scholarly journals The polyketide backbone of thiolactomycin is assembled by an unusual iterative polyketide synthase

2017 ◽  
Vol 53 (13) ◽  
pp. 2182-2185 ◽  
Author(s):  
Marie E. Yurkovich ◽  
Robert Jenkins ◽  
Yuhui Sun ◽  
Manuela Tosin ◽  
Peter F. Leadlay
Keyword(s):  
Polyketide Synthase ◽  
Chemical Probes ◽  
Iterative Polyketide Synthase

Thiotetronate polyketide assembly by an unusual iterative synthase is reconstructed via in vitro enzymology and chemical probes.

scholarly journals Complete Reconstitution of a Highly Reducing Iterative Polyketide Synthase

Science ◽  
2009 ◽  
Vol 326 (5952) ◽  
pp. 589-592 ◽  
Author(s):  
S. M. Ma ◽  
J. W.-H. Li ◽  
J. W. Choi ◽  
H. Zhou ◽  
K. K. M. Lee ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Iterative Polyketide Synthase

Probing the Flexibility of an Iterative Modular Polyketide Synthase with Non-Native Substrates in Vitro

2018 ◽  
Vol 13 (8) ◽  
pp. 2261-2268 ◽  
Author(s):  
Samuel C. Curran ◽  
Andrew Hagen ◽  
Sean Poust ◽  
Leanne Jade G. Chan ◽  
Brett M. Garabedian ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Modular Polyketide Synthase

scholarly journals Biosynthesis of Aliphatic Polyketides by Type III Polyketide Synthase and Methyltransferase in Bacillus subtilis

2009 ◽  
Vol 191 (15) ◽  
pp. 4916-4923 ◽  
Author(s):  
Chiaki Nakano ◽  
Hiroki Ozawa ◽  
Genki Akanuma ◽  
Nobutaka Funa ◽  
Sueharu Horinouchi
Keyword(s):  
Bacillus Subtilis ◽  
Polyketide Synthase ◽  
Bacterial Genome ◽  
Fatty Acyl ◽  
Gram Positive ◽  
Type Iii Polyketide Synthase ◽  
Type Iii ◽  
Vitro Analysis

ABSTRACT Type III polyketide synthases (PKSs) synthesize a variety of aromatic polyketides in plants, fungi, and bacteria. The bacterial genome projects predicted that probable type III PKS genes are distributed in a wide variety of gram-positive and -negative bacteria. The gram-positive model microorganism Bacillus subtilis contained the bcsA-ypbQ operon, which appeared to encode a type III PKS and a methyltransferase, respectively. Here, we report the characterization of bcsA (renamed bpsA, for Bacillus pyrone synthase, on the basis of its function) and ypbQ, which are involved in the biosynthesis of aliphatic polyketides. In vivo analysis demonstrated that BpsA was a type III PKS catalyzing the synthesis of triketide pyrones from long-chain fatty acyl-coenzyme A (CoA) thioesters as starter substrates and malonyl-CoA as an extender substrate, and YpbQ was a methyltransferase acting on the triketide pyrones to yield alkylpyrone methyl ethers. YpbQ thus was named BpsB because of its functional relatedness to BpsA. In vitro analysis with histidine-tagged BpsA revealed that it used broad starter substrates and produced not only triketide pyrones but also tetraketide pyrones and alkylresorcinols. Although the aliphatic polyketides were expected to localize in the membrane and play some role in modulating the rigidity and properties of the membrane, no detectable phenotypic changes were observed for a B. subtilis mutant containing a whole deletion of the bpsA-bpsB operon.

scholarly journals Interrogation of Global Active Site Occupancy of a Fungal Iterative Polyketide Synthase Reveals Strategies for Maintaining Biosynthetic Fidelity

2012 ◽  
Vol 134 (15) ◽  
pp. 6865-6877 ◽  
Author(s):  
Anna L. Vagstad ◽  
Stefanie B. Bumpus ◽  
Katherine Belecki ◽  
Neil L. Kelleher ◽  
Craig A. Townsend
Keyword(s):  
Active Site ◽  
Polyketide Synthase ◽  
Site Occupancy ◽  
Iterative Polyketide Synthase

scholarly journals In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase

2017 ◽  
Vol 53 (10) ◽  
pp. 1727-1730 ◽  
Author(s):  
Emma Liddle ◽  
Alan Scott ◽  
Li-Chen Han ◽  
David Ivison ◽  
Thomas J. Simpson ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Kinetic Study ◽  
Fatty Acid Synthase ◽  
Polyketide Synthase ◽  
Substrate Selectivity ◽  
Dh Domain

The substrate selectivity of the isolated dehydratase (DH) domain of a fungal highly-reducing polyketide synthase is closely related to that of mammalian fatty acid synthase.

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