Identification of a Nonaketide Product for the Iterative Polyketide Synthase in Biosynthesis of the Nine-Membered Enediyne C-1027

2010 ◽  
Vol 49 (43) ◽  
pp. 7926-7928 ◽  
Author(s):  
Xiaolei Chen ◽  
Zu-Feng Guo ◽  
Pok Man Lai ◽  
Kong Hung Sze ◽  
Zhihong Guo
Keyword(s):  
Polyketide Synthase ◽  
Iterative Polyketide Synthase

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

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 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 Context-Dependent Behavior of the Enterocin Iterative Polyketide Synthase

2004 ◽  
Vol 11 (4) ◽  
pp. 461-468 ◽  
Author(s):  
Christian Hertweck ◽  
Longkuan Xiang ◽  
John A Kalaitzis ◽  
Qian Cheng ◽  
Michelle Palzer ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Dependent Behavior ◽  
Context Dependent ◽  
Iterative Polyketide Synthase

scholarly journals Biosynthesis of Cell Envelope-Associated Phenolic Glycolipids in Mycobacterium marinum

2015 ◽  
Vol 197 (6) ◽  
pp. 1040-1050 ◽  
Author(s):  
Olivia Vergnolle ◽  
Sivagami Sundaram Chavadi ◽  
Uthamaphani R. Edupuganti ◽  
Poornima Mohandas ◽  
Catherine Chan ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Cell Envelope ◽  
Acyl Chain ◽  
Deep Understanding ◽  
Fatty Acyl ◽  
Chain Extension ◽  
Type I ◽  
Content Type ◽  
Iterative Polyketide Synthase ◽  
Phenolic Glycolipids

Phenolic glycolipids (PGLs) are polyketide synthase-derived glycolipids unique to pathogenic mycobacteria. PGLs are found in several clinically relevant species, including variousMycobacterium tuberculosisstrains,Mycobacterium leprae, and several nontuberculous mycobacterial pathogens, such asM. marinum. Multiple lines of investigation implicate PGLs in virulence, thus underscoring the relevance of a deep understanding of PGL biosynthesis. We report mutational and biochemical studies that interrogate the mechanism by which PGL biosynthetic intermediates (p-hydroxyphenylalkanoates) synthesized by the iterative polyketide synthase Pks15/1 are transferred to the noniterative polyketide synthase PpsA for acyl chain extension inM. marinum. Our findings support a model in which the transfer of the intermediates is dependent on ap-hydroxyphenylalkanoyl-AMP ligase (FadD29) acting as an intermediary between the iterative and the noniterative synthase systems. Our results also establish thep-hydroxyphenylalkanoate extension ability of PpsA, the first-acting enzyme of a multisubunit noniterative polyketide synthase system. Notably, this noniterative system is also loaded with fatty acids by a specific fatty acyl-AMP ligase (FadD26) for biosynthesis of phthiocerol dimycocerosates (PDIMs), which are nonglycosylated lipids structurally related to PGLs. To our knowledge, the partially overlapping PGL and PDIM biosynthetic pathways provide the first example of two distinct, pathway-dedicated acyl-AMP ligases loading the same type I polyketide synthase system with two alternate starter units to produce two structurally different families of metabolites. The studies reported here advance our understanding of the biosynthesis of an important group of mycobacterial glycolipids.

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