Literature summary for 3.2.1.144 extracted from

  • Nakagawa, T.; Shimada, Y.; Pavlova, N.V.; Li, S.C.; Li, Y.T.
    Cloning and expression of 3-deoxy-D-manno-oct-2-ulosonic acid alpha-ketoside hydrolase from oyster hepatopancreas (2015), Glycobiology, 25, 1431-1440 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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 Crassostrea virginica

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
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Crassostrea virginica
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-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Crassostrea virginica 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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?

Organism

Organism UniProt Comment Textmining
Crassostrea virginica A0A0M3N009
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-

Purification (Commentary)

Purification (Comment) Organism
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 Crassostrea virginica

Source Tissue

Source Tissue Comment Organism Textmining
hepatopancreas
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Crassostrea virginica
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Crassostrea virginica ?
-
?
4-methylumbelliferyl 3-deoxy-alpha-D-manno-oct-2-ulosonic acid + H2O
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Crassostrea virginica 4-methylumbelliferone + 3-deoxy-D-manno-oct-2-ulosonic acid
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?

Subunits

Subunits Comment Organism
? x * 44604, sequence calculation Crassostrea virginica

Synonyms

Synonyms Comment Organism
alpha-Kdo-ase
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Crassostrea virginica
3-deoxy-D-manno-oct-2-ulosonic acid alpha-ketoside hydrolase
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Crassostrea virginica
3-deoxy-octulo-sonase
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Crassostrea virginica

General Information

General Information Comment Organism
evolution the deduced amino acid sequence of the enzyme contains two Asp boxes (S277PDDGKTW and S328TDQGKTW) commonly found in sialidases Crassostrea virginica