Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis
Wajant H
Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis - Plant science 1996 - 25-31
Hydroxynitrile lyase from Hevea brasiliensis (HbHNL) was purified to apparent homogeneity. Purified HbHNL consists of non-covalently linked monomers of 30kDa. HbHNL exhibits a typical Michaelis-Menten kinetics with a Km of 115 mM and the enzyme activity is strongly inhibited by diisopropyl fluorophosphate and diethyl pyrocarbonate indicating a serine and histidine in the active site. HbHNL is serologically related to the HNL from Manohot esculenta but not to other HNLs.
Cyanogenesis
Enzyme purification
Hevea brasiliensis
Hydroxynitrile lyase
Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis - Plant science 1996 - 25-31
Hydroxynitrile lyase from Hevea brasiliensis (HbHNL) was purified to apparent homogeneity. Purified HbHNL consists of non-covalently linked monomers of 30kDa. HbHNL exhibits a typical Michaelis-Menten kinetics with a Km of 115 mM and the enzyme activity is strongly inhibited by diisopropyl fluorophosphate and diethyl pyrocarbonate indicating a serine and histidine in the active site. HbHNL is serologically related to the HNL from Manohot esculenta but not to other HNLs.
Cyanogenesis
Enzyme purification
Hevea brasiliensis
Hydroxynitrile lyase