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1.14.18.1: tyrosinase

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

Word Map on EC 1.14.18.1

Reaction

2 L-dopa +

O2
= 2 dopaquinone + 2 H2O

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

Crystallization

Crystallization on EC 1.14.18.1 - tyrosinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
-
hanging drop vapor diffusion method, using 10% (w/v) PEG 4000, 100 mM sodium acetate buffer pH 4.6 and 5 mM HoCl3
purified recombinant detagged latent tyrosinase, X-ray diffraction structure determination and analysis. In contrast to the crystals obtained with the enzyme isolated from the natural source which contains two different chains in the asymmetric unit (one latent and one active protein) and does only form in the presence of sodium hexatungstotellurate(VI) (Na6[TeW6O24] x 22 H2O), the recombinant enzyme forms crystals containing exclusively the latent tyrosinase. The latent chain of AbPPO4 isolated from Agaricus bisporu, PDB ID 4OUA, chain B, is aligned with the heterologously produced protein, PDB ID 5M6B, chain B
purified enzyme in its resting met form with a Cu-Cu distance of 4.0 A, X-ray diffraction structure determination and analysis
-
purified recombinant wild-type enzyme and mutants A239T and F259A, hanging drop vapour diffusion technique, mixing 0f 0.001 ml of 5-10 mg/ml protein solution with 0.002 ml reservoir solution containing 50 mM Tris-HCl, pH 7.0, 19-21% PEG 3350, at 20°C, 10-15 days, method optimization, X-ray diffraction structure determination and analysis at 1.35, 1.55 and 1.70 A resolution, respectively. Soaking of crystals with a monophenolic (tyramine) and a diphenolic (dopamine) substrate in 50 mM Tris-HCl, pH 7.5, 200 mM NaCl, 20% PEG 3350, 20-25% PEG 1500, using SDS as an activator in order to perform in crystallo activity tests
sitting drop vapor diffusion method using 28% (w/v) PEG 1500, 100 mM bis-Tris buffer, pH 5.0, at 18°C, and hanging drop vapor diffusion method using 24% (w/v) PEG 2000, 10 mM NaCl, 10 mM CaCl2, and 3% 6-aminocaproic acid in 100 mM bis-Tris buffer, pH 6.5, at 18°C
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hanging drop vapor diffusion method
hanging drop vapor diffusion method, using 18% (w/v) PEG 8000, 0.2 M zinc acetate, 0.1 M cacodylic acid pH 5.6-6.1, at 16°C
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purified enzyme bound with L-tyrosine or L-dopa and zinc ions, hanging drop vapour diffusion method, mixing of 0.002 ml or 2 mg/ml protein in 20mM Tris-HCl, pH 7.5, and 500 mM NaCl, with 0.002 ml reservoir solution containing 18% PEG 8000 and 0.1 M cacodylic acid, pH 6.5, and equilibration against 0.6 ml of reservoir solution, 20°C, soaking of the crystals in inhibiting ZnCl2 before soaking them in the substrate solution in order to trap the substrates within the active site of TyrBm in the crystal, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
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