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Literature summary for 1.14.18.1 extracted from

  • Shuster Ben-Yosef, V.; Sendovski, M.; Fishman, A.
    Directed evolution of tyrosinase for enhanced monophenolase/diphenolase activity ratio (2010), Enzyme Microb. Technol., 47, 372-376.
No PubMed abstract available
Search for more literature for 1.14.18.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Priestia megaterium

Protein Variants

Protein Variants Comment Organism
R209H the mutant exhibits a 1.7fold increase in monophenolase activity accompanied by a 1.5fold decrease in diphenolase activity, resulting in a 2.6fold improvement in the monophenolase/diphenolase activity ratio Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.038
-
 L-tyrosine wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
0.4
-
 L-Dopa wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
0.62
-
 L-Dopa mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
1.2
-
 D-Dopa wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
1.3
-
 L-tyrosine mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
3.8
-
 D-Dopa mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography, gel filtration Priestia megaterium

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
tyrosinase
-
 Priestia megaterium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.29
-
 L-tyrosine wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
2.24
-
 L-tyrosine mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
6.35
-
 D-Dopa wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
6.88
-
 D-Dopa mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
7.18
-
 L-Dopa mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
10.59
-
 L-Dopa wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 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
1.72
-
 L-tyrosine mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
1.81
-
 D-Dopa mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
5.29
-
 D-Dopa wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
11.58
-
 L-Dopa mutant enzyme R209H, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
26.47
-
 L-Dopa wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium
34.05
-
 L-tyrosine wild type enzyme, in 50 mM Tris-HCl buffer pH 7.0, 0.01 mM CuSO4, 28°C Priestia megaterium