A vanadium-dependent bromoperoxidase in the marine red alga Kappaphycus alvarezii (Doty) Doty displays clear substrate specificity.
Bromoperoxidase activity was initially detected in marine macroalgae belonging to the Solieriaceae family (Gigartinales, Rhodophyta), including Solieria robusta (Greville) Kylin, Eucheuma serra J. Agardh and Kappaphycus alvarezii (Doty) Doty, which are important industrial sources of the polysaccharide carrageenan. Notably, the purification of bromoperoxidase was difficult because due to the coexistence of viscoid polysaccharides. The activity of the partially purified enzyme was dependent on the vanadate ion, and displayed a distinct substrate spectrum from that of previously reported vanadium-dependent bromoperoxidases of marine macroalgae. The enzyme was specific for Br- and I- ions and inactive toward F- and Cl-. The K(m) values for Br- and H2O2 were 2.5x10(-3) M and 8.5x10(-5) M, respectively. The halogenated product, dibromoacetaldehyde, that accumulated in K. alvarezii was additionally determined.
Kamenarska
Zornitsa
Z
Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria.
Taniguchi
Tomokazu
T
Ohsawa
Noboru
N
Hiraoka
Masanori
M
Itoh
Nobuya
N
D020418:Algal Proteins / Q000302:isolation & purification / Q000378:metabolism*; D008968:Molecular Conformation; D010544:Peroxidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000461:Rhodophyta / Q000201:enzymology*; D013379:Substrate Specificity; D014638:Vanadates / Q000378:metabolism*
D020418:Algal Proteins; D014638:Vanadates; D010544:Peroxidases; C026195:bromide peroxidase