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Substrate Specificity of Ketosynthase Domains Part II: Amino Acid-Containing Acyl Chains

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Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases

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Abstract

In this chapter, the first study of a KS domain immediately downstream of a NRPS module is reported. Using full-length acyl precursors the substrate specificity of BaeJ KS1 from the bacillaene trans-AT PKS was examined. BaeJ KS1 is the first PKS module in the biosynthesis of bacillaene, and is believed 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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  1. School of Chemistry, University of Warwick, Coventry, UK

    Matthew Jenner

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  1. Matthew Jenner
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Correspondence to Matthew Jenner .

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Jenner, M. (2016). Substrate Specificity of Ketosynthase Domains Part II: Amino Acid-Containing Acyl Chains. In: Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-32723-5_4

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