Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.18.1 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)

Crystallization (Comment) Organism
-
Priestia megaterium

Protein Variants

Protein Variants Comment Organism
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
-
L-Dopa mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium
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
1.4
-
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)

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

Organism

Organism UniProt Comment Textmining
Priestia megaterium B2ZB02
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
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
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
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
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
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
80
-
L-tyrosine wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C Priestia megaterium