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Termination of the polyketide scaffold biosynthesis can also vary. It is sometimes accompanied by a thioesterase that releases the polyketide via hydrating the thioester linkage (as in fatty acid synthesis) creating a linear polyketide scaffold. However, if water is not able to reach the active site, the hydrating reaction will not occur and an ...
The polyketide synthase reactions are shown on top. Each type I polyketide-synthase module consists of several domains with defined functions, separated by short spacer regions. The order of modules and domains of a complete polyketide-synthase is as follows (in the order N-terminus to C-terminus): Starting or loading module: AT-ACP-
The acetate pathway, also known as the polyketide pathway, is a fundamental biosynthetic route in organisms for the production of fatty acids and polyketides. This pathway operates at the interface of central metabolism and specialized metabolite synthesis, playing a crucial role in the synthesis of both primary and secondary metabolites. [2 ...
The biosynthesis of nonribosomal peptides shares characteristics with the polyketide and fatty acid biosynthesis. Due to these structural and mechanistic similarities, some nonribosomal peptide synthetases contain polyketide synthase modules for the insertion of acetate or propionate -derived subunits into the peptide chain.
The Tetracenomycin polyketide synthesis protein, tcmI, from Streptomyces glaucescens catalyses an aromatic rearrangement in the biosynthetic pathway of tetracenomycin C from Streptomyces coelicolor. The protein is a homodimer where each subunit forms a beta-alpha-beta fold belonging to the ferrodoxin fold superfamily. [1]
KSs exist as individual enzymes, as they do in type II fatty acid synthesis and type II polyketide synthesis, or as domains in large multidomain enzymes, such as type I fatty acid synthases (FASs) and polyketide synthases (PKSs). KSs are divided into five families: KS1, KS2, KS3, KS4, and KS5. [1] The general mechanism for Ketoacyl synthases
Tylactone synthase or TYLS is a Type 1 polyketide synthase. [1] [2] [3] TYLS is found in strains of Streptomyces fradiae and responsible for the synthesis of the macrolide ring, tylactone, the precursor of an antibiotic, tylosin. [4] TYLS is composed of five large multi-functional proteins, TylGI-V. [5] Each protein contains either one or two ...
However, in polyketide synthesis these enzymes can be used in different combinations to create segments of polyketide that are saturated, unsaturated, or have a hydroxyl or carbonyl functional group. There are also enzymes used in both fatty acid synthesis and polyketide synthesis that can make modifications to the molecule after it has been ...