Releases Kdo (alpha- and beta-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and de-O-acyl-re-LPS. 4-Methylumbelliferyl-alpha-Kdo (alpha-Kdo-OMec) is also a substrate.
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The expected taxonomic range for this enzyme is: Crassostrea virginica
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SYSTEMATIC NAME
IUBMB Comments
3-deoxyoctulosonyl-lipopolysaccharide hydrolase
Releases Kdo (alpha- and beta-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and de-O-acyl-re-LPS. 4-Methylumbelliferyl-alpha-Kdo (alpha-Kdo-OMec) is also a substrate.
the recombinant alpha-Kdo-ase effectively hydrolyzes the alpha-ketoside in the core-oligosaccharide of the structurally defined lipopolysaccharide (LPS), Re-LPS (Kdo2-lipid A) from Salmonella minnesota strain R595 and Escherichia coli strain D31m4, while Rd-LPS from Salmonella minnesota strain R7, that contains an extra outer core phosphorylated heptose, is only slowly hydrolyzed. The complex type LPS from Neisseria meningitides strains A1 and M992 that contain extra 5-6 sugar units at the outer core are refractory to recombinnat alpha-Kdo-ase
the recombinant alpha-Kdo-ase effectively hydrolyzes the alpha-ketoside in the core-oligosaccharide of the structurally defined lipopolysaccharide (LPS), Re-LPS (Kdo2-lipid A) from Salmonella minnesota strain R595 and Escherichia coli strain D31m4, while Rd-LPS from Salmonella minnesota strain R7, that contains an extra outer core phosphorylated heptose, is only slowly hydrolyzed. The complex type LPS from Neisseria meningitides strains A1 and M992 that contain extra 5-6 sugar units at the outer core are refractory to recombinnat alpha-Kdo-ase
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant extracellular enzyme from Pichia pastoris and Saccharomyces cerevisiae in large scale by ultracentrifugation of culture supernatant, followed by two steps ultrafiltration and gel filtration, recombinnat His-tagged enzyme from Pichia pastoris by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, functional recombinant expression in Saccharomyces cerevisiae and CHO-S cells, expression in Escherichia coli strains is not successful
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3.2.1.144 3-deoxyoctulosonase
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