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Highly Enantioselective sec-Alkyl Sulfatase Activity of the Marine Planctomycete Rhodopirellula baltica Shows Retention of Configuration

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  • This study was performed within the Research Centre for Applied Biocatalysis. Financial support by the FFG, the City of Graz, and the Province of Styria is gratefully acknowledged. L. Arbanas, T. Glieder, W. Kroutil, and U. Wagner (Graz) are thanked for their valuable contributions in sequence analysis.

Abstract

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Hydrolytic enzymes: The marine planctomycete Rhodopirellula baltica DSM 10527 displays high stereo- and enantioselective alkyl sulfatase activity towards (±)-sec-alkyl sulfates with retention of configuration through cleavage of their S[BOND]O bond (see scheme; pathway B), whereas inversion of configuration is observed upon cleavage of the C[BOND]O bond (pathway A).

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