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Literature summary for 4.1.2.10 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
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Application

Application Comment Organism
synthesis the enantiospecific formation of alpha-hydroxynitriles Prunus dulcis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-mandelonitrile Prunus dulcis
-
 cyanide + benzaldehyde
-
 r

Organism

Organism UniProt Comment Textmining
Prunus dulcis
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Hydroxynitrile lyase
-
 Prunus dulcis
PaHNL
-
 Prunus dulcis

Cofactor

Cofactor Comment Organism Structure
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