High impact information on Ascophyllum

• An amino acid sequence comparison with vanadium-containing bromoperoxidase from the seaweed Ascophyllum nodosum shows high similarities in the regions of the metal binding site, with all hydrogen vanadate(V) interacting residues conserved except for lysine-353, which is an asparagine [1].
• Analysis of the catalytic parameters of the mutant vanadium bromoperoxidase from the seaweed Ascophyllum nodosum also adds fuel to the discussion regarding factors governing the halide specificity of vanadium haloperoxidases [2].
• The reaction of vanadium-bromoperoxidase from the brown alga Ascophyllum nodosum with hydrogen peroxide, bromide, and 2-chlorodimedone has been subjected to an extensive steady-state kinetic analysis [3].
• The basis of the irreversible inactivation of the vanadium bromoperoxidase (V-BrPO) isolated from the marine alga Ascophyllum nodosum under turnover conditions at low pH (i.e., 15 to 100 mM H2O2, 0.1 KBr, ca. 15 nM V-BrPO in 0.1 M citrate, pH 4) has been investigated [4].
• V-BrPO (F. distichus, M. pyrifera, and Ascophyllum nodosum) also catalyzes the oxidation of bromide using peracetic acid [5].

Biological context of Ascophyllum

• Characterization of a new alpha-L-fucosidase isolated from the marine mollusk Pecten maximus that catalyzes the hydrolysis of alpha-L-fucose from algal fucoidan (Ascophyllum nodosum) [6].

Associations of Ascophyllum with chemical compounds

• The brown alga Ascophyllum nodosum contains two different vanadium bromoperoxidases [7].
• (Model) studies on vanadate-dependent bromo/iodoperoxidase from Ascophyllum nodosum. VO2+ is not incorporated into the active site [8].
• The study of the structural bases of the biological properties of algal fucoidan (Ascophyllum nodosum) led us to look for enzymes able to modify this sulfated polysaccharide [9].
• The method provided direct, rapid chromatography of phenol sulfates in crude extracts of the red alga (Polysiphonia lanosa (2,3-dibromo-4,5-dihydroxybenzyl alcohol 1',4-disulfate), of the brown alga Ascophyllum nodosum (1,2,3,5-tetrahydroxybenzene 2,5-disulfate), and in rat urine (resorcinol mono- and disulfates) [10].
• We have previously shown that vanadium bromoperoxidase from Ascophyllum nodosum mediates production of the (R)-enantiomer of methyl phenyl sulfoxide with 91% enantiomeric excess [11].

Gene context of Ascophyllum

• Tasco-Forage is an Ascophyllum nodosum seaweed-based product that has increased antioxidant activity in both plants and animals [12].

References