Corallina pilulifera

Itoh N, AKM Quamrul Hasan, Y Izumi, H Yamada (1988) Substrate specificity, regiospecificity and stereospecificity of halogenation reactions catalyzed by non-heme-type bromoperoxidase of Corallina pilulifera. Eur J Biochem 172 477-484. 

Krenn BE, Y Izumi, H Yamada, R Wever (1989) A comparison of different (vanadium) peroxidases the bro-moperoxidase of Corallina pilulifera is also a vanadium enzyme. Biochim Biophys Acta 998 63-68. 

Ohsawa N, Ogata Y, Okada N, Itoh N (2001) Physiological function of bromoperoxidase in the red marine alga, Corallina pilulifera production of bromoform as an allelochemical and the simultaneous elimination of hydrogen peroxide. Phytochemistry 58 683-692... 

Shimonishi M, Kuwamoto S, Inoue H, Wever R, Ohshiro T, Izumi Y, Tanabe T (1998) Cloning and Expression of the Gene for a Vanadium-Dependent Bromoperoxidase from a Marine Macro-alga, Corallina pilulifera. FEBS Lett 428 105... 

Ohshiro T, Hemrika W, Aibara T, Wever R, Izumi Y (2002) Expression of the Vanadium-Dependent Bromoperoxidase Gene from a Marine Macro-alga Corallina pilulifera in Saccharomyces cerevisiae and Characterization of the Recombinant Enzyme. Phytochemistry 60 595... 

Kitamura, H., Kitahara, S., and Koh, H.B., The induction of larval settlement and metamorphosis of two sea urchins, Pseudocentrotus depressus and Anthocidaris crassispina, by free fatty acids extracted from the coralline red alga Corallina pilulifera, Mar. Biol., 115, 387, 1993. 

Fig. 3. The 13C NMR spectrum of a sulfated xylogalactan from the calcareous red alga Corallina pilulifera (X—signals of the corresponding carbon atoms of nonreducing unsubstituted /J-D-xylopyranosyl branches, L-6—signal of C-6 of 4-linked a-L-galactopyranose residues of the backbone, adapted from ref. 166).

A. I. Usov, M. I. Bilan, and N. G. Klochkova, Polysaccharides of algae. 48. Polysaccharide composition of several calcareous red algae Isolation of alginate from Corallina pilulifera P. et R. (Rhodo-phyta, Corallinaceae), Hot. Mar., 38 (1995) 43-51. 

The X-ray structures of vanadium bromoperoxidases from the red seaweeds Corallina pilulifera and C. officinalis have also been determined and their structures are almost identical. The native structure of these enzymes is dodecameric and the structure is made up of 6 homo-dimers. The secondary stmcture of the chloroperoxidase from the ftmgus Curvularia inaequalis that will be discussed later can be superimposed with the Corallina hromoperoxidase dimer. Many of the a helices of each chloroperoxidase domain are structurally equivalent to the a helices in the Corallina hromoperoxidase dimer. This is in line with the evolutionary relationship between the haloperoxidases that will be discussed later. The disulfide bridges in the enzyme from A. nodosum are not found in the enzyme from Corallina and the two remaining cysteine residues are not involved in disulfide bonds. Additionally, in this enzyme binding sites are present for divalent cations that seem to be necessary to maintain the stmcture of the active site cleft. All the residues directly involved in the binding of vanadate are conserved in the algal bromoperoxidases. ... 

Bromoperoxidase (non-heme) Corallina pilulifera nucleic bases (Br-, I-) 14... 

The chlorination, bromination, and iodination of various nitrogen-containing heterocycles catalyzed by chloroperoxidase from Caldariomyces jumago and bromo-peroxidase from Corallina pilulifera were compared by Itoh et al.[14. ... 

Similar results were obtained by Itoh et al.1U 691 for the halogenation of different substrates using bromoperoxidase from Corallina pilulifera and chloroperoxidase from Caldariomyces jumago. 

Ryu, B., Qian, Z.-J., Kim, M.-M., Nam, K. W., and Kim, S.-K. (2009a). Anti-photoaging activity and inhibition of matrix metalloproteinase (MMP) by marine red alga Corallina pilulifera methanol extract Radiat. Phys. Chem. 78,98-105. 

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