EC Number   |
General Information |
Reference |
|---|
    2.4.99.12 | malfunction |
construction of a kdtA::kan insertion mutation, using a gene replacement method. Growth of this strain is absolutely dependent upon the presence of a functional copy of the kdtA gene (or the related gseA gene) carried on a plasmid |
698699 |
| 2.4.99.12 | malfunction |
kdtA deletion mutants are viable when lpxL and lpxM (the lauroyl- or the myristoyltransferase of lipid A biosynthesis) are overexpressed, encoded by deletion of kdtA in strains overexpressing LpxM causes accumulation of pentaacylated lipid A with a secondary myristate moiety. None of the strains lacking kdtA grow in the presence of bile salts at any temperature or on nutrient broth at 42°C |
696364 |
| 2.4.99.12 | malfunction |
the O35EkdtA knockout mutant produces only lipid A without any core oligosaccharide, and it is viable |
698237 |
| 2.4.99.12 | malfunction |
waaA (monofunctional Kdo transferase) of Haemophilus influenzae can not complement a knockout mutation in the corresponding gene of an Re-type Escherichia coli strain (encoding a bifunctional enzyme that transfers two 3-deoxy-D-manno-octulosonate residues to the lipid A precursor). However, complementation is possible by coexpressing the recombinant waaA together with the LPS-specific KDO kinase gene (kdkA) of Haemophilus influenzae DSM11121 or I69, respectively |
698715 |
| 2.4.99.12 | metabolism |
a model for the biosynthesis of the outer membrane in Escherichia coli is presented. Lipopolysaccharide is an endotoxin that elicits a strong immune response from humans, and its biosynthesis is in part regulated via degradation of LpxC and WaaA enzymes by the protease FtsH. Overexpression of waaA results in increased levels of 3-deoxy-D-manno-oct-2-ulosonic acid sugar in membrane extracts. Kdo and heptose levels are not elevated in lipopolysaccharides. This implies that uncontrolled production of WaaA does not increase the lipopolysaccharide production rate but rather reglycosylates lipid A precursors |
-, 760065 |
| 2.4.99.12 | metabolism |
the enzyme is involved in the synthesis of a mitochondrial not yet identified lipid A-like molecule rather than in the synthesis of the cell wall rhamnogalacturonan II |
722347 |
| 2.4.99.12 | physiological function |
chlamydial KDO transferases can replace in Escherichia coli K-12 the host's KDO transferase and retain the product specificities described in their natural background. WaaA from Chlamydia psittaci transfers predominantly four KDO residues to lipid A, forming a branched tetrasaccharide with the structure alpha-KDO-(2,8)-[alpha-KDO-(2,4)]-alpha-KDO-(2,4)-alpha-KDO |
-, 697697 |
| 2.4.99.12 | physiological function |
the main function of Kdo transferase is to provide the right substrates for the acyltransferases LpxL and LpxM, resulting in the synthesis of penta- and hexaacylated lipid A, which is optimal for the MsbA flippase |
696364 |
