Results 201 to 210 of about 31,758 (236)
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Tolerance and Specificity of Polyketide Synthases

Annual Review of Biochemistry, 1999
▪ Abstract  Polyketide synthases catalyze the assembly of complex natural products from simple precursors such as propionyl-CoA and methylmalonyl-CoA in a biosynthetic process that closely parallels fatty acid biosynthesis. Like fatty acids, polyketides are assembled by successive decarboxylative condensations of simple precursors.
C, Khosla   +3 more
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Non-modular polyketide synthases in myxobacteria

Phytochemistry, 2009
Myxobacteria are prolific producers of a wide variety of secondary metabolites. The vast majority of these compounds are complex polyketides which are biosynthesised by multimodular polyketide synthases (PKSs). In contrast, few myxobacterial metabolites isolated to date are derived from non-modular PKSs, in particular type III PKSs. This review reports
Yanyan, Li, Rolf, Müller
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Polyketide Synthase Genes from Marine Dinoflagellates

Marine Biotechnology, 2003
Rapidly developing techniques for manipulating the pathways of polyketide biosynthesis at the genomic level have created the demand for new pathways with novel biosynthetic capability. Polyketides derived from dinoflagellates are among the most complex and unique structures identified thus far, yet no studies of the biosynthesis of dinoflagellate ...
Snyder, R. V.   +6 more
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Polyketide Synthases: Mechanisms and Models

2006
The modular structure of the multienzyme PKSs makes them particularly attractive targets for combinatorial biosynthesis aimed at generating novel polyketide medicines. We are beginning to understand those features of subunit organization and structure and their linking and docking elements, which are critical for productive engineering efforts ...
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Building-block selectivity of polyketide synthases

Current Opinion in Chemical Biology, 2003
For the past decade, polyketide synthases have presented an exciting paradigm for the controlled manipulation of complex natural product structure. These multifunctional enzymes catalyze the biosynthesis of polyketide natural products by stepwise condensation and modification of metabolically derived building blocks.
Grace F, Liou, Chaitan, Khosla
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Polyketide Synthase Secrets Revealed

Chemical & Engineering News Archive, 2014
A new study solves long-standing mysteries about how bacterial natural-product-making factories are put together and how they work. The findings could accelerate efforts to engineer these workshops to produce novel bioactive agents for drug discovery. Bacteria use huge multienzyme complexes called polyketide synthases (PKSs) to create a wide variety of
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Structures and Mechanisms of Polyketide Synthases

The Journal of Organic Chemistry, 2009
Nearly a quarter-century ago, the advent of molecular genetic tools in the field of natural product biosynthesis led to the remarkable revelation that the genes responsible for the biosynthesis, regulation, and self-resistance of complex polyketide antibiotics were clustered in the genomes of the bacteria that produced these compounds.
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Novel applications of plant polyketide synthases

Current Opinion in Chemical Biology, 2012
The structurally and mechanistically simple type III polyketide synthases (PKSs) catalyze iterative condensations of CoA thioesters to produce a variety of polyketide scaffolds with remarkably diverse structures and biological activities. By exploiting the enzymes, we combined precursor-directed biosynthesis with nitrogen-containing substrates and ...
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The Chalcone Synthase Superfamily of Type III Polyketide Synthases

ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Michael B, Austin, Joseph P, Noel
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Chalcone synthases (CHSs): the symbolic type III polyketide synthases

Planta, 2019
Present review provides a thorough insight on some significant aspects of CHSs over a period of about past three decades with a better outlook for future studies toward comprehending the structural and mechanistic intricacy of this symbolic enzyme. Polyketide synthases (PKSs) form a large family of iteratively acting multifunctional proteins that are ...
Shahzad A, Pandith   +4 more
openaire   +2 more sources

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