Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Gou, L.; Lu, Z.R.; Park, D.; Sang, H.; Shi, L.; Seong, J.; Bhak, J.; Park, Y.; Ren, Z.; Zou, F.
    The effect of histidine residue modification on tyrosinase activity and conformation: Inhibition kinetics and computational prediction (2008), J. Biomol. Struct. Dyn., 26, 395-401.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.18.1 Bromoacetate noncompetitive inhibition in a dose-dependent manner Agaricus bisporus
1.14.18.1 additional information histidine chemical modification of tyrosinase conspicuously inactivates enzyme activity Agaricus bisporus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.18.1 0.51
-
L-Dopa
-
Agaricus bisporus

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.1 Agaricus bisporus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.1 L-DOPA + O2
-
Agaricus bisporus dopaquinone + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.18.1 tyrosinase
-
Agaricus bisporus

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.14.18.1 25
-
-
Agaricus bisporus Bromoacetate