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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

Engineering

Engineering on EC 1.14.18.1 - tyrosinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N111Q
N111Q/N337Q
-
mutations in potential N-glycosylation site, 95% of wild-type L-dopa oxidase activity
N111Q/N337Q/N371Q
-
mutations in potential N-glycosylation site, no L-dopa oxidase activity
N111Q/N371Q
-
mutations in potential N-glycosylation site, 59% of wild-type L-dopa oxidase activity
N161Q
similar properties as wild-type
N230Q
similar properties as wild-type
N290Q
similar properties as wild-type
N337Q
N337Q/N3711Q
-
mutations in potential N-glycosylation site, 37% of wild-type L-dopa oxidase activity
N371Q
N86Q/N111Q
-
mutations in potential N-glycosylation site, 68% of wild-type L-dopa oxidase activity
N86Q/N111Q/N337Q
-
mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N111Q/N337Q/N371Q
-
mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N111Q/N371Q
-
mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N337Q
-
mutations in potential N-glycosylation site, 35% of wild-type L-dopa oxidase activity
N86Q/N337Q/N371Q
-
mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N371Q
-
mutations in potential N-glycosylation site, 30% of wild-type L-dopa oxidase activity, contains at least 3 times less copper than wild-type
P406L
a phenotype OCA1A-related mutant, inactive mutant
R402Q
a phenotype OCA1A-related mutant, inactive mutant
R422Q
a phenotype OCA1A-related mutant, inactive mutant
R422W
a phenotype OCA1A-related mutant, inactive mutant
R77Q
a phenotype OCA1A-related mutant, inactive mutant
T373K
a phenotype OCA1A-related mutant, inactive mutant
A239T
site-directed mutagenesis, mutation of an activity controller residue
E234A
site-directed mutagenesis, mutation of the water-keeper residue
F259A
site-directed mutagenesis, mutation of the gatekeeper residue
L243R
site-directed mutagenesis, mutation of an activity controller residue
M374G
potential to delete the enzymatic activity of Tyr. Major effect on the active site: the packing density of this normally rigid environment is significantly lowered when the original amino acid is mutated to the smaller glycine because the missing side chain of G374 can neither anchor the loop nor orient the side chain of H367
M374G/S375G
Tyr-GG double mutant, potential to delete the enzymatic activity of Tyr. The M374G/S375G mutation, designated Tyr-GG, replaces two residues present in mTyr by the equivalent residues in mTyrp1 and could potentially modify the enzymatic properties of the protein, when compared with wild-type Tyr. Analysis of the behaviour of the individual mutants M374G and S374G indicates that loss of enzymatic activity in Tyr-GG is mostly because of the M374G mutation
S375G
potential to delete the enzymatic activity of Tyr
R209H
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
V218G
in this mutant, the Vmax and kcat values towards L-tyrosine increase by 7.8fold and towards L-DOPA by 1.7fold, respectively
145-D317Y
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
145-L330V
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
145-V153A
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
145-Y119F
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
C10-F185Y
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
C10-N322S
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
C10-T183I
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
C10-T359M
the overall catalytic efficiency for the variant has improved compared to the wild type for D-tyrosine
RV145
the random mutation variant exhibits a 3.2fold increase in kcat, respectively, compared to the wild type while the Km is 5.2fold lower. The overall catalytic efficiency for the variant has improved 16fold compared to the wild type for D-tyrosine
RVC10
the random mutation variant exhibits a 2.1fold increase in kcat, respectively, compared to the wild type while the Km is 3.2fold lower. The overall catalytic efficiency for the variant has improved 6.7fold compared to the wild type for D-tyrosine
additional information