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Information on EC 2.4.99.12 - lipid IVA 3-deoxy-D-manno-octulosonic acid transferase and Organism(s) Aquifex aeolicus and UniProt Accession O66663

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IUBMB Comments
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 .
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Aquifex aeolicus
UNIPROT: O66663
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The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
kdo transferase, 3-deoxy-d-manno-oct-2-ulosonic acid transferase, monofunctional kdo transferase, multi-functional kdo-transferase, 3-deoxy-d-manno-octulosonic acid transferase, mono-functional kdo transferase, 3-deoxy-manno-octulosonic acid transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Kdo transferase
-
Kdo transferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tetraacyl-1,4-bisphosphate lipid A precursor 406 + CMP-alpha-Kdo
CMP + ?
show the reaction diagram
-
-
-
?
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->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
-
strictly monofunctional enzyme. The enzyme catalyzes the transfer of only a single KDO residue from CMP-3-deoxy-D-manno-octulosonate to differently modified lipid A acceptors. The KDO transferase is capable of utilizing a broad spectrum of acceptor substrates, whereas it is highly selective for the donor substrate. 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
-
-
r
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
x * 42000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
substrate-free form and in complex with CMP, hanging drop vapor diffusion method, using 100 mM Tris-HCl (pH 8.5), 35-40% (v/v) PEG 400, 200 mM Na-citrate, 50 mM 2-mercaptoethanol, at 19°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E276A
the mutation causes a decrease in the catalytic activity of the enzyme
G30A
the mutant is completely inactive
H272A/N273A
the mutations drastically affect the ability of the enzyme to transfer Kdo
R212A
the mutation clearly affects but does not completely prevent Kdo transfer activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
16 h, no effect
90
-
incubation for 1 h results in gradual loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Heparin-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mamat, U.; Schmidt, H.; Munoz, E.; Lindner, B.; Fukase, K.; Hanuszkiewicz, A.; Wu, J.; Meredith, T.C.; Woodard, R.W.; Hilgenfeld, R.; Mesters, J.R.; Holst O.
WaaA of the hyperthermophilic bacterium Aquifex aeolicus is a monofunctional 3-deoxy-D-manno-oct-2-ulosonic acid transferase involved in lipopolysaccharide biosynthesis
J. Biol. Chem.
284
22248-22262
2009
Aquifex aeolicus
Manually annotated by BRENDA team
Schmidt, H.; Hansen, G.; Singh, S.; Hanuszkiewicz, A.; Lindner, B.; Fukase, K.; Woodard, R.; Holst, O.; Hilgenfeld, R.; Mamat, U.; Mesters, J.
Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis
Proc. Natl. Acad. Sci. USA
109
6253-6258
2012
Aquifex aeolicus (O66663)
Manually annotated by BRENDA team