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N202Q
-
T50-value is 3°C lower than wild-type value. Vmax towards p-nitrophenyl-alpha-L-arabinofuranoside is 0.76fold of wild-type value. No significant effect on kcat/Km with p-nitrophenyl-alpha-L-arabinofuranoside as substrate. Significant decrease in specific activity towards arabinan and debranched arabinan compared to wild-type enzyme
N83Q
-
T50-value is 1°C lower than wild-type value. No significant effect on kcat/Km
N83Q/N202Q
-
T50-value is 3°C lower than wild-type valueVmax towards p-nitrophenyl-alpha-L-arabinofuranoside is 0.71fold of wild-type value. No significant effect on kcat/K with p-nitrophenyl-alpha-L-arabinofuranoside as substrate. Significant decrease in specific activity towards arabinan and debranched arabinan compared to wild-type enzyme
N83Q
the mutant is not glycosylated but shows about wild type activity
Y312F
the mutant shows significantly reduced activity compared to the wild type enzyme
Y312S
the mutant shows significantly reduced activity compared to the wild type enzyme
N83Q
-
the mutant is not glycosylated but shows about wild type activity
-
Y312F
-
the mutant shows significantly reduced activity compared to the wild type enzyme
-
Y312S
-
the mutant shows significantly reduced activity compared to the wild type enzyme
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E170A
-
site-directed mutagenesis of a catalytic residue, inactive mutant
E242A
-
site-directed mutagenesis of a catalytic residue, the mutant shows 7% of wild-type enzyme activity
Y337A
-
site-directed mutagenesis of a catalytic residue, inactive mutant
E175A
site-directed mutagenesis, altered kinetic properties
E294A
site-directed mutagenesis, reduced activity and about 10fold increased Km for substrate 2',4',6'-trichlorophenyl alpha-L-arabinofuranoside compared to the wild-type enzyme
E175A
-
site-directed mutagenesis, altered kinetic properties
-
E294A
-
site-directed mutagenesis, reduced activity and about 10fold increased Km for substrate 2',4',6'-trichlorophenyl alpha-L-arabinofuranoside compared to the wild-type enzyme
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L307S
-
the mutant shows almost 2.5fold increased activity and exhibits higher thermal stability but lower alkaline stability compared to the wild type enzyme
Q90H/L307S
-
the mutant shows almost 2.5fold increased activity and exhibits higher thermal stability but lower alkaline stability compared to the wild type enzyme
L307S
-
the mutant shows almost 2.5fold increased activity and exhibits higher thermal stability but lower alkaline stability compared to the wild type enzyme
-
Q90H/L307S
-
the mutant shows almost 2.5fold increased activity and exhibits higher thermal stability but lower alkaline stability compared to the wild type enzyme
-
E449G
about 10% of wild-type activity
F435Y/Y446F
random mutagenesis, the mutant shows 3fold increased activity and altered substrate specificity and is active with larch arabinogalactan in contrast to the wild-type enzyme
S160G
catalytic properties are slightly changed. The mutation negatively affects the stability of the enzyme at various pHs and temperatures. Circular dichroism analyses show a minimum at 210 nm for wild-type, which is shifted for mutant S160G, suggesting the presence of an unfolded structure, with a role of the glycosylation at the S160 residue for secondary structure stability
H337K
-
the mutation prolongs the half-life of thermal inactivation at 50°C 5fold versus the wild type, and the specific activity of this mutant is increased
K208W
-
the mutation enhances the half-life of thermal inactivation at 50°C more than 11.1times versus the wild type
H337K
-
the mutation prolongs the half-life of thermal inactivation at 50°C 5fold versus the wild type, and the specific activity of this mutant is increased
-
K208W
-
the mutation enhances the half-life of thermal inactivation at 50°C more than 11.1times versus the wild type
-
D127A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 191860fold lower than wild-type value
D14A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 2727fold lower than wild-type value
E186A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 18333fold lower than wild-type value
F31A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 9.5fold lower than wild-type value
F508A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 18fold lower than wild-type value
H248A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 334fold lower than wild-type value
R290A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 1765fold lower than wild-type value
R290G
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 3028fold lower than wild-type value
R290H
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 1089fold lower than wild-type value
R290K
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 314fold lower than wild-type value
R290Q
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is213fold lower than wild-type value
R290V
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 1709fold lower than wild-type value
W73A
-
kcat/Km for p-nitrophenyl-alpha-L-arabinofuranoside is 2520fold lower than wild-type value
D20N
-
the mutant shows 0.7% of wild type activity
L289A
-
the mutant shows 10% of wild type activity
N159A
-
the mutant shows 1.5fold increased activity compared to the wild type
N159L
-
the mutant shows 19fold increased activity compared to the wild type
Y192A
-
the mutant shows 40% of wild type activity
D165E
site-directed mutagenesis
D165N
site-directed mutagenesis
D202N
site-directed mutagenesis, inactive mutant
E324Q
site-directed mutagenesis
E361Q
site-directed mutagenesis, inactive mutant
N425Q
site-directed mutagenesis
N462Q
site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme
W233A
site-directed mutagenesis
W233F
site-directed mutagenesis
W233Y
site-directed mutagenesis
W270A
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
W270F
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme
W270Y
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
Y424A
site-directed mutagenesis
Y424F
site-directed mutagenesis
Y424W
site-directed mutagenesis
Y461A
site-directed mutagenesis, the mutant shows 20% reduced activity compared to the wild-type enzyme
Y461F
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type enzyme
Y461W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D165E
-
site-directed mutagenesis
-
D165N
-
site-directed mutagenesis
-
D202N
-
site-directed mutagenesis, inactive mutant
-
E324Q
-
site-directed mutagenesis
-
E361Q
-
site-directed mutagenesis, inactive mutant
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R239A
-
the activity of the mutant enzyme with wheat arabinoxylan is reduced by 100times compared to the wild type enzyme
R239A/F212A
-
the activity of the mutant enzyme with wheat arabinoxylan is reduced by 200times compared to the wild type enzyme
R239A/F212A/I233A
-
the activity of the mutant enzyme with wheat arabinoxylan is reduced by 8000times compared to the wild type enzyme
R239A/I233A
-
the activity of the mutant enzyme with wheat arabinoxylan is reduced by 250times compared to the wild type enzyme
R239K
-
the activity of the mutant enzyme with wheat arabinoxylan is reduced by 100times compared to the wild type enzyme
R239S
-
the activity of the mutant enzyme with wheat arabinoxylan is reduced by 150times compared to the wild type enzyme
C180A
site-directed mutagenesis, reduced thermostability
D55A
site-directed mutagenesis, activity is similar to wild-type enzyme activity
E112A
site-directed mutagenesis, activity is similar to wild-type enzyme activity
E143A
site-directed mutagenesis, activity is similar to wild-type enzyme activity
E176A
site-directed mutagenesis, exchange of the acid-base residue, nearly inactive mutant, 8925fold reduced activity compared to the wild-type enzyme
E176D
site-directed mutagenesis, exchange of the acid-base residue, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E28A
site-directed mutagenesis, nearly inactive mutant, 5950fold reduced activity compared to the wild-type enzyme
E28A/E176A
site-directed mutagenesis, completely inactive mutant
E28D
site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E298A
site-directed mutagenesis, nearly inactive mutant, 178500fold reduced activity compared to the wild-type enzyme
E298D
site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E298Q
site-directed mutagenesis, mutant enzyme shows increased sensitivity to pH and a lower pH optimum compared to the wild-type enzyme
G179F
mutant displays stronger xylotriose-mediated inhibition than wild-type
H98A
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
H98A/W99A
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
H98F
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
H98F/W99F
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
L352M
37fold increase of the KM value, mutant displays increased transglycosylation activity (about 18%)
M94_I103delinsGG
site-directed mutagenesis, 70fold less active than the wild-type enzyme
N216W
almost total absence of inhibition by xylotriose
R69H
mutant displays severely reduced specific activity and biphasic reaction profile. Transglycosylation activitiy is increased
R69H/G179F/L352M
mutant displays severely reduced specific activity and biphasic reaction profile and is activated in the presence of xylotriose. Transglycosylation activitiy is increased
R69H/L352M
activity increases up to 260% in the presence of xylotriose, whereas wild-type is inhibited
R69H/N216W/L352M
mutant displays severely reduced specific activity and biphasic reaction profile and is activated in the presence of xylotriose. Transglycosylation activitiy is increased
W99F
-
site-directed mutagenesis, the mutant shows affected kinetics, reduced activity, and altered binding of the aglycon motif in the active site compared to the wild-type enzyme
D170N
-
kcat is 31fold lower than wild-type value
D221N
-
significant decrease in catalytic activity, kcat is 7000fold lower than wild-type value
D299G
-
kcat is 263fold lower than wild-type value
D299N
-
significant decrease in catalytic activity, kcat is 1300fold lower than wild-type value
E223Q
-
enzyme is nearly inactive
E310G
-
kcat is 70fold lower than wild-type value
D170N
-
kcat is 31fold lower than wild-type value
-
D221N
-
significant decrease in catalytic activity, kcat is 7000fold lower than wild-type value
-
D299G
-
kcat is 263fold lower than wild-type value
-
D299N
-
significant decrease in catalytic activity, kcat is 1300fold lower than wild-type value
-
E223Q
-
enzyme is nearly inactive
-
E296A
AM283040
about 1600fold decrease in activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
E296A
-
about 1600fold decrease in activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
-
E176Q
site-directed mutagenesis, inactive mutant
E176Q
site-directed mutagenesis, exchange of the acid-base residue, mutant enzyme is insensitive to pH
E28Q
site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E28Q
site-directed mutagenesis, mutant enzyme shows increased sensitivity to pH and a lower pH optimum compared to the wild-type enzyme
W99A
site-directed mutagenesis, the arabinosyl moiety is not correctly bound in the active site when Trp99 is replaced by Ala
W99A
-
site-directed mutagenesis, the mutation causes the loss of a hydrogen bond and leads to an alternative binding mode that is detrimental for catalysis, altered binding of the aglycon motif in the active site, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
additional information
identification of a T-DNA insertion mutant of AtBXL1, that shows mucilage release both patchy and slow, and the seeds display delayed germination. While developmental analysis of mutant seeds reveals no change in mucilage secretory cell morphology, changes in monosaccharide quantities are detected, suggesting the mucilage release defect results from altered mucilage composition. bxl1 Mutant seeds and antibody staining of developing seed coats reveal an increase in alpha-1,5-linked arabinans, phenotype, overview. Mutational analysis of the genetic interactions between AtBXL1 and MSC-related transcription factors
additional information
individually expressed catalytic GH43 module does not show hydrolytic activity, the purified CBM6 binds to soluble arabinoxylan
additional information
-
individually expressed catalytic GH43 module does not show hydrolytic activity, the purified CBM6 binds to soluble arabinoxylan
-
additional information
-
construction of an isozyme pfabf62c mutant pfabf62cDELTACBM truncated of the DNA region encoding canonical cellulose binding module, CBM1