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C807T
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naturally occuring polymorphism involved in gastric cancer development
K246R
natural mutation observed in female infant patient with lack in transformylase activity and about 40% residual enzymic activity, showing massive excretion of 5-amino-4-imidazolecarboxamide riboside, dysmorphic features, severe neurological defects, and congenital blindness. Recombinant protein with K426R mutation completely lacks AICAR transformylase activity
C61A
site-directed mutagenesis, the mutant shows 8fold increased activity compared to the wild-type enzyme
E102Q
site-directed mutagenesis, inactive mutant
R31K
site-directed mutagenesis, the mutant shows 76% reduced activity compared to the wild-type enzyme
Y59F
site-directed mutagenesis, the mutant shows 34% reduced activity compared to the wild-type enzyme
H256A
complete loss of activity, mutation lowers the thermostability
K255A
complete loss of activity, mutation lowers the thermostability
K255R
mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C
N415A
decrease in AICAR transformylase activity as compared with wild-type SlugATIC, indicating it might also play essential role in substrate binding. Increase in the thermostability
D125A
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dramatically reduced kcat-value
D125A
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10fold increase in KM-value
D125E
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dramatically reduced kcat-value
D125E
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5fold increase in Km-value
D125N
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dramatically reduced kcat-value
D125N
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3fold increase in Km-value
K137A
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dramatically reduced kcat-value
K137A
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30fold increase in KM-value, 30fold decrease in kcat-value
K137R
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dramatically reduced kcat-value
K137R
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3fold increase in KM-value15fold decrease in kcat-value
K66A
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dramatically reduced kcat-value
K66A
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more than 100fold increase in KM-value
Y104A
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dramatically reduced kcat-value
Y104A
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decrease in kcat-value by one orders of magnitude
Y104A/D125A
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no enzymic activity
Y104A/D125A
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enzyme activity very low but detectable, contrary to wild type a minimal dependence of specific activity on concentration
Y104F
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dramatically reduced kcat-value
Y104F
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decrease in kcat-value by two orders of magnitude
Y104F/D125A
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enzyme activity very low but detectable, contrary to wild type a minimal dependence of specific activity on concentration
Y104F/D125A
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no enzymice activity