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Results 1 - 10 of 32 > >>
EC Number
Amino acid exchange
Commentary
Reference
D385A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D402A
100fold decrease in ratio kcat/Km for CoA
D402P
crystallization data. Mutant adopts the proposed adenylate-forming conformation with very little change to the overall structure.The ability of the mutant to catalyze the adenylate-forming half-reaction is reduced by about 3fold, catalysis of the second half-reaction is reduced by 4 orders of magnitude
E306Q
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
E410A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F473A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat
G163I
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
G166I
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate
G408A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H207A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Results 1 - 10 of 32 > >>