1.4.1.19: tryptophan dehydrogenase
This is an abbreviated version!
For detailed information about tryptophan dehydrogenase, go to the full flat file.
Reaction
Synonyms
dehydrogenase, tryptophan, L-Trp dehydrogenase, L-Trp-dehydrogenase, L-tryptophan dehydrogenase, NAD(P)-L-tryptophan dehydrogenase, NAD+-dependent L-tryptophan dehydrogenase, TDH, TrpDH
ECTree
1.4.1.19 tryptophan dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.4.1.19 - tryptophan dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A234D
the mutant shows higher specific activity and stability compared to the wild type enzyme
A69L
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
A69M
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D168G
the mutant shows higher specific activity and stability compared to the wild type enzyme
I296A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I296N
the mutant shows wild type specific activity and higher stability compared to the wild type enzyme
L288M
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
L59F
the mutant shows higher specific activity and stability compared to the wild type enzyme
L59F/D168G/A234D/I296N
M295A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M40L
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M65A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
V132A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V133A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
V291A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292F
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y292H
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y292W
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
A234D
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
D168G
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
I296N
-
the mutant shows wild type specific activity and higher stability compared to the wild type enzyme
-
L59F
-
the mutant shows higher specific activity and stability compared to the wild type enzyme
-
L59F/D168G/A234D/I296N
-
mutant with thermal stability whose specific activity and stability are higher than those of the wild type enzyme
-
A69L
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
A69M
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
-
V132A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
V291A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
Y292F
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
-
L59F/D168G/A234D/I296N
mutant with thermal stability whose specific activity and stability are higher than those of the wild type enzyme
L59F/D168G/A234D/I296N
the mutant exhibits higher stability and specific activity than the wild type enzyme
