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Literature summary for 1.11.1.18 extracted from

  • Littlechild, J.; Garcia Rodriguez, E.; Isupov, M.
    Vanadium containing bromoperoxidase--insights into the enzymatic mechanism using X-ray crystallography (2009), J. Inorg. Biochem., 103, 617-621.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Corallina pilulifera

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method, two crystal forms are obtained, one hexagonal form using ammonium phosphate as precipitant (form 1) and a second cubic vanadium bound form (form 2). The best crystals of the cubic form 2 containing vanadate are only obtained with the wild type enzyme. The optimised conditions use an initial protein concentration of 18 mg/ml in 50 mM Tris-H2SO4, 0.4 M KBr, 1 mM Na3VO4, 20% (w/v) polyethylene glycol 6000. For the wild type enzyme crystals grown in form 2, a mother liquor substituting the precipitant with 25% polyethylene glycol 400 and 25% polyethylene glycol 6000 is used Corallina pilulifera

Protein Variants

Protein Variants Comment Organism
R397W the mutant shows a different behaviour on bromide binding compared to the wild type enzyme, (the bromide is missing the hydrogen-binding interaction that held it in the active site of the wild type enzyme) Corallina pilulifera

Organism

Organism UniProt Comment Textmining
Corallina pilulifera
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-
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Purification (Commentary)

Purification (Comment) Organism
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Corallina pilulifera

Synonyms

Synonyms Comment Organism
vanadium containing bromoperoxidase
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Corallina pilulifera