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Literature summary extracted from

  • Dreveny, I.; Kratky, C.; Gruber, K.
    The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesis (2002), Protein Sci., 11, 292-300.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.2.10 synthesis the enantiospecific formation of alpha-hydroxynitriles 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
-
cyanide + benzaldehyde
-
r

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.10 (R)-mandelonitrile
-
Prunus dulcis cyanide + benzaldehyde
-
r
4.1.2.10 (R)-mandelonitrile modeling studies provide insights into the mechanism of cyanogenesis Prunus dulcis cyanide + benzaldehyde
-
r

Synonyms

EC Number Synonyms Comment Organism
4.1.2.10 Hydroxynitrile lyase
-
Prunus dulcis
4.1.2.10 PaHNL
-
Prunus dulcis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.10 FAD absolute requirement of oxidized FAD as cofactor. Enzyme activity requires the FAD cofactor to be bound in its oxidized form. The observed inactivation upon cofactor reduction is largely caused by the reversal of the electrostatic potential within the active site Prunus dulcis