1.14.18.1: tyrosinase

This is an abbreviated version!
For detailed information about tyrosinase, go to the full flat file.

Reaction

2 L-dopa +

Synonyms

AbPPO1, AbPPO4, AbTYR, aurone synthase, catalase-phenol oxidase, catechol oxidase, catecholase, CATPO, chlorogenic acid oxidase, chlorogenic oxidase, cresolase, cresolase/monophenolase, CsPPO, CZA14Tyr, deoxy-tyrosinase, dihydroxy-L-phenylalanine:oxygen oxidoreductase, Diphenol oxidase, diphenolase, dopa oxidase, EC 1.10.3.1, EC 1.14.17.2, Hc-derived phenoloxidase, Hc-phenoloxidase, HcPO, HdPO, hemocyanin-derived phenoloxidase, jrPPO1, jrTYR, L-DOPA monophenolase, L-DOPA oxidase, L-DOPA:oxygen oxidoreductase, L-tyrosine hydroxylase, MdPPO1, melC2, MelC2 tyrosinase, met-tyrosinase, monophenol dihydroxyphenylalanine:oxygen oxidoreductase, monophenol monooxidase, monophenol monooxygenase, monophenol monoxygenase, monophenol oxidase, monophenol oxygen oxidoreductase, monophenol, 3,4-dihydroxy L-phenylalanine (L-DOPA):oxygen oxidoreductase, monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase, monophenol, dihydroxy-L-phenylalanine:oxygen oxidoreductase, monophenol, dihydroxyphenylalanine:oxygen oxidoreductase, monophenol, L-Dopa: oxidoreductase, monophenol, L-DOPA: oxygen oxidoreductase, monophenol, o-diphenol: oxygen oxidoreductase, monophenol, o-diphenol:O2 oxidoreductase, monophenol, o-diphenol:oxygen oxido-reductase, monophenol, o-diphenol:oxygen oxidoreductase, monophenol, polyphenol oxidase, monophenol: dioxygen oxidoreductases, hydroxylating, monophenolase, monphenol mono-oxygenase, More, mTyr, murine tyrosinase, mushroom tyrosinase, mushroom tyrosine, N-acetyl-6-hydroxytryptophan oxidase, o-diphenol oxidase, o-diphenol oxidoreductase, o-diphenol oxygen oxidoreductase, o-diphenol: O2 oxidoreductase, o-diphenol: oxidoreductase, o-diphenol:O2 oxidoreductase, o-diphenol:oxygen oxidoreductase, o-diphenolase, OCA1, Orf13, oxygen oxidoreductase, phenol oxidase, phenol oxidases, phenolase, phenoloxidase, PO, polyaromatic oxidase, polyphenol oxidase, polyphenol oxidase 3, polyphenol oxidase 4, polyphenol oxidase B, polyphenolase, polyphenoloxidase, PotPPO, PPO, PPO 3, PPO B, PPO1, PPO2, PPO3, pro-PO III, prophenoloxidase III, pyrocatechol oxidase, SPRTyr, ST94, ST94t, tryosinase, tryrosinase, TY, tyr, TYR1, TYR2, tyrA, TyrBm, tyrosinase, tyrosinase 2, tyrosinase 4, tyrosinase diphenolase, tyrosine-dopa oxidase

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor

                1.14.18.1 tyrosinase

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Results	in table
132	Activating Compound
2612	AA Sequence
40	Application
1	CAS Registry Number
43	Cloned(Commentary)
10	Cofactor
12	Crystallization (Commentary)
8024	Disease/ Diagnostics
7	Expression
81	General Information
10	General Stability
803	IC50 Value
1765	Inhibitors
56	kcat/KM [mM/s]
274	Ki Value [mM]
587	KM Value [mM]
53	Localization
181	Metals/Ions
180	Molecular Weight [Da]
210	Natural Substrates/ Products (Substrates)
39	Organic Solvent Stability
469	Organism
10	Pathway
103	PDB ID
199	pH Optimum
65	pH Range
38	pH Stability
16	pI Value
30	Posttranslational Modification
61	Protein Variants
153	Purification (Commentary)
24	Reaction
3	Reaction Type
463	Reference
2	Renatured (Commentary)
328	Source Tissue
164	Specific Activity [micromol/min/mg]
35	Storage Stability
1490	Substrates and Products (Substrate)
128	Subunits
643	Synonyms
1	Systematic Name
127	Temperature Optimum [°C]
28	Temperature Range [°C]
94	Temperature Stability [°C]
220	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

all proteins including hTyrCtr and OCA1B-related mutant variants are a subjected to equilibrium unfolding/refolding using 0.001 mM protein in 10 mM phosphate buffer, pH 7.4, 5 h at 8 M urea, followed by dilution with 10 mM phosphate buffer, pH 7.4 to 0-8 M urea and incubated for 24 h at room temperature

Homo sapiens

P14679

744758

recombinant enzyme from inclusion bodies, extensive standardization of buffers and methods of refolding such as 1. dialysis, 2. on-column refolding, and 3. rapid dilution yield active PPO from solubilized inclusion bodies with copper content of 0.880 atom/molecule of protein, method development, detailed overview

Camellia sinensis

C0L3S4

746343