EC Number   |
General Information |
Reference |
|---|
    2.7.1.130 | evolution |
kinase LpxK is a member of the P-loop containing nucleoside triphosphate hydrolase superfamily. The active site Walker A (P-loop) and Walker B (Mg2+-binding) motifs are common to all P-loop kinase family members |
737675 |
| 2.7.1.130 | metabolism |
a model for the biosynthesis of the outer membrane in Escherichia coli is presented. The catalytic activity is dependent on the concentration of unsaturated fatty acids. LpxC is additionally regulated by an unidentified protease whose activity is independent of lipid A disaccharide concentration (the feedback source for FtsH-mediated LpxC regulation) but can be induced in vitro by palmitic acid |
-, 760065 |
| 2.7.1.130 | metabolism |
tetraacyldisaccharide 4'-kinase (LpxK) of Pseudomonas aeruginosa is an important tparticipant in the biosynthesis of lipopolysaccharide |
-, 762384 |
| 2.7.1.130 | metabolism |
the sixth step in the lipid A biosynthetic pathway involves phosphorylation of the tetraacyldisaccharide-1-phosphate (DSMP) intermediate by the cytosol-facing inner membrane kinase LpxK |
737675 |
| 2.7.1.130 | more |
apparent steady-state kinetic parameters for LpxK activity support the formation of a ternary LpxK-ATP/Mg2+-DSMP complex. In its closed catalytically competent form, the C-terminal domain of LpxK undergoes a hinge motion to close around the nucleotide substrate upon binding. Active sites of ATP-bound enzyme LpxK are in the open form, modeling, overview |
737675 |
| 2.7.1.130 | more |
structural and kinetic studies reveal the molecular basis of lipid binding, overview. The LpxK active site recognizes the lipid's glucosamine/phosphate headgroups and only accommodates disaccharides. Steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and characterization of N-terminal helix truncation mutants uncovers the role of this substructure as a hydrophobic membrane anchor |
738621 |
| 2.7.1.130 | more |
the enzyme's active site is modeled with residues Tyr28, Val31, Arg35, Asn58, Val61, Gly62, Thr64, Lys66, Ser88, Arg89, Gly90, Tyr91, Glu114, Pro115, Arg72, Arg132, Asp151, Asp152, Gln155, His156, Leu180, Arg186 and Glu187 |
-, 762384 |
| 2.7.1.130 | physiological function |
enzyme LpxK is an essential membrane-bound kinase in the lipid A biosynthetic pathway. In Gram-negative bacteria, lipidA is the hydrophobic anchor of lipopolysaccharide, which makes up the outer leaflet of the asymmetric outer membrane of these organisms. This acylated disaccharide of glucosamine plays an important role in eliciting an immunogenic response to bacterial pathogens and is essential to the survival of the vast majority of these microbes |
738621 |
| 2.7.1.130 | physiological function |
in the reaction catalyzed by LpxK in Kdo2-lipid A biosynthesis, enzyme LpxK is responsible for the phosphorylation of the 4'-hydroxyl of tetraacyldisaccharide-1-phosphate (DSMP) |
737675 |
