2.7.1.130: tetraacyldisaccharide 4'-kinase
This is an abbreviated version!
For detailed information about tetraacyldisaccharide 4'-kinase, go to the full flat file.
Word Map on EC 2.7.1.130
-
2.7.1.130
-
4'-position
-
4'-phosphate
-
substructure
-
sixth
-
endotoxin
-
raetz
-
triphosphate
-
hexaacylated
-
lipopolysaccharide
-
drug development
-
kdo
-
phospholipids
-
nucleoside
- 2.7.1.130
-
4'-position
- 4'-phosphate
-
substructure
- sixth
- endotoxin
-
raetz
- triphosphate
-
hexaacylated
- lipopolysaccharide
- drug development
- kdo
- phospholipids
- nucleoside
Reaction
Synonyms
ATP:2,2',3,3'-tetrakis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-alpha-D-glucosaminyl-phosphate 4'-O-phosphotransferase, kinase, lipid A 4'-(phosphorylating), lipid A 4'-kinase, LpxK, membrane-bound tetraacyldisaccharide-1-phosphate 4'-kinase, tetraacyldisaccharide-1-phosphate 4-kinase
ECTree
Advanced search results
Engineering
Engineering on EC 2.7.1.130 - tetraacyldisaccharide 4'-kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
D138A
D138N
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D139A
D139N
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D260A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D99A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D99E
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D99N
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E100A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E100D
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E100Q
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
E172A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
H143A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
H261A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
K51A
N43A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
Q142A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
R119A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
R171A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
R72A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
S49A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
S53A
T52A
Y74A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
additional information
steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and construction of two N-terminal helix truncated forms of LpxK, one in which amino acids 2-12 are removed, DELTA12LpxK, and another in which amino acids 2-29 are removed, DELTA29LpxK
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D138A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D139A
point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity
K51A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
T52A
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme