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Literature summary for 1.11.1.B6 extracted from

  • Colin, C.; Leblanc, C.; Michel, G.; Wagner, E.; Leize-Wagner, E.; van Dorsselaer, A.; Potin, P.
    Vanadium-dependent iodoperoxidases in Laminaria digitata, a novel biochemical function diverging from brown algal bromoperoxidases (2005), J. Biol. Inorg. Chem., 10, 156-166.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Br- competitive versus I- Laminaria digitata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5
-
I- pH 6.2 Laminaria digitata

Organism

Organism UniProt Comment Textmining
Laminaria digitata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Laminaria digitata

Source Tissue

Source Tissue Comment Organism Textmining
sporophyte
-
Laminaria digitata
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme does not catalyze monochlorodimedone bromination Laminaria digitata ?
-
?
RH + I- + H2O2 + H+
-
Laminaria digitata RI + H2O
-
?

Synonyms

Synonyms Comment Organism
vanadium-dependent iodoperoxidase
-
Laminaria digitata
vIPO
-
Laminaria digitata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
462
-
I- pH 6.2 Laminaria digitata