Titlebook: Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases; Matthew Jenner Book 2016 Springer Internat

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AMOR

,Substrate Specificity of Ketosynthase Domains Part I: β-Branched Acyl Chains,guyen et al., Nat. Biotechnol. 26:225–233, 2008, [.]). The extent of this evolution-based specificity is believed to reach as far as the β-position for each given biosynthetic intermediate, as detailed in section “KS Specificity-Based Assignment of .-AT PKSs”. Compared to textbook colinearity rules,

Coterminous

expire

打算

endure

Substrate Specificity of Ketosynthase Domains Part II: Amino Acid-Containing Acyl Chains,to accept a glycine-derived intermediate incorporated by the previous NRPS module. KS1 is positioned in a phylogenetic clade with other amino-acid accepting KS domains, of which the majority accept a glycine intermediate.

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Substrate Specificity of Ketosynthase Domains Part III: Elongation-Based Substrate Specificity, Chap. ., which is able to accept a β-Me branched acyl unit, is also shown to elongate this bulky acyl group in addition to 5- and 6-membered rings, demonstrating scope for engineering new polyketides.

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,Substrate Specificity of Ketosynthase Domains Part I: β-Branched Acyl Chains,om the psymberin PKS are reported. Using the data from these assays, in conjunction with homology modelling, the molecular rules dictating the ability of KS domains to accept carbon based β-branched substrates is revealed.

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