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Substrate specificity of a ketosynthase domain involved in bacillaene biosynthesis.


ABSTRACT: An isotopic labelling method was developed to investigate substrate binding by ketosynthases, exemplified by the second ketosynthase of the polyketide synthase BaeJ involved in bacillaene biosynthesis (BaeJ-KS2). For this purpose, both enantiomers of a 13C-labelled N-acetylcysteamine thioester (SNAC ester) surrogate of the proposed natural intermediate of BaeJ-KS2 were synthesised, including an enzymatic step with glutamate decarboxylase, and incubated with BaeJ-KS2. Substrate binding was demonstrated through 13C NMR analysis of the products against the background of various control experiments.

SUBMITTER: Yin Z 

PROVIDER: S-EPMC10999986 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature

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Substrate specificity of a ketosynthase domain involved in bacillaene biosynthesis.

Yin Zhiyong Z   Dickschat Jeroen S JS  

Beilstein journal of organic chemistry 20240405


An isotopic labelling method was developed to investigate substrate binding by ketosynthases, exemplified by the second ketosynthase of the polyketide synthase BaeJ involved in bacillaene biosynthesis (BaeJ-KS2). For this purpose, both enantiomers of a <sup>13</sup>C-labelled <i>N</i>-acetylcysteamine thioester (SNAC ester) surrogate of the proposed natural intermediate of BaeJ-KS2 were synthesised, including an enzymatic step with glutamate decarboxylase, and incubated with BaeJ-KS2. Substrate  ...[more]

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