期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 47, 页码 20940-20945出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202008859
关键词
biotechnology; C-H activation; enzyme engineering; hydroxylase versus oxidase activity; polyphenol oxidases
资金
- Austrian Science Fund (FWF) [P25217, P32326]
- University of Vienna
- Austrian Science Fund (FWF) [P25217, P32326] Funding Source: Austrian Science Fund (FWF)
Tyrosinases (TYRs) catalyze the hydroxylation of phenols and the oxidation of the resultingo-diphenols too-quinones, while catechol oxidases (COs) exhibit only the latter activity. Aurone synthase (AUS) is not able to react with classical tyrosinase substrates, such as tyramine andl-tyrosine, while it can hydroxylate its natural substrate isoliquiritigenin. The structural difference of TYRs, COs, and AUS at the heart of their divergent catalytic activities is still a puzzle. Therefore, a library of 39 mutants of AUS fromCoreopsis grandiflora(CgAUS) was generated and the activity studies showed that the reactivity of the three conserved histidines (HisA(2), HisB(1), and HisB(2)) is tuned by their adjacent residues (HisB(1)+1, HisB(2)+1, and waterkeeper residue) either to react as stronger bases or / and to stabilize a position permissive for substrate proton shuffling. This provides the understanding for C-H activation based on the type-III copper center to be used in future biotechnological processes.
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