Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Brabetz, W.; Müller-Loennies, S.; Brade, H.
    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 (2000), J. Biol. Chem., 275, 34954-34962.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.99.12 the gene is expressed in the Gram-positive host Corynebacterium glutamicum. Both Escherichia coli strains which express waaA and kdkA from Haemophilus influenzae synthesize an lipopolysaccharide containing a single Kdo residue that was exclusively phosphorylated at position 4 Haemophilus influenzae
2.7.1.166 both Escherichia coli strains which express waaA and kdkA from Haemophilus influenzae synthesize an lipopolysaccharide containing a single Kdo residue that is exclusively phosphorylated at position 4 Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.12 Escherichia coli
-
-
-
2.4.99.12 Haemophilus influenzae P44806
-
-
2.4.99.13 Escherichia coli
-
-
-
2.7.1.166 Haemophilus influenzae O86224
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.166 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]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 + ATP = 3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]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 + ADP (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. (4-O-phospho-KDO)-lipid IV(A) = 3-deoxy-4-O-phosphono-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 Haemophilus influenzae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.12 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 + CMP-3-deoxy-D-manno-octulosonate Escherichia coli WBB22 and WBB34 produce lipopolysaccharide composed of a single terminal KDO-residue, which is exclusively phosphorylated at position 4 and is linked to the 6'-position of the lipid A backbone (beta-GlcN-4P-(1-6)-alpha-GlcN-1P). 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 Haemophilus influenzae 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 + CMP
-
 r
2.7.1.166 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 + ATP both Escherichia coli strains which express waaA and kdkA from Haemophilus influenzae synthesize an lipopolysaccharide containing a single Kdo residue that is exclusively phosphorylated at position 4. (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. (4-O-phospho-KDO)-lipid IV(A) = 3-deoxy-4-O-phosphono-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 Haemophilus influenzae 3-deoxy-4-O-phosphono-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 + ADP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.99.12 3-deoxy-D-manno-oct-2-ulosonic acid transferase
-
 Escherichia coli
2.4.99.12 3-deoxy-D-manno-oct-2-ulosonic acid transferase
-
 Haemophilus influenzae
2.4.99.12 Kdo transferase
-
 Escherichia coli
2.4.99.12 monofunctional KDO transferase
-
 Haemophilus influenzae
2.4.99.13 3-deoxy-D-manno-oct-2-ulosonic acid transferase
-
 Escherichia coli
2.4.99.13 Kdo transferase
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
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 Escherichia coli
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 Escherichia coli