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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.11.1.B6 Br- competitive versus I- Laminaria digitata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.B6 2.5
-
I- pH 6.2 Laminaria digitata

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.B6 Laminaria digitata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.B6
-
Laminaria digitata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.B6 sporophyte
-
Laminaria digitata
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.B6 additional information the enzyme does not catalyze monochlorodimedone bromination Laminaria digitata ?
-
?
1.11.1.B6 RH + I- + H2O2 + H+
-
Laminaria digitata RI + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.B6 vanadium-dependent iodoperoxidase
-
Laminaria digitata
1.11.1.B6 vIPO
-
Laminaria digitata

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.B6 462
-
I- pH 6.2 Laminaria digitata