Characterization of Two Bacterial Hydroxynitrile Lyases with High Similarity to Cupin Superfamily Proteins | Zendy

Zahid Hussain | Zendy; Romana Wiedner | Zendy; Kerstin Steiner | Zendy; Tanja Hajek | Zendy; Manuela Avi | Zendy; Bianca Hecher | Zendy; Angela Sessitsch | Zendy; Helmut Schwab | Zendy

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Characterization of Two Bacterial Hydroxynitrile Lyases with High Similarity to Cupin Superfamily Proteins

Author(s) -

Zahid Hussain,

Romana Wiedner,

Kerstin Steiner,

Tanja Hajek,

Manuela Avi,

Bianca Hecher,

Angela Sessitsch,

Helmut Schwab

Publication year - 2012

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.06899-11

Subject(s) - enantioselective synthesis , chemistry , bacteria , biochemistry , benzaldehyde , superfamily , stereochemistry , enzyme , condensation reaction , cleavage (geology) , biology , catalysis , gene , genetics , paleontology , fracture (geology)

Hydroxynitrile lyases (HNLs) catalyze the cleavage of cyanohydrins. In the reverse reaction, they catalyze the formation of carbon-carbon bonds by enantioselective condensation of hydrocyanic acid with carbonyls. In this study, we describe two proteins from endophytic bacteria that display activity in the cleavage and the synthesis reaction of (R)-mandelonitrile with up to 74% conversion of benzaldehyde (enantiopreference ee 89%). Both showed high similarity to proteins of the cupin superfamily which so far were not known to exhibit HNL activity.

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