New bromoperoxidases of marine origin: partial purification and characterization.
Enzymes capable of catalyzing the bromination of p-hydroxybenzyl alcohol by Br- have been shown to be present in crude homogenates of the alga Rhodomela larix (Rhodophyta). There are also indications of such activity in the marine invertebrates Thelepus setosus and Ptychodera flava laysanica. Detailed analysis of R. larix samples indicated that the activity in this species is greatest in the late spring and summer. After partial purification the enzyme had a pH optimum of approx. 4.4, a temperature optimum around 32 degrees C and was inhibited by NaN3. This algal bromoperoxidase requires the presence of H2O2 and can brominate monochlorodimedon and oxidize iodide, but it cannot oxidize chloride. The enzyme appears to be particulate.
D000818:Animals; D000845:Annelida / Q000201:enzymology*; D001592:Benzyl Alcohols; D004072:Digitonin / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D006219:Halogens; D010544:Peroxidases / Q000302:isolation & purification / Q000378:metabolism*; D000461:Rhodophyta / Q000201:enzymology*; D012621:Seasons; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet
D001592:Benzyl Alcohols; D006219:Halogens; C018966:4-hydroxybenzyl alcohol; D010544:Peroxidases; C026195:bromide peroxidase; D004072:Digitonin