The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.13 [(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase]) . The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus and Haemophilus influenzae catalyse the transfer of a single 3-deoxy-D-manno-oct-2-ulosonate residue from CMP-3-deoxy-D-manno-oct-2-ulosonate to lipid IVA [2-4]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes .
kdo transferase, 3-deoxy-d-manno-oct-2-ulosonic acid transferase, monofunctional kdo transferase, 3-deoxy-d-manno-octulosonic acid transferase, mono-functional kdo transferase, 3-deoxy-manno-octulosonic acid transferase, multi-functional kdo-transferase, more
The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.13 [(Kdo)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase]) [1]. The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus and Haemophilus influenzae catalyse the transfer of a single 3-deoxy-D-manno-oct-2-ulosonate residue from CMP-3-deoxy-D-manno-oct-2-ulosonate to lipid IVA [2-4]. The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes [5].
the enzyme is responsible for attachment of the two 3-deoxy-D-manno-octulosonic acid residues that constitute the link between lipid A and the core oligosaccharide of the lipopolysaccharide. Lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
KDO attachment during lipid A biosynthesis is essential for cell growth and accounts for the conditional lethality associated with mutations in KDO biosynthesis. lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the bifunctional enzyme transfers two 3-deoxy-D-manno-octulosonate residues to lipid A precursors. Key enzyme in lipopolysaccharide biosynthesis. Lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme is responsible for attachment of the two 3-deoxy-D-manno-octulosonic acid residues that constitute the link between lipid A and the core oligosaccharide of the lipopolysaccharide. Lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
KDO attachment during lipid A biosynthesis is essential for cell growth and accounts for the conditional lethality associated with mutations in KDO biosynthesis. lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the bifunctional enzyme transfers two 3-deoxy-D-manno-octulosonate residues to lipid A precursors. Key enzyme in lipopolysaccharide biosynthesis. Lipid IV(A) = 2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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
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
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
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
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
The gene coding for 3-deoxy-manno-octulosonic acid transferase and the rfaQ gene are transcribed from divergently arranged promoters in Escherichia coli
3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and kdo kinase (KdkA) of Haemophilus influenzae are both required to complement a waaA knockout mutation of Escherichia coli