A new catalytic function of halohydrin hydrogen-halide-lyase, synthesis of beta-hydroxynitriles from epoxides and cyanide.
Halohydrin hydrogen-halide-lyase, which catalyzes the interconversion of halohydrins to epoxides, purified from a recombinant E. coli was found to catalyze the transformation of 1,2-epoxybutane into beta-hydroxyvaleronitrile in the presence of cyanide. Chloride inhibited competitively the formation of beta-hydroxyvaleronitrile. The enzyme also catalyzed the transformation of some other epoxides into the corresponding beta-hydroxynitriles in the presence of cyanide.
Nakamura
T
T
Central Research Laboratory, Nitto Chemical Industry Co., Ltd., Yokohama, Japan.
Nagasawa
T
T
Yu
F
F
Watanabe
I
I
Yamada
H
H
D000446:Aldehyde-Lyases; D002384:Catalysis; D004852:Epoxy Compounds / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006856:Hydrogen Cyanide / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008190:Lyases; D009153:Mutagens / Q000737:chemistry*; D009570:Nitriles / Q000138:chemical synthesis*; D011994:Recombinant Proteins; D013055:Spectrophotometry, Infrared
D004852:Epoxy Compounds; D009153:Mutagens; D009570:Nitriles; D011994:Recombinant Proteins; C027488:1,2-epoxybutane; D006856:Hydrogen Cyanide; C071333:beta-hydroxyvaleronitrile; D008190:Lyases; D000446:Aldehyde-Lyases; C021541:mandelonitrile lyase; C066813:haloalcohol hydrogen-halide lyase