Literature summary for 1.14.18.1 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.

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Inhibitors

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

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Agaricus bisporus	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
tyrosinase	-	Agaricus bisporus

IC50 Value

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

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Release 2023.1 (January 2023)