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PDBsum entry 5e4m
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References listed in PDB file
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Key reference
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Title
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Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the bet v1 superfamily.
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Authors
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E.Lanfranchi,
T.Pavkov-Keller,
E.M.Koehler,
M.Diepold,
K.Steiner,
B.Darnhofer,
J.Hartler,
T.Van den bergh,
H.J.Joosten,
M.Gruber-Khadjawi,
G.G.Thallinger,
R.Birner-Gruenberger,
K.Gruber,
M.Winkler,
A.Glieder.
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Ref.
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Sci Rep, 2017,
7,
46738.
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PubMed id
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Abstract
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Homology and similarity based approaches are most widely used for the
identification of new enzymes for biocatalysis. However, they are not suitable
to find truly novel scaffolds with a desired function and this averts options
and diversity. Hydroxynitrile lyases (HNLs) are an example of non-homologous
isofunctional enzymes for the synthesis of chiral cyanohydrins. Due to their
convergent evolution, finding new representatives is challenging. Here we show
the discovery of unique HNL enzymes from the fern Davallia tyermannii by
coalescence of transcriptomics, proteomics and enzymatic screening. It is the
first protein with a Bet v1-like protein fold exhibiting HNL activity, and has a
new catalytic center, as shown by protein crystallography. Biochemical
properties of D. tyermannii HNLs open perspectives for the development of a
complementary class of biocatalysts for the stereoselective synthesis of
cyanohydrins. This work shows that systematic integration of -omics data
facilitates discovery of enzymes with unpredictable sequences and helps to
extend our knowledge about enzyme diversity.
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