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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

Reaction

ATP
+
2-deoxy-2-([(3R)-3-hydroxyacyl]amino)-3-O-[(3R)-3-hydroxyacyl]-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-([(3R)-3-hydroxyacyl]amino)-1-O-phospho-alpha-D-glucopyranose
=
ADP
 +
2-deoxy-2-([(3R)-3-hydroxyacyl]amino)-3-O-[(3R)-3-hydroxyacyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxyacyl]-2-([(3R)-3-hydroxyacyl]amino)-1-O-phospho-alpha-D-glucopyranose

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

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.130 tetraacyldisaccharide 4'-kinase

Engineering

Engineering on EC 2.7.1.130 - tetraacyldisaccharide 4'-kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
G47A
about 43% of wild-type activity
G48A
about 1.8% of wild-type activity
G50A
about 0.1% of wild-type activity
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
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
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