (SAM)-dependent methyltransferases has revealed that one of the sequence motifs previously suggested to be part of the SAM-binding site is present not only in EyG but also in many other recently sequenced SAM-dependent methyl transferases.
Journal ArticleDOI
Evidence for a double-helical structure for modular polyketide synthases
James Staunton,Patrick Caffrey,Jesús F. Aparicio,Gareth A. Roberts,Susanne S. Bethell,Peter F. Leadlay +5 more
TL;DR: It is shown here that each multi-enzyme in a typical modular polyketide synthase forms a (possibly helical) parallel dimer, and that each pair of identical modules interacts closely across the dimer interface.
Journal ArticleDOI
Heterologous expression in Escherichia coli of an intact multienzyme component of the erythromycin-producing polyketide synthase
TL;DR: 6-Deoxyerythronolide B synthase 3 was purified from extracts of the recombinant E. coli to apparent homogeneity, and was found not to be modified by covalent attachment of the prosthetic group 4'-phosphopantetheine.