1up8
From Proteopedia
Recombinant vanadium-dependent bromoperoxidase from red algae Corallina pilulifera
Structural highlights
FunctionPRXV_CORPI Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBromoperoxidase from the macro-alga Corallina pilulifera is an enzyme that possesses vanadate in the catalytic center, and shows a significant thermostability and stability toward organic solvents. The structural analysis of the recombinant enzyme overexpressed in yeast revealed that it contains one calcium atom per subunit. This has been confirmed by inductively coupled plasma emission spectrometry experiments. The study of the effect of metal ions on the apo-enzyme stability has shown that the calcium ion significantly increased the enzyme stability. In addition, vanadate also increased the thermostability and strontium and magnesium ions had similar effects as calcium. The holo-enzyme shows high stability in a range of organic solvents. The effect of the different ions and solvents on the structure of the enzyme has been studied by circular dichroism experiments. The high stability of the enzyme in the presence of organic solvents is useful for its application as a biocatalyst. Enhancing effect of calcium and vanadium ions on thermal stability of bromoperoxidase from Corallina pilulifera.,Garcia-Rodriguez E, Ohshiro T, Aibara T, Izumi Y, Littlechild J J Biol Inorg Chem. 2005 May;10(3):275-82. Epub 2005 Mar 18. PMID:15776268[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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