Information on EC 2.6.1.109 - 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase

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The expected taxonomic range for this enzyme is: Shewanella

EC NUMBER
COMMENTARY hide
2.6.1.109
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RECOMMENDED NAME
GeneOntology No.
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate + 2-oxoglutarate = 8-dehydro-3-deoxy-alpha-D-manno-octulosonate + L-glutamate
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
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate:2-oxoglutarate aminotransferase
The enzyme, characterized from the bacterium Shewanella oneidensis, forms 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 1.1.3.48, 3-deoxy-alpha-D-manno-octulosonate 8-oxidase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) is found exclusively in marine bacteria of the genus Shewanella
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
metabolism
physiological function
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. KdnA is a pyridoxal 5'-phosphate-dependent aminotransferase that utilizes L-glutamate and may play a role in outer membrane integrity
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-dehydro-3-deoxy-D-manno-octulosonic acid + L-glutamate
8-amino-3,8-dideoxy-D-manno-octulosonic acid + 2-oxoglutarate
show the reaction diagram
additional information
?
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the reaction catalyzed by KdnB, EC 1.1.3.48, is thermodynamically unfavorable and requires the second reaction catalyzed by KdnA to drive product formation, both enzymes are required for product formation. Production of H2O2 when Mn-KdnB and PLP-KdnA are incubated with Kdo and L-Glu
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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
8-dehydro-3-deoxy-D-manno-octulosonic acid + L-glutamate
8-amino-3,8-dideoxy-D-manno-octulosonic acid + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
additional information
NAD+ and NADP+ are not required for activity
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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)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of KdnA, trapped in the presence of the external aldimine with pyridoxal 5'-phosphate and glutamate, to 2.15 A resolution. KdnA adopts the classical aspartate aminotransferase fold. Residue Lys 186 forms an internal aldimine with the cofactor
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coi strain C41 by nickel affinity chromatography and dialysis, to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene kdnA, 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 37°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 lipopolysaccharide 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
enzyme knockout by in-frame deletion, chromosomal deletion of kdnA/kdnB, overview. The knock-out strain shows increased sensitivity to polymyxin B (3fold) and bile salts (2fold)