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Literature summary for 4.1.2.10 extracted from

  • Andexer, J.N.; Staunig, N.; Eggert, T.; Kratky, C.; Pohl, M.; Gruber, K.
    Hydroxynitrile lyases with alpha/beta-hydrolase fold: two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms (2012), ChemBioChem, 13, 1932-1939.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at a crystallographic resolution of 2.5 A and comparison with the S-selective HNL from Hevea brasiliensis. The structures exhibit an alpha/beta-hydrolase fold and a Ser-His-Asp catalytic triad. Modeling of complexes of the enzymes with both (R)- and (S)-mandelonitrile leads to a catalytic mechanism, in which His236 from the catalytic triad acts as a general base and the emerging negative charge on the cyano group is stabilized by main-chain amide groups and an alpha-helix dipole very similar to alpha/beta-hydrolases Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
D208N less than 2% residual activity Arabidopsis thaliana
H236F less than 2% residual activity Arabidopsis thaliana
M237K no residual activity Arabidopsis thaliana
M237L 100% residual activity Arabidopsis thaliana
N12T less than 2% residual activity Arabidopsis thaliana
N12T/M237K expression results in insoluble protein Arabidopsis thaliana
S81A less than 2% residual activity Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9LFT6
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