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I140V
Aspergillus luchuensis var. saitoi
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about 25% decrease in catalytic efficiency
V197D
Aspergillus luchuensis var. saitoi
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about 25% decrease in catalytic efficiency
I140V
Aspergillus luchuensis var. saitoi KBN 2022
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about 25% decrease in catalytic efficiency
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V197D
Aspergillus luchuensis var. saitoi KBN 2022
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about 25% decrease in catalytic efficiency
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R227W
EDW21517
increase in expression and specific activity, no increase in thermostability
R227W/S145C/T206A
EDW21517
increase in specific activity and thermostability
R227W/S145C/T50T
EDW21517
increase in specific activity and thermostability
R227W/T206A/T222T
EDW21517
increase in specific activity and thermostability
R235A
site-directed mutagenesis, inactive catalytic residue mutant
R227W
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increase in expression and specific activity, no increase in thermostability
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R227W/S145C/T206A
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increase in specific activity and thermostability
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R227W/S145C/T50T
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increase in specific activity and thermostability
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R227W/T206A/T222T
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increase in specific activity and thermostability
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R235A
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site-directed mutagenesis, inactive catalytic residue mutant
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D106N
mutant enzyme without pectate lyase activity
D126N
the ratio of turnover number to Km-value is 57.5% of the wild-type value
D63N
mutant enzyme without pectate lyase activity
D80N
the ratio of turnover number to Km-value is 93% of the wild-type value
D84N
the ratio of turnover number to Km-value is 28.6% of the wild-type value
E38Q
mutant enzyme without pectate lyase activity
E47Q
mutant enzyme retains almost full activity relative to wild-type enzyme
E83Q
mutant enzyme without pectate lyase activity
H66A
the ratio of turnover number to Km-value is 70.4% of the wild-type value
K107A
mutant enzyme without pectate lyase activity
K107H
mutant enzyme without pectate lyase activity
K107R
mutant enzyme without pectate lyase activity
K129A
mutant enzyme without pectate lyase activity
K129H
mutant enzyme without pectate lyase activity
K129R
mutant enzyme is not produced extracellularly
K182A
mutant enzyme retains almost full activity relative to wild-type enzyme
K185A
mutant enzyme retains almost full activity relative to wild-type enzyme
K20A
mutant enzyme retains almost full activity relative to wild-type enzyme
K41A
the ratio of turnover number to Km-value is 105% of the wild-type value
K89A
the ratio of turnover number to Km-value is 31.5% of the wild-type value
R132A
mutant enzyme without pectate lyase activity
R132H
mutant enzyme without pectate lyase activity
R132K
mutant enzyme without pectate lyase activity
R152A
mutant enzyme retains almost full activity relative to wild-type enzyme
W78F
the ratio of turnover number to Km-value is identical to wild-type value
W78Y
mutant enzyme with slightly increased activity relative to wild-type enzyme
Y174A
the ratio of turnover number to Km-value is 90.7% of the wild-type value
D80N
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the ratio of turnover number to Km-value is 93% of the wild-type value
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D84N
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the ratio of turnover number to Km-value is 28.6% of the wild-type value
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K41A
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the ratio of turnover number to Km-value is 105% of the wild-type value
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K89A
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the ratio of turnover number to Km-value is 31.5% of the wild-type value
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E124I
mutant displays increased thermostability
E124I/T178A/N186D/I211V/A254T/S271G/N289H
140fold increase in the t50 value at 50°C, accompanied by an 84.3% decrease in activity
K313R
mutation does not improve thermostability
N186D/I211V/A254T/S271G/N289H
24fold increase in the t50 value at 50°C, with a 23.3% increase in activity
R72S
mutation does not improve thermostability
S233C
mutation does not improve thermostability
S271G
mutant displays increased thermostability
S308L
mutation does not improve thermostability
T178A
mutant displays increased thermostability
D173A
the mutation results in approximately 40% of wild type activity
D173A/N180A/K247A
the mutation results in approximately 0.2% of wild type activity
D173A/N180N
the mutation results in approximately 5% of wild type activity
K47D/V132F
2.2fold improvement in specific activity compared to wild-type
K47D/V132F/R272W
specific activity is significantly improved by about 400% in the presence of 1 mM Ca2+. Half-life at 50°C is extended to 330 min. Mutant can significantly improve the wettability and softness of fabrics
K47E
displays 1.8fold increase in activity, and half-life increased by 2.0fold at 50°C
K47E/V132F
3.9fold improvement in specific activity compared to wild-type
N180A
the mutation results in approximately 30% of wild type activity
V132F
mutant shows 1.7fold increase in activity with wider pH stability
K47D/V132F
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2.2fold improvement in specific activity compared to wild-type
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K47D/V132F/R272W
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specific activity is significantly improved by about 400% in the presence of 1 mM Ca2+. Half-life at 50°C is extended to 330 min. Mutant can significantly improve the wettability and softness of fabrics
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K47E
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displays 1.8fold increase in activity, and half-life increased by 2.0fold at 50°C
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K47E/V132F
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3.9fold improvement in specific activity compared to wild-type
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V132F
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mutant shows 1.7fold increase in activity with wider pH stability
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D107N
complete loss of activity, crystallization data
E84A
complete loss of activity
K108A
complete loss of activity, crystallization data
K108A/D107N
crystallization data
K108A/E39Q
crystallization data
K108A/Q111A
crystallization data
K108A/Q111N
crystallization data
K108A/R133A
crystallization data
D107N
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complete loss of activity, crystallization data
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E84A
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complete loss of activity
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K108A
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complete loss of activity, crystallization data
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K108A/E39Q
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crystallization data
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K108A/Q111A
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crystallization data
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D154E
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mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 1.2fold higher than the Km-value of the wild-type enzyme
D154N
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mutant enzyme with 44% of the activity of the wild-type enzyme, the Km-value for the substrate lime pectin (with 75% methyl esterification) is 2.3fold higher than the Km-value of the wild-type enzyme. The pH-optimum is higher than that of the wild-type enzyme
K224R
mutant is completely defective in lyase activity
K249R
mutant shows 40-60% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected
K273A
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inactive but correctly folded enzyme
N215S/T217S/S219G/A220S
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the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE
R218K
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inactive mutant enzyme R218K. Crystals of mutant enzyme R218K are isomorphous with wild-type PelC crystals and belong to space group P2(1)2(1)2(1) with unit cell parameters of a = 72.14 A, b = 78.32 A and c = 94.43 A
R236K
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mutant enzyme with 0.2% of the activity of the wild-type enzyme
R236Q
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inactive mutant enzyme
R252K
mutant shows 6-9% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected
N215S/T217S/S219G/A220S
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the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE
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D174A
mutation in Ca2+ binding site, complete loss of activity
K93I
1.75fold increase in specific activity, folding free energy decreases by 1.03 kcal/ml
C132I/C156N/C194L
mutations increase expression level
D125
loss of catalytic activity
D147
loss of catalytic activity
D125
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loss of catalytic activity
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D147
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loss of catalytic activity
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N198A
95% of wild-type activity
N198D
77% of wild-type activity
N198Q
72% of wild-type activity
N95A
38% of wild-type activity
N95D
51% of wild-type activity
N95Q
54% of wild-type activity
N95S
81% of wild-type activity
additional information
chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal regions: the ratio of turnover number to Km-value is 5.1% of the wild-type value
additional information
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chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal regions: the ratio of turnover number to Km-value is 5.1% of the wild-type value
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additional information
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construction of CcpelA gene-disrupted mutants, the mutants show reduced aggressiveness towards tomato fruits and impaired pectate lyase secretion and extracellular activity
additional information
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regulation of pectate lyase secretion by knocking out PAC1, which encodes the PacC transcription factor that regulates gene products with pH-sensitive activities is studied. Loss-of-function PAC1 mutants show 85% reduction of PELB transcript expression, delayed pectate lyase secretion and dramatically reduced virulence, as detected in infection assays with avocado fruits. PELB is up-regulated in the presence of carbon sources. When glucose is used as a carbon source in the medium for the WT strain and the knock out pac1 mutant PELB transcript expression and PL secretion are activated
additional information
genetic inactivation, function of the pecCl1 gene is assessed using the genetic inactivation strategy known as split-marker, protoplast transformation, molecular phenotype, overview
additional information
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genetic inactivation, function of the pecCl1 gene is assessed using the genetic inactivation strategy known as split-marker, protoplast transformation, molecular phenotype, overview
additional information
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in a gacA deletion mutant the production of pectate lyase, protease, and cellulase is diminished in mutant cells compared with the wild-type cells
additional information
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construction of mutants, type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
additional information
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construction of mutants, type II secretion system-deficient mutant of Dickeya dadantii 3937, A1919, DELTA ouC, loses the capability to promote the multiplication of EDL933, whereas Ech159, DELTApoS, a stress-responsive sigma-factor RpoS-deficient mutant, increases EDL933 proliferation on lettuce leaves 2fold mor than the wild-type strain. Mutant A1919 is completely deficient in the secretion of pectate lyases, which play a major role in plant tissue maceration
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additional information
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transgenic lines exhibiting a greater than 90% reduction in pectate lyase transcript abundance are generated. Wall extracts from transgenic fruits show a reduction in pectin solubility and decreased depolymerization of more tightly bound polyuronides. Additional patterns of differential extraction of other wall-associated pectin subclasses are apparent, particularly in the sodium carbonate and chelator-soluble polymers. Microscopic studies reveal that the typical ripening-associated loss of cell-cell adhesion is substantially reduced in the transgenic fruits
additional information
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improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
additional information
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improvement of thermostability and activity of pectate lyase in the presence of hydroxyapatite nanoparticles
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