1.14.14.5: alkanesulfonate monooxygenase
This is an abbreviated version!
For detailed information about alkanesulfonate monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.5
-
1.14.14.5
-
flavin
-
sulfur
-
desulfonation
-
two-component
-
octanesulfonate
-
sulfite
-
c4a-hydroperoxyflavin
-
organosulfonate
-
petroleum
-
oxygenolytic
-
tim-barrel
-
c4a-peroxyflavin
-
organosulfur
- 1.14.14.5
- flavin
- sulfur
-
desulfonation
-
two-component
- octanesulfonate
- sulfite
-
c4a-hydroperoxyflavin
-
organosulfonate
-
petroleum
-
oxygenolytic
-
tim-barrel
-
c4a-peroxyflavin
-
organosulfur
Reaction
Synonyms
alkanesulfonate alpha-hydroxylase, alkanesulfonate monooxygenase, AOLE_19265, FMNH2-dependent alkanesulfonate monooxygenase, msuD, oxygenase, alkanesulfonate 1-mono-, Pfl01_3916, SsuD, SsuE, sulfate starvation-induced protein 6, YcbN
ECTree
Advanced search results
Engineering
Engineering on EC 1.14.14.5 - alkanesulfonate monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
C54A
-
has little effect on FMN or FMNH2 binding, kcat/Km value decreases 6fold relative to wild-type
C54S
-
has little effect on FMN or FMNH2 binding, kcat/Km value increases 3fold relative to wild-type. Is able to generate the C4a-(hydro)peroxyflavin, but the rate of formation is increased 10fold relative to wild-type
D251A/D252A/E253A
mutation of conserved charged amino acids, 4fold decrease in kcat/Km value
DELTA251-261
deletion of alpha-helix containing conserved charged amino acids, complete loss of activity
R271A
mutation does not alter the catalytic activity, but in the presence of reduced flavin the variant is more susceptible to proteolytic digestion compared to wild-type