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Results 1 - 8 of 8
EC Number
Amino acid exchange
Commentary
Reference
D42A
inactive, the mutation leads to a concomitant loss of the metal ion
H45A
by site-directed mutagenesis, mutant enzyme has 24fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values
H45A
the mutation leads to a decrease in kcat of the enzyme by 78fold
H45Q
by site-directed mutagenesis, mutant enzyme has 69fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values
H45Q
the mutation leads to a decrease in kcat of the enzyme by 2059fold
R70A
almost inactive
R70A
replacement by site-specific mutagenesis results in an enzyme that lacks both aldolase and decarboxylase activities. The mutant enzyme is also unable to catalyze pyruvate proton exchange
R70K
the mutation reduces catalytic efficiency by 270fold
Results 1 - 8 of 8