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Literature summary extracted from

  • Goldfeder, M.; Kanteev, M.; Adir, N.; Fishman, A.
    Influencing the monophenolase/diphenolase activity ratio in tyrosinase (2013), Biochim. Biophys. Acta, 1834, 629-633.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.18.1
-
 Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.14.18.1 V218F the monophenolase activity of the mutant on L-tyrosine improves, as the Vmax and kcat values increase 4.2fold. Th same values for diphenolase activity on L-Dopa, however, decrease 2.1fold Priestia megaterium
1.14.18.1 V218G in this mutant, the Vmax and kcat values towards L-tyrosine increase by 7.8fold and towards L-DOPA by 1.7fold, respectively Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.18.1 0.05
-
 L-tyrosine wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 0.5
-
 L-tyrosine mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 0.8
-
 L-Dopa wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 1
-
 L-Dopa mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 1.1
-
 L-Dopa mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 1.4
-
 L-tyrosine mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.18.1 L-DOPA + O2 Priestia megaterium
-
 L-dopachrome + H2O
-
 ?
1.14.18.1 L-tyrosine + O2 Priestia megaterium
-
 dopaquinone + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.1 Priestia megaterium B2ZB02
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.1 L-DOPA + O2
-
 Priestia megaterium L-dopachrome + H2O
-
 ?
1.14.18.1 L-tyrosine + O2
-
 Priestia megaterium dopaquinone + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.18.1 4
-
 L-tyrosine wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 16.7
-
 L-tyrosine mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 21
-
 L-Dopa wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 31.1
-
 L-Dopa mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 44.1
-
 L-tyrosine mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 73.3
-
 L-Dopa mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.18.1 11.9
-
 L-tyrosine mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 19.1
-
 L-Dopa wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 55.1
-
 L-tyrosine mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 62.1
-
 L-Dopa mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 73.7
-
 L-Dopa mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
1.14.18.1 80
-
 L-tyrosine wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium