Manipulation of macrolide ring size by directed mutagenesis of a modular polyketide synthase

1995 ◽  
Vol 117 (35) ◽  
pp. 9105-9106 ◽  
Author(s):  
Camilla M. Kao ◽  
Guanglin Luo ◽  
Leonard Katz ◽  
David E. Cane ◽  
C. Khosla
Keyword(s):  
Polyketide Synthase ◽  
Directed Mutagenesis ◽  
Ring Size ◽  
Modular Polyketide Synthase

Promiscuity of a modular polyketide synthase towards natural and non-natural extender units

2013 ◽  
Vol 11 (27) ◽  
pp. 4449 ◽  
Author(s):  
Irina Koryakina ◽  
John B. McArthur ◽  
Matthew M. Draelos ◽  
Gavin J. Williams
Keyword(s):  
Polyketide Synthase ◽  
Modular Polyketide Synthase

scholarly journals Type II thioesterase ScoT is required for coelimycin production by the modular polyketide synthase Cpk of Streptomyces coelicolor A3(2).

2014 ◽  
Vol 61 (1) ◽  
Author(s):  
Magdalena Kotowska ◽  
Jarosław Ciekot ◽  
Krzysztof Pawlik
Keyword(s):  
Culture Medium ◽  
Polyketide Synthase ◽  
Streptomyces Coelicolor ◽  
Acyl Chain ◽  
No Production ◽  
Type I ◽  
Type Ii ◽  
Peptide Synthetases ◽  
Modular Polyketide Synthase ◽  
Editing Enzyme

Type II thioesterases were shown to maintain efficiency of modular type I polyketide synthases and nonribosomal peptide synthetases by removing acyl residues blocking extension modules. We found that thioesterase ScoT from Streptomyces coelicolor A3(2) is required for the production of the yellow-pigmented coelimycin by the modular polyketide synthase Cpk. No production of coelimycin was observed in cultures of scoT disruption mutant. Polyketide production was restored upon complementation with an intact copy of the scoT gene. An enzymatic assay showed that ScoT thioesterase can hydrolyse a 12-carbon acyl chain but the activity is too low to play a role in product release from the polyketide synthase. We conclude that ScoT is an editing enzyme necessary to maintain the activity of polyketide synthase Cpk. We provide a HPLC based method to measure the amount of coelimycin P2 in a culture medium.

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

Insights into the stereospecificity of ketoreduction in a modular polyketide synthase

2011 ◽  
Vol 9 (7) ◽  
pp. 2053 ◽  
Author(s):  
David H. Kwan ◽  
Manuela Tosin ◽  
Nadin Schläger ◽  
Frank Schulz ◽  
Peter F. Leadlay
Keyword(s):  
Polyketide Synthase ◽  
Modular Polyketide Synthase

scholarly journals Active site labeling of fatty acid and polyketide acyl-carrier protein transacylases

2019 ◽  
Vol 17 (19) ◽  
pp. 4720-4724 ◽  
Author(s):  
Tony D. Davis ◽  
Jennifer M. Michaud ◽  
Michael D. Burkart
Keyword(s):  
Fatty Acid ◽  
Fluorescent Probe ◽  
Active Site ◽  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Site Directed Mutagenesis ◽  
Probe Design ◽  
Directed Mutagenesis ◽  
Carrier Protein

Fluorescent probe design and site-directed mutagenesis unveil new activity-based chemical reporters for fatty acid and polyketide synthase acyl-carrier protein transacylases.

scholarly journals Directed Mutagenesis Alters the Stereochemistry of Catalysis by Isolated Ketoreductase Domains from the Erythromycin Polyketide Synthase

2006 ◽  
Vol 13 (3) ◽  
pp. 277-285 ◽  
Author(s):  
Abel Baerga-Ortiz ◽  
Bojana Popovic ◽  
Alexandros P. Siskos ◽  
Helen M. O'Hare ◽  
Dieter Spiteller ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Directed Mutagenesis

scholarly journals Molecular basis of celmer's rules: the role of two ketoreductase domains in the control of chirality by the erythromycin modular polyketide synthase

1999 ◽  
Vol 6 (4) ◽  
pp. 189-195 ◽  
Author(s):  
Inès E Holzbaur ◽  
Rebecca C Harris ◽  
Matthew Bycroft ◽  
Jesus Cortes ◽  
Christian Bisang ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Polyketide Synthase ◽  
Modular Polyketide Synthase
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