GtHNL from Granulicella tundricola is a
Mn(II) containing hydroxynitrile lyase with a cupin fold. The
quasi-octahedral manganese is pentacoordinated by the enzyme. It catalyzes
the enantioselective addition of HCN to aldehydes, yielding R-cyanohydrins. On the Lewis acidic vacant coordination
site the Mn binds either substrate or the product, leading to a hexacoordinated
17 electron complex. EPR spectra of the active enzyme are unusually
wide with a zero-field splitting approximately equal to the X-band
microwave energy. A spectral change is induced by incubation with
either one of the substrates/products HCN, benzaldehyde, and/or mandelonitrile.
This points toward Mn(II) catalyzed cyanohydrin synthesis.
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