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the enzyme is induced by 24-epibrassinolide signalling, auxin, cytokinin, phosphate deficiency, abscisic acid, and salt stress. NPC4 does demonstrate a positive response to Botrytis cinerea, Golovinomyces orontii, Pseudomonas syringae and Phytophthora infestans treatment
E4D
significant decrease in catalytic efficiency
E4L
significant decrease in catalytic efficiency
E4Q
significant decrease in catalytic efficiency
F66A
dramatic decrease in catalytic efficiency
F66R
dramatic decrease in catalytic efficiency
F66Y
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the mutant enzyme can remove up to 90% of phosphatidylethanolamine while retaining its efficiency at hydrolyzing phosphatidylcholine
Y56A
little decrease in catalytic efficiency
Y56R
little decrease in catalytic efficiency
Y56W
little decrease in catalytic efficiency
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isoform Plc-2 inactivation mutant shows decreased extracellular enzyme activity. Plc-2 is involved in plaque formationand has a significant role in host cell cytotoxicity
D293S
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reduced hemolytic activity, reduced cytotoxic and myotoxic activities, reduced activity against p-nitrophenylphosphorylcholine, increased dependence on Ca2+
D305G
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reduced hemolytic activity, reduced cytotoxic and myotoxic activities, significantly increased activity against p-nitrophenylphosphorylcholine
H148G
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pretreatment of the inactive mutant H148G losing PLC and SMase activities does not affect the production of NO and tumor necrosis factor-alpha in lipopolysaccharide-stimulated RAW264.7 cells
K330E
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reduced hemolytic activity, reduced cytotoxic and myotoxic activities
hNPP6-ex
truncated form of hNPP6, cDNA for the extracellular domain of hNPP6, amino acids 1-421
D251V
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
D314V
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
D63V
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
E286A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
F167A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
F244A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
F253A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H166N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H179N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H247N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H257N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H284N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H409N
site-directed mutagenesis, the mutant enzyme shows similar catalytic activity as the wild-type enzyme
R265Q
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
R326Q
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
R365Q
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
S336A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
Y156A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H179N
-
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
H284N
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site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
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R265Q
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site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
S336A
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site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
C143S
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the mutant shows increased activity compared to the wild type enzyme
C168S
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the mutant shows decreased activity compared to the wild type enzyme
C28A/C29A/D30A
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site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
D30A/E31A
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site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 75% of wild-type level
D55N
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the mutation causes a dramatic loss of activity
E31A
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site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
E31A/Y32A/L33A
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site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 42% of wild-type level
F66Y
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the mutation causes a dramatic loss of activity
H56Y
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the activity of the mutant is comparable to the wild type enzyme
L33A
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site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 54% of wild-type level
P36A
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site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 82% of wild-type level
Q34A/T35A
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site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
Q34A/T35A/P36A
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site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 79% of wild-type level
Q34K/T35P
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site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
Y32A
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site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 68% of wild-type level
mNPP6-ex
truncated form of hNPP6, cDNA for the extracellular domain of mNPP6 with Myc tag at the carboxyl terminus
T178A
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site-directed mutagenesis, hydrolytically inactive mutant. The PlcHR 2 T178A mutant is also unable to induce vesicle aggregation or release intravesicular aqueous contents in contrast to the wild-type enzyme
F66W
catalytic activity comparable to wild type
F66W
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the mutant enzyme can remove up to 90% of phosphatidylethanolamine while retaining its efficiency at hydrolyzing phosphatidylcholine
additional information
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amino acid sequence differs from that of strain SBUG516 by substitution D173E
additional information
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amino acid sequence differs from that of strain SBUG516 by substitution E173D
additional information
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amino acid sequence differs from that of strain SBUG516 by substitution D173E
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additional information
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amino acid sequence differs from that of strain SBUG516 by substitution E173D
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additional information
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amino acid sequence differs from that of strain SBUG516 by substitution D173E
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additional information
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amino acid sequence differs from that of strain SBUG516 by substitution E173D
-
additional information
isoform Plc-1 inactivation mutant shows decreased extracellular enzyme activity. Plc-1 has no effect on plaque-forming efficinecy, but increases the efficiency of isoform Plc-2 to form plaques
additional information
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isoform Plc-1 inactivation mutant shows decreased extracellular enzyme activity. Plc-1 has no effect on plaque-forming efficinecy, but increases the efficiency of isoform Plc-2 to form plaques
additional information
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separate expression of amino- and C-terminal fragments of enzyme, requirements for reconstitution of enzyme activity and activation by Gbetagamma
additional information
construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
additional information
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construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
additional information
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construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
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additional information
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construction and generation of PC-PLC propeptide deletion mutants
additional information
plcC-deficient mutants to determine whether PlcC contributes to the hemolytic activity of MFN1032. Construction of a plcC-overexpressing MFN1032 clone: MFN1036
additional information
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plcC-deficient mutants to determine whether PlcC contributes to the hemolytic activity of MFN1032. Construction of a plcC-overexpressing MFN1032 clone: MFN1036
additional information
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construction of a series of fragments, N-terminal Gbetagamma binding region in first 180 amino acids of enzyme, amino acids 150-180 are required for interaction with Gbetagamma, mutations in this region reduce binding capacity and ability to be activated by Gbetagamma
additional information
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overexpression of enzyme induces overexpression of cyclin D3
additional information
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generation of a SMc00171-deficient mutant, which is inactive with phosphatidylcholine. SMc00171 restores phosphatidylcholine and phosphatidylethanolamine degradation in a smc00171-deficient mutant