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Results 1 - 10 of 65 > >>
EC Number
Amino acid exchange
Commentary
Reference
A128E
naturally occuring mutation after treatment with pyrazinoic acid
A128S
naturally occuring mutation after treatment with pyrazinoic acid
C17R
naturally occuring mutation after treatment with pyrazinoic acid
D116Y
naturally occuring mutation after treatment with pyrazinoic acid
D41G
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
E130G
naturally occuring mutation after treatment with pyrazinoic acid
E56S
site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel
F107L
naturally occuring mutation after treatment with pyrazinoic acid
G24S
study of the structure and processing activity
H11A
study of the structure and processing activity
Results 1 - 10 of 65 > >>