2.4.99.12: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

This is an abbreviated version!
For detailed information about lipid IVA 3-deoxy-D-manno-octulosonic acid transferase, go to the full flat file.

Word Map on EC 2.4.99.12

2.4.99.12

lipopolysaccharide

lps

chlamydia

cmp-kdo

trachomatis

hexaacylated

genus-specific

tetraacylated

glycosyltransferases

lipooligosaccharide

heptosyltransferase

meningitidis

Reaction

Synonyms

3-deoxy-D-manno-2-octulosonic acid transferase, 3-deoxy-D-manno-oct-2-ulosonic acid transferase, 3-deoxy-D-manno-oct-2-ulosonic acid transferases, 3-deoxy-D-manno-octulosonic acid transferase, 3-deoxy-manno-octulosonic acid transferase, beta-Kdo transferase, Kdo transferase, KdtA, KpsC, KpsS, LipA, LipB, mono-functional Kdo transferase, monofunctional KDO transferase, multi-functional Kdo-transferase, WaaA, WaaAAAE

ECTree

2 Transferases

2.4 Glycosyltransferases

2.4.99 Transferring other glycosyl groups

2.4.99.12 lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
1	Activating Compound
24593	AA Sequence
12	Cloned(Commentary)
1	Crystallization (Commentary)
2	Expression
10	General Information
3	Inhibitors
2	KM Value [mM]
2	Localization
1	Metals/Ions
4	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
29	Organism
12	Pathway
3	pH Optimum
1	pH Range
4	Protein Variants
5	Purification (Commentary)
2	Reaction
27	Reference
3	Source Tissue
1	Specific Activity [micromol/min/mg]
24	Substrates and Products (Substrate)
5	Subunits
52	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
3	Temperature Stability [°C]

Cloned

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Cloned on EC 2.4.99.12 - lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Cloned (commentary) Search

3 entries

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

Chlamydia psittaci

F0T4D1

700252

expressed in Corynebacterium glutamicum

Chlamydia pneumoniae

Q46222

700253

expressed in Escherichia coli CMR300 cells lacking Kdo-transferase

Haemophilus influenzae

P44806

721620

expressed in Escherichia coli Top10 cells

2 entries

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

Chlamydia psittaci

697697

heterologous expression of the Aquifex aeolicus waaA gene in a newly constructed Escherichia coli waaA suppressor strain results in synthesis of lipid IV(A) precursors substituted with one Kdo sugar

Aquifex aeolicus

698923

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

Chlamydia trachomatis

698690

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

P44806

698715