EC Number |
General Information |
Reference |
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2.4.99.13 | 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 |
2.4.99.13 | malfunction |
kdtA deletion mutants are viable when lpxL and lpxM (the lauroyl- or the myristoyltransferase of lipid A biosynthesis) are overexpressed. 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 |
2.4.99.13 | 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 |
2.4.99.13 | 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 |
2.4.99.13 | 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 |
2.4.99.13 | 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 |