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4.1.2.10: (R)-mandelonitrile lyase

This is an abbreviated version!
For detailed information about (R)-mandelonitrile lyase, go to the full flat file.

Word Map on EC 4.1.2.10

Reaction

(R)-mandelonitrile
=
cyanide
 +
benzaldehyde

Synonyms

(R)-(+)-Mandelonitrile lyase, (R)-HNL, (R)-HNL5, (R)-hydroxynitrile lyase, (R)-Mandelonitrile lyase, (R)-Oxynitrilase, (R)-PeHNL, (R)-selective HNL, AciX9_0562, almond oxynitrilase, APHNL, AtHNL, cupin 2 conserved barrel domain protein, cupin 2 domain-containing protein, D-alpha-hydroxynitrile lyase, D-Hydroxynitrile lyase, D-Oxynitrilase, DtHNL1, EjHNL, FAD-HNL, HNL, HNL1, HNL2, HNL4, HNL5, Hydroxynitrile lyase, hydroynitrile lyase, Lyase, mandelonitrile, mandelonitrile lyase, MDL, Mdl1, NdHNL, Oxynitrilase, PaHNL, PaHNL1, PaHNL5, PaMDL, ParsHNL, PhaMDL, PmHNL, R-HNL, R-hydroxynitrile lyase, R-selective HNL, R-selective hydroxynitrile lyase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.10 (R)-mandelonitrile lyase

Crystallization

Crystallization on EC 4.1.2.10 - (R)-mandelonitrile lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
sitting drop vapor-diffusion method
to 2.5 A resolution, Structure exhibits a cupin fold, and manganese is bound to three histidine and one glutamine residue
crystals of the His6-tagged hydroxynitrile lyase are prepared using vapor diffusion sitting drop method at 20°C. The crystal structures of Passiflora edulis hydroxynitrile lyase and its C-terminal peptide depleted derivative are determined by molecular replacement method using the template structure of a heat stable protein, SP1, from Populus tremula at 2.8 and 1.8 A resolution, respectively. Passiflora edulis hydroxynitrile lyase belongs to dimeric alpha+beta barrel superfamily consisting of a central beta-barrel in the middle of a dimer. The structure of Passiflora edulis hydroxynitrile lyase complexed with (R)-mandelonitrile is also determined. The hydroxyl group of (R)-mandelonitrile forms hydrogen bonds with His8 and Tyr30 in the active site, whereas the nitrile group is oriented toward the carboxyl group of Glu54, unlike other hydroxynitrile lyases, where it interacts with basic residues typically
3D structural data of the enzyme with the reaction product benzaldehyde bound within the active site, which allow unambiguous assignment of the location of substrate binding
crystal structuture of mutant V317A of hydroxynitrile lyase isoenzyme 5 in complex with benzyl alcohol. The structure of is determined at a resolutionof 2.3 A by molecular replacement
hanging drop vapor diffusion using polyethylene glycol 4000 and isopropanol as coprecipitants. The crystals belong to the monoclinic space group P2(1) with unit cell parameters a = 69.9, b = 95.1, c = 95.6 A, and beta = 118.5 degrees. A complete set of diffraction data collected to 2.6 A resolution on native crystals of isoenzyme III
-
triclinic crystals grown in hanging drops, 1.5 A resolution, space group P1 with cell parameters a = 56.2 A, b = 67.5 A, c = 79.8
vapor diffusion method, high resolution X-ray structure of the highly glycosylated Prunus amygdalus HNL isoenzyme 5 (PaHNL5 V317A) expressed in Aspergillus niger and its complex with benzyl alcohol. In PaHNLs benzyl alcohol is bound too far away from the FAD cofactor in order to be oxidized