Characterization of two bacterial hydroxynitrile lyases with high similarity to cupin superfamily proteins.
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.
Institute of Molecular Biotechnology, Graz University of Technology, Graz, Austria.
Zahid
Z
Hussain
Romana
R
Wiedner
Kerstin
K
Steiner
Tanja
T
Hajek
Manuela
M
Avi
Bianca
B
Hecher
Angela
A
Sessitsch
Helmut
H
Schwab
D000097:Acetonitriles / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D001547:Benzaldehydes / Q000378:metabolism*; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D060026:Endophytes / Q000201:enzymology* / Q000235:genetics; D008190:Lyases / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D000097:Acetonitriles; D001547:Benzaldehydes; D004269:DNA, Bacterial; C045516:mandelonitrile; D008190:Lyases; C032175:benzaldehyde