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IUBMB Comments The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli.
The enzyme appears in viruses and cellular organisms
Synonyms kdo hydrolase, kdhab, hp0580, more
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3-deoxy-D-manno-octulosonic acid hydrolase
hydrolase, 2-keto-3-deoxyoctonate
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octulofuranosylono hydrolase
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octulopyranosylonohydrolase
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octulosylono hydrolase
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3-deoxy-D-manno-octulosonic acid hydrolase
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3-deoxy-D-manno-octulosonic acid hydrolase
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3-deoxy-D-manno-octulosonic acid hydrolase
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KdhAB
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Kdo hydrolase
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(Rib-beta-(1-2)-Rib-beta-(1-7)-3-deoxymanno-2-octulosonyl-alpha-(2-2))n + H2O = beta-D-ribofuranosyl-(1-2)-beta-D-ribofuranosyl-(1-7)-3-deoxy-alpha-D-manno-oct-2-ulopyranonosyl-(2-2)-beta-D-ribofuranosyl-(1-2)-beta-D-ribofuranosyl-(1-7)-3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid + (Rib-beta-(1-2)-Rib-beta-(1-7)-3-deoxymanno-2-octulosonyl-alpha-(2-2))n-2
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hydrolysis of O-glycosyl bond
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capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase
The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli.
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1-dephosphorylated Kdo2-lipid A + H2O
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Substrates: - Products: -
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Kdo2-lipid A + H2O
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Substrates: - Products: -
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Coliphage PHI20
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Substrates: cleaves only substrates that contain beta-ketosidic KDO substituted at 0-7 by a beta-ribofuranosyl residue Products: i.e. main product, beta-Ribf1 to 7beta-KDOp2 to 3beta-Ribf1 to 7KDO
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Coliphage PHI20
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Substrates: catalyzes depolymerization of 3-deoxy-2-octulosonide containing capsular polysaccharides from E. coli K13, K20 and K23 Products: -
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Coliphage PHI95
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Substrates: specific for K95-antigen Products: -
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Coliphage PHI95
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Substrates: i.e. KDO, native or deacetylated polysaccharides are substrates Products: -
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Coliphage PHI95
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Substrates: cleaves beta-octylfuranosidonic linkages of K95-glycan Products: -
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3-deoxy-D-manno-2-octulosonic acid glycoside + H2O
tetrasaccharide of two repeating units
Coliphage PHI20
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Substrates: catalyzes depolymerization of 3-deoxy-2-octulosonide containing capsular polysaccharides from E. coli K13, K20 and K23 Products: -
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6.5
Coliphage PHI95
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assay at
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Coliphage PHI95
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assay at
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Coliphage PHI20
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assay at
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Coliphage PHI20
growing on Escherichia coli K13, K20 or K23
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Coliphage PHI95
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brenda
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brenda
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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malfunction
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inactivation of Kdo hydrolase activity produces two phenotypes associated with cationic antimicrobial peptide resistance and O-antigen expression. Kdo hydrolase mutants are highly sensitive to polymyxin B. Production of a fully extended O-antigen is also diminished in a Kdo hydrolase mutant, with a consequent increase in core-lipid A
malfunction
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immunization of mice with the kdhAB-deficient mutant provides significant protection against fully virulent Francisella tularensis type A strain Schu S4
malfunction
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immunization of mice with the kdhAB-deficient mutant provides significant protection against fully virulent Francisella tularensis type A strain Schu S4
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physiological function
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Kdo hydrolase plays a role in the maintenance of the bacterial surface. Kdo hydrolase activity modulates O-antigen expression
physiological function
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the enzyme is involved in the virulence of Francisella tularensis strain LVS
physiological function
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the enzyme is involved in the virulence of Francisella tularensis strain LVS
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expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli HMS174 cells
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Altmann, F.; Kwiatkowski, B.; Stirm, S.; Mrz, L.; Unger, F.M.
A bacteriophage-associated glycanase cleaving beta-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO)
Biochem. Biophys. Res. Commun.
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329-335
1986
Coliphage PHI20
brenda
Altmann, F.; Mrz, L.; Stirm, S.; Unger, F.M.
Two additional bacteriophage-associated glycan hydrolases cleaving ketosidic bonds of 3-deoxy-D-manno-octulosonic acid in capsular polysaccharides of Escherichia coli
FEBS Lett.
221
145-149
1987
Coliphage PHI95
brenda
Stead, C.; Zhao, J.; Raetz, C.; Trent, M.
Removal of the outer Kdo from Helicobacter pylori lipopolysaccharide and its impact on the bacterial surface
Mol. Microbiol.
78
837-852
2010
Helicobacter pylori
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Okan, N.A.; Chalabaev, S.; Kim, T.H.; Fink, A.; Ross, R.A.; Kasper, D.L.
Kdo hydrolase is required for Francisella tularensis virulence and evasion of TLR2-mediated innate immunity
mBio
4
00638-00612
2013
Francisella tularensis, Francisella tularensis LVS
brenda
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