1.13.12.22: deoxynogalonate monooxygenase
This is an abbreviated version!
For detailed information about deoxynogalonate monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.22
-
1.13.12.22
-
nogalater
-
cofactor-independent
-
polyketide
-
prosthetic
-
deprotonated
-
asparagines
-
o2-dependent
-
pka
-
oxygenases
-
cofactor-free
- 1.13.12.22
- nogalater
-
cofactor-independent
- polyketide
-
prosthetic
-
deprotonated
- asparagines
-
o2-dependent
- pka
- oxygenases
-
cofactor-free
Reaction
Synonyms
SnoaB
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.12.22 - deoxynogalonate monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
H49A
kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 13% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
N18A
N63A
R90E
kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 17% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
W67F
kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 0.5% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 1.5% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
N18A
the mutation suppresses the kcat value 120fold compared to the wild type enzyme
kcat/Km for [4,5-dihydroxy-10-oxo-3-(3-oxobutanoyl)-9,10-dihydroanthracen-2-yl]acetate is 1.5% compared to the activity of recombinant wild-type enzyme with N-terminal polyhistidine tag
N63A
the mutation suppresses the kcat value 50fold compared to the wild type enzyme