Information on EC 2.4.99.14 - (KDO)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase

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The expected taxonomic range for this enzyme is: Chlamydia

EC NUMBER
COMMENTARY hide
2.4.99.14
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RECOMMENDED NAME
GeneOntology No.
(KDO)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-beta-Kdo = alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Kdo transfer to lipid IVA III (Chlamydia)
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lipid A biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)2-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase [(2->8) glycosidic bond-forming]
The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-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-3-deoxy-D-manno-octulosonate
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->8)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-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
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-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-3-deoxy-D-manno-octulosonate
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->8)-3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->4)-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
show the reaction diagram
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45851
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x * 45851, calculated from sequence
46615
x * 46615, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a rough mutant (Re chemotype) of Escherichia coli (strain F515) that contains an lipopolysaccharide with only two alpha 2-4-linked Kdo residues. Recombinant strains are able to add the immunodominant Kdo residue in alpha 2-8-linkage to the parental lipopolysaccharide. Comparison of nucleotide and the deduced amino acid sequences of gseA of Chlamydia psittaci 6BC and Chlamydia trachomatis L
expressed in Corynebacterium glutamicum
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli. 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
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introduction of gseA into an Escherichia coli mutant with a thermolabile kdtA gene product endows cell extracts with the ability to transfer not only the third but also the first two Kdos to lipid A precursors, the Chlamydia trachomatis enzyme is at least trifunctional
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