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N111Q/N337Q
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mutations in potential N-glycosylation site, 95% of wild-type L-dopa oxidase activity
N111Q/N337Q/N371Q
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mutations in potential N-glycosylation site, no L-dopa oxidase activity
N111Q/N371Q
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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/N3711Q
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mutations in potential N-glycosylation site, 37% of wild-type L-dopa oxidase activity
N86Q/N111Q
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mutations in potential N-glycosylation site, 68% of wild-type L-dopa oxidase activity
N86Q/N111Q/N337Q
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mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N111Q/N337Q/N371Q
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mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N111Q/N371Q
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mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N337Q
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mutations in potential N-glycosylation site, 35% of wild-type L-dopa oxidase activity
N86Q/N337Q/N371Q
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mutations in potential N-glycosylation site, no L-dopa oxidase activity
N86Q/N371Q
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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
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
N111Q
glycosylation site is required for recognition by individual T cell clones
N111Q
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mutation in potential N-glycosylation site, 95% of wild-type L-dopa oxidase activity
N337Q
glycosylation site is required for recognition by individual T cell clones
N337Q
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mutation in potential N-glycosylation site, 93% of wild-type L-dopa oxidase activity
N371Q
glycosylation site is required for recognition by individual T cell clones
N371Q
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mutation in potential N-glycosylation site, 64% of wild-type L-dopa oxidase activity
N86Q
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mutation in potential N-glycosylation site, 70% of wild-type L-dopa oxidase activity
N86Q
glycosylation site is required for recognition by individual T cell clones
R209H
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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
R209H
the mutant possesses a higher monophenolase/diphenolase activity ratio than the wild type enzyme
R209H
the mutant has a 45fold increase in activity towards phenol in the presence of SDS compared to the wild type enzyme
additional information
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tyrosinase overexpressing clones
additional information
mutations relative to GQ354802 mRNA for the reference sequence for AbPPO4, Uniprot ID C7FF05 : C21T, T168C, T306C, T362C (V121A), T483C, A504C, G536A (S179N), A540C, T717C, T735C, G1089A, C1104T, C1131G, G1218A, C1359T, T1449C, C1458T, A1521G, C1650T, T1686C, T1704C, G1717A (V573I), G1783A (A595T) in the wild-type AbPPO4 and C21T, G97A (V33I), G133T (A45S), T168C, G301A (V101I), G324C, T362C (V121A), T483C, A504C, G536A (S179N), A540C, G563A (R188K), C618T, C620G (A207G), T171C, T735C, G1089A, C1131G, T1172A & C1173A (L391Q), G1783A (A595T) in the mutant AbPPO4DELTA(A436-A580). Construction of a truncated enzyme mutant encoding only the main domain of the tyrosinase up to residue S383, which does not exhibit any tyrosinase activity
additional information
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mutations relative to GQ354802 mRNA for the reference sequence for AbPPO4, Uniprot ID C7FF05 : C21T, T168C, T306C, T362C (V121A), T483C, A504C, G536A (S179N), A540C, T717C, T735C, G1089A, C1104T, C1131G, G1218A, C1359T, T1449C, C1458T, A1521G, C1650T, T1686C, T1704C, G1717A (V573I), G1783A (A595T) in the wild-type AbPPO4 and C21T, G97A (V33I), G133T (A45S), T168C, G301A (V101I), G324C, T362C (V121A), T483C, A504C, G536A (S179N), A540C, G563A (R188K), C618T, C620G (A207G), T171C, T735C, G1089A, C1131G, T1172A & C1173A (L391Q), G1783A (A595T) in the mutant AbPPO4DELTA(A436-A580). Construction of a truncated enzyme mutant encoding only the main domain of the tyrosinase up to residue S383, which does not exhibit any tyrosinase activity
additional information
generation of the recombinant human tyrosinase intra-melanosomal domain and mutant variants, which mimic genetic changes in both subtypes of OCA1 patients, by site-directed mutagenesis and recombinant expression in insect cells. The recombinant OCA1A show very low protein expression, protein yield, and are enzymatically inactive, while mutants mimicking OCA1B are biochemically similar to the wild-type, but exhibit lower specific activities and protein stabilities than the wild-type enzyme
additional information
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generation of the recombinant human tyrosinase intra-melanosomal domain and mutant variants, which mimic genetic changes in both subtypes of OCA1 patients, by site-directed mutagenesis and recombinant expression in insect cells. The recombinant OCA1A show very low protein expression, protein yield, and are enzymatically inactive, while mutants mimicking OCA1B are biochemically similar to the wild-type, but exhibit lower specific activities and protein stabilities than the wild-type enzyme
additional information
the strategy of deleting the membrane-anchoring helix is standard to simplify handling of protein. Deletion of the anchoring helix of the human tyrosinase does not affect the tyrosinase activity
additional information
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the strategy of deleting the membrane-anchoring helix is standard to simplify handling of protein. Deletion of the anchoring helix of the human tyrosinase does not affect the tyrosinase activity
additional information
generation of a truncated enzyme comprisine residues 101-445
additional information
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generation of several PPO-silenced RNAi transgenic lines that show over 95% reduction in catechol oxidase activity relative to wild-type controls, the plants develop a phenotype with disease-like necrotic lesions. Levels of salicylic acid, H2O2, or malondialdehyde are not significantly different in the PPO-silenced leaves compared to wild-type leaves. Metabolomic analysis of PPO-silenced and wild-type leaves reveal significant differences in many metabolites, particularly phenylpropanoids, and about 10fold increased levels of tyramine. Although L-DOPA is undetectable in both PPO-silenced and wild-type walnut plants, levels of dopamine (derived from either L-DOPA or tyramine) and 5,6 dihydroxyindole (derived from L-DOPA) are reduced approximately 6 and 100fold, respectively, in PPO-silenced plants relative to wild-type controls
additional information
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homogentisate 1,2-dioxygenase mutant with 3.8fold lower tyrosine activity compared to wild-type (induced with ferulic acid), no detectable activity with L-tyrosine induction within 2 h, pigment production 6fold higher than in wild-type after 20 h, biomass yield of mutant grown on tyrosine as sole carbon and energy source is 1.2fold lower than wild-type, higher UV (5 min at 254 nm) survival rate of both mutants (73-79%) than wild-type (42%) (colonies grown on agar plates and resuspended), 1.5fold smaller zones of inhibition under 10 mM hydrogen peroxide stress compared to wild-type and transcriptional regulator mutant, transcription regulator mutant with 3.7fold higher tyrosine activity compared to wild-type (induced with ferulic acid), 3.5fold higher activity without induction, 4.7fold higher activity with tyrosine induction, higher UV resistance than wild-type and similar melanin production as wild-type after 48 h (higher levels only after long term incubation), tyrosine uptake 8times higher than in wild-type (after an initial lag-phase of 3 h). Laccase and superoxide dismutase activity is similar in wild-type and both mutants, catalase activity is 1.5fold higher in homogentisate 1,2-dioxygenase mutant and peroxidase activity 2.1fold higher than wild-type, transcription regulator mutant with similar catalase activity as wild-type, and with 2.3fold lower peroxidase activity than wild-type
additional information
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enzyme immobilization on electrospun nylon nanofiber membranes
additional information
enzyme immobilization on electrospun nylon nanofiber membranes
additional information
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enzyme immobilization on electrospun nylon nanofiber membranes
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additional information
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low PPO mutant with greatly reduced levels of PPO activity (low PPO mutant, LP)
additional information
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enzyme immobilization on electrospun nylon nanofiber membranes