Substrate specificity, regiospecificity and stereospecificity of halogenation reactions catalyzed by non-heme-type bromoperoxidase of Corallina pilulifera.
Many organic compounds were found to be substrates for halogenation reactions catalyzed by the non-heme-type bromoperoxidase found in the red alga Corallina pilulifera. Anisole, 1-methoxynaphthalene and thiophene were converted to o and p-bromoanisoles, 1-methoxy-4-bromonaphthalene and 2-bromothiophene respectively. Regiospecificity of the enzymatic bromination of anisole was tested and found to be the same as in the chemical reaction with NaOBr. The enzyme also acted on substituted alkenes such as styrene, cyclohexene, trans-cinnamic acid, trans-cinnamyl alcohol and cis-propenylphosphonic acid, to give the respective bromohydrin compounds or decarboxylated bromo compound. These bromohydrin compounds were always mixtures of stereoisomers. In the light of the above findings together with the previous studies concerning the halogenation mechanism, the bromoperoxidase of C. pilulifera was considered to have no specific restriction site for these substrates.
Itoh
N
N
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
Hasan
A K
AK
Izumi
Y
Y
Yamada
H
H
D000438:Alcohols / Q000096:biosynthesis; D001665:Binding Sites; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D003653:Decarboxylation; D008401:Gas Chromatography-Mass Spectrometry; D006219:Halogens / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D010544:Peroxidases / Q000378:metabolism*; D000461:Rhodophyta / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity
D000438:Alcohols; D006219:Halogens; C023963:bromohydrins; D010544:Peroxidases; C026195:bromide peroxidase