Information on EC 1.1.3.48 - 3-deoxy-alpha-D-manno-octulosonate 8-oxidase

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The expected taxonomic range for this enzyme is: Shewanella oneidensis

EC NUMBER
COMMENTARY hide
1.1.3.48
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RECOMMENDED NAME
GeneOntology No.
3-deoxy-alpha-D-manno-octulosonate 8-oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-deoxy-alpha-D-manno-octulopyranosonate + O2 = 3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + H2O2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CMP-8-amino-3,8-dideoxy-D-manno-octulosonate biosynthesis
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CMP-KDO biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
3-deoxy-alpha-D-manno-octulopyranosonate:oxygen 8-oxidoreductase
The enzyme, characterized from the bacterium Shewanella oneidensis, is involved in the formation of 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus. cf. EC 2.6.1.109, 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to a putative distinct class of metal-dependent alcohol oxidases
malfunction
creation of an Shewanella oneidensis kdnA/kdnB in-frame deletion strain shows increased sensitivity to the cationic antimicrobial peptide polymyxin as well as bile salts by 3fold and 2fold, respectively
metabolism
8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) biosynthesis pathway, 8-dehydro-3-deoxy-D-manno-octulosonic acid is directly converted to Kdo8N followed by incorporation into lipid A, overview. The entire gene cluster is required for 8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) biosynthesis
physiological function
a KdnB knock-out strain shows 3fold increased sensitivity to polymyxin B and 2fold increased sensitivity to bile salts; endotoxin lipopolysaccharide is composed of a hydrophobic anchor, known as lipid A, an inner core oligosaccharide, and a repeating O-antigen polysaccharide. The first sugar bridging the hydrophobic lipid A and the polysaccharide domain is 3-deoxy-D-manno-octulosonic acid. Derivative 8-amino-3,8-dideoxy-Dmanno-octulosonic acid is found exclusively in marine bacteria of the genus Shewanella. Data are consistent with direct conversion of 3-deoxy-D-manno-octulosonic acid to 8-amino-3,8-dideoxy-D-manno-octulosonic acid prior to its incorporation into the 8-amino-3,8-dideoxy-D-manno-octulosonic acid-lipid A domain of lipopolysaccharide by a metal-dependent oxidase followed by a glutamate-dependent aminotransferase; the first sugar bridging the hydrophobic lipid A and the polysaccharide domain is 3-deoxy-D-manno-octulosonic acid (Kdo), and thus it is critically important for lipopolysaccharide biosynthesis
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-octulopyranosonate + O2
3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + H2O2
show the reaction diagram
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enzyme oxidizes an alcohol using a metal and molecular oxygen
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?
3-deoxy-alpha-D-manno-octulopyranosonate + O2 + L-Glu
3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + H2O2
show the reaction diagram
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enzyme oxidizes an alcohol using a metal and molecular oxygen
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?
3-deoxy-alpha-D-manno-octulosonic acid + O2
3,8-dideoxy-8-oxo-alpha-D-manno-octulosonic acid + H2O2
show the reaction diagram
additional information
?
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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-octulopyranosonate + O2
3,8-dideoxy-8-oxo-alpha-D-manno-octulosonate + H2O2
show the reaction diagram
Q8EEB0
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enzyme oxidizes an alcohol using a metal and molecular oxygen
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?
3-deoxy-alpha-D-manno-octulosonic acid + O2
3,8-dideoxy-8-oxo-alpha-D-manno-octulosonic acid + H2O2
show the reaction diagram
Q8EEB0
i.e. Kdo
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
activates, KdnB contains 0.51 mol of iron/mol of enzyme; or Mn2+, required
Mn2+
activates, required for activity; or Fe2+, required
Zn2+
KdnB contains 0.24 mol of iron/mol of enzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
slight inhibition
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Shewanella oneidensis (strain MR-1)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coi strain C41 by nickel affinity chromatography, dialysis, and gel filtration, to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; gene kdnB, encoded in the Kdo8N biosynthetic cluster, DNA and amino acid sequence determination and analysis, subcloning and expression in Escherichia coli strains EC100D and WBB06 at 25°C, recombinant expression of the gene cluster for 8-amino-3,8-dideoxy-D-manno-octulosonic acid biosynthesis from Shewanella oneidensis in Escherichia coli results in lipid A containing 8-amino-3,8-dideoxy-D-manno-octulosonic acid, and in vitro assays confirm the enzymatic functionality converting 3-deoxy-D-manno-octulosonic acid to 8-amino-3,8-dideoxy-D-manno-octulosonic acid, with incorporation into the Kdo8N-lipid A domain of LPS by a metal-dependent oxidase followed by a glutamate-dependent aminotransferase, recombinant expression of His-tagged enzyme in Escherichia coi strain C41
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information