SilE-R and SilE-S - DABB Proteins Catalyzing Enantiospecific Hydrolysis of Organosilyl Ethers

Lisa Pick, Vivien Oehme, Julia Hartmann, Jessica Wenzlaff, Qingyun Tang, Gideon James Grogan, Marion Ansorge-Schumacher

Research output: Contribution to journalArticlepeer-review

Abstract

Silyl ethers fulfil a fundamental role in synthetic organic chemistry as protecting groups and their selective cleavage is an important factor in their application. We present here for the first time two enzymes, SilE-R and SilE-S, which are able to hydrolyze silyl ethers. They belong to the stress-response A/B barrel domain (DABB) family and are able to cleave the Si-O bond with opposite enantiopreference. Silyl ethers containing aromatic, cyclic or aliphatic alcohols and, depending on the alcohol moiety, silyl functions as large as TBDMS are accepted. The X-ray crystal structure of SilE-R, determined to a resolution of 1.98 Ȧ, in combination with mutational studies, revealed an active site featuring two histidine residues, H8 and H79, which likely act synergistically as nucleophile and Brønsted base in the hydrolytic mechanism, which has not previously been described for enzymes. Although the natural function of SilE-R and SilE-S is unknown, we propose that these ‘silyl etherases’ may have significant potential for synthetic applications.
Original languageEnglish
Number of pages12
JournalAngewandte Chemie International Edition
Early online date16 May 2024
DOIs
Publication statusE-pub ahead of print - 16 May 2024

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© 2024 The Authors.

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