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Literature summary extracted from

  • Dreveny, I.; Andryushkova, A.S.; Glieder, A.; Gruber, K.; Kratky, C.
    Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity (2009), Biochemistry, 48, 3370-3377.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.2.10 synthesis hydroxynitrile lyases are proficient biocatalysts for the stereospecific synthesis of cyanohydrins Prunus dulcis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.10 expression of mutant and wild-type enzymes in Pichia pastoris X33 Prunus dulcis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.10 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 Prunus dulcis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.10 H459N less than 5% of the activity compared to wild type Prunus dulcis
4.1.2.10 H497N less than 5% of the activity compared to wild type Prunus dulcis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.2.10 (R)-mandelonitrile Prunus dulcis in a large number of plant species hydroxynitrile lyases catalyzes the decomposition of cyanohydrins in order to generate hydrogen cyanide upon tissue damage. Hydrogen cyanide serves as a deterrent against herbivores and fungi cyanide + benzaldehyde
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.10 Prunus dulcis O24243
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.2.10 (R)-mandelonitrile = cyanide + benzaldehyde based on the binding geometry, a reaction mechanism is proposed that involves one of the two conserved active site histidine residues acting as a general base abstracting the proton from the cyanohydrin hydroxyl group. Site-directed mutagenesis shows that both active site histidines are required for the reaction to occur Prunus dulcis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.10 (R)-mandelonitrile in a large number of plant species hydroxynitrile lyases catalyzes the decomposition of cyanohydrins in order to generate hydrogen cyanide upon tissue damage. Hydrogen cyanide serves as a deterrent against herbivores and fungi Prunus dulcis cyanide + benzaldehyde
-
 r
4.1.2.10 cyanide + benzaldehyde
-
 Prunus dulcis (R)-mandelonitrile
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.2.10 FAD-HNL
-
 Prunus dulcis
4.1.2.10 PaHNL1
-
 Prunus dulcis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.10 FAD there is no evidence that the flavin cofactor directly participates in the reaction Prunus dulcis