Cloned (Comment) | Organism |
---|---|
- |
Arabidopsis thaliana |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | Q9LFT6 | - |
- |