Literature summary for 1.14.18.1 extracted from

Sendovski, M.; Kanteev, M.; Ben-Yosef, V.S.; Adir, N.; Fishman, A.
First structures of an active bacterial tyrosinase reveal copper plasticity (2011), J. Mol. Biol., 405, 227-237.

Search for more literature for 1.14.18.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21 cells	Priestia megaterium

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method	Priestia megaterium

Protein Variants

Protein Variants	Comment	Organism
R209H	the mutant possesses a higher monophenolase/diphenolase activity ratio than the wild type enzyme	Priestia megaterium

Inhibitors

Inhibitors	Comment	Organism	Structure
kojic acid	i.e. 5-hydroxy-2-(hydroxymethyl)-g-pyrone	Priestia megaterium

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	tyrosinase is a member of the type 3 copper enzyme family, two Cu2+ ions serveas the major cofactors within the active site	Priestia megaterium

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
35000	-	2 * 35000, X-ray crystallography	Priestia megaterium
70000	-	gel filtration	Priestia megaterium

Organism

Organism	UniProt	Comment	Textmining
Priestia megaterium	B2ZB02	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Priestia megaterium

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-tyrosine + O2	-	Priestia megaterium	dopachrome + H2O	-	?

Subunits

Subunits	Comment	Organism
homodimer	2 * 35000, X-ray crystallography	Priestia megaterium

Synonyms

Synonyms	Comment	Organism
tyr	-	Priestia megaterium
tyrosinase	-	Priestia megaterium

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Release 2023.1 (January 2023)