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Results 1 - 10 of 27 > >>
EC Number
Amino acid exchange
Commentary
Reference
C145V/T146V
mutant shows lower kcat and higher Km value compared to wild-type
C145V/T146V/P147N/V217G
quadruble mutant is affected least by pteridine inhibitors, mutant shows lowest kcat and highest Km value compared to wild-type and other mutants
C145V/T146V/V217G
triple mutant shows lowest Ki value for biopterin, mutant shows lower kcat and higher Km value compared to wild-type
D143A
mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D143N
mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D143S
mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D143T
mutant enzymes in order of ascending Km-values: D143A, D143N, D143S, D143T. Mutant enzmyes in order of descending binding affinity: wild-type, D143A, d143N, D143S, D143T
D264A
mutant shows no catalytic activity
D264E
mutant enzyme is capable of forming an enzyme-RNA covalent intermediate, however , unlike wild-type enzyme, only hydroxylamine is capable of cleaving the enzyme-RNA covalent complex
D264H
mutant shows no catalytic activity
Results 1 - 10 of 27 > >>