3.5.4.13: dCTP deaminase
This is an abbreviated version!
For detailed information about dCTP deaminase, go to the full flat file.
Word Map on EC 3.5.4.13
-
3.5.4.13
-
dttp
-
deamination
-
thymidylate
-
jannaschii
-
thymine
-
uracil
-
methanocaldococcus
-
bifunctionality
- 3.5.4.13
- dttp
-
deamination
- thymidylate
- jannaschii
- thymine
- uracil
-
methanocaldococcus
-
bifunctionality
Reaction
Synonyms
5-methyl-dCTP deaminase, DCD:DUT, dcdB, dCMP-dCTP deaminase, dCTP deaminase, dCTP deaminase:deoxyuridine triphosphatase, dCTP deaminase:dUTPase, deoxycytidine triphosphate deaminase
ECTree
Advanced search results
Engineering
Engineering on EC 3.5.4.13 - dCTP deaminase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
E138A
E138D
site-directed mutagenesis, the mutant enzyme shows a 140fold reduction in kcat and altered dTTP inhibition compared to the wild-type enzyme
E138Q
no enzymic activity, no change in overall structure compared to wild-type
H121A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered
R115A
no enzymic activity, no change in overall structure compared to wild-type
S111T
site-directed mutagenesis, the mutant enzyme shows a 30fold reduction in kcat and altered dTTP inhibition compared to the wild-type enzyme, modeling of the active site of the S111T enzyme, overview
no enzymic activity, no change in overall structure compared to wild-type
E138A
site-directed mutagenesis, inactive mutant, dTTP is bound to the active site of E138A, the region between Val120 and His125 is formed in a new conformation, the C-terminal fold is disordered