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Information on EC 3.1.3.45 - 3-deoxy-manno-octulosonate-8-phosphatase for references in articles please use BRENDA:EC3.1.3.45
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
2-keto-3-deoxy-D-manno-octulosonate 8-phosphate phosphohydrolase, 3-deoxy-D-manno-octulosonate-8-phosphate phosphatase, 3-deoxy-D-manno-octulosonate-8-phosphate phosphohydrolase, 3-deoxy-manno-octulosonate-8-phosphatase, KDO8P phosphatase, KDO8PP, KdsC, KPP, phosphatase, phospho-3-deoxy-2-octulosonate,
yrbI ,
more
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2-keto-3-deoxy-D-manno-octulosonate 8-phosphate phosphohydrolase
3-deoxy-D-manno-octulosonate-8-phosphate phosphatase
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3-deoxy-D-manno-octulosonate-8-phosphate phosphohydrolase
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3-deoxy-manno-octulosonate-8-phosphatase
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phosphatase, phospho-3-deoxy-2-octulosonate
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2-keto-3-deoxy-D-manno-octulosonate 8-phosphate phosphohydrolase
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2-keto-3-deoxy-D-manno-octulosonate 8-phosphate phosphohydrolase
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KDO8P phosphatase
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KDO8PP
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KdsC
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yrbI
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3-deoxy-D-manno-octulosonate 8-phosphate + H2O = 3-deoxy-D-manno-octulosonate + phosphate
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hydrolysis of phosphoric ester
additional information
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KDO-phosphatase is not essential for viability of Escherichia coli
hydrolysis of phosphoric ester
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hydrolysis of phosphoric ester
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3-deoxy-D-manno-octulosonate-8-phosphate 8-phosphohydrolase
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2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
KDN 9-phosphate + H2O
3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + phosphate
additional information
?
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last enzyme of 3-deoxy-D-manno-octulosonate biosynthetic pathway
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?
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
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?
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
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best substrate
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?
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
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?
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
best substrate
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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high specificity
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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the enzyme is absolutely specific for the alpha-pyranose anomer
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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?
KDN 9-phosphate + H2O
3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + phosphate
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?
KDN 9-phosphate + H2O
3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate + phosphate
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?
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2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
additional information
?
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last enzyme of 3-deoxy-D-manno-octulosonate biosynthetic pathway
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?
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
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best substrate
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?
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate + H2O
? + phosphate
best substrate
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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the enzyme is absolutely specific for the alpha-pyranose anomer
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?
3-deoxy-D-manno-octulosonate 8-phosphate + H2O
3-deoxy-D-manno-octulosonate + phosphate
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?
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additional information
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divalent metal cofactor required
Ba2+
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1.0 mM, stimulates to a lesser extent than Co2+ or Mg2+
Ba2+
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1 mM, little stimulation
Co2+
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1.0 mM, optimal concentration for stimulation
Co2+
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1 mM, stimulation about 9fold
Mg2+
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required
Mg2+
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1.0 mM, optimal concentration for stimulation
Mg2+
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1 mM, stimulation about 9fold
Mn2+
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1.0 mM, stimulates to a lesser extent than Co2+ or Mg2+
Mn2+
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1 mM, little stimulation
Zn2+
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1.0 mM, stimulates to a lesser extent than Co2+ or Mg2+
Zn2+
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1 mM, little stimulation
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0.0001 - 0.16
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
0.058 - 0.8
3-deoxy-D-manno-octulosonate 8-phosphate
0.0009 - 1.6
KDN 9-phosphate
0.0001
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
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at pH 7.0 and 25°C
0.16
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
at pH 7.0 and 25°C
0.058
3-deoxy-D-manno-octulosonate 8-phosphate
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in presence of 1.0 mM Co2+, 37°C
0.075
3-deoxy-D-manno-octulosonate 8-phosphate
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pH 7.0, 37°C, presence of 1 mM Mg2+
0.091
3-deoxy-D-manno-octulosonate 8-phosphate
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in presence of 1.0 mM Mg2+, 37°C
0.8
3-deoxy-D-manno-octulosonate 8-phosphate
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37°C, pH 7.0
0.0009
KDN 9-phosphate
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at pH 7.0 and 25°C
1.6
KDN 9-phosphate
at pH 7.0 and 25°C
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0.78 - 1.5
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
0.021 - 0.061
KDN 9-phosphate
0.78
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
at pH 7.0 and 25°C
1.5
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
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at pH 7.0 and 25°C
0.021
KDN 9-phosphate
at pH 7.0 and 25°C
0.061
KDN 9-phosphate
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at pH 7.0 and 25°C
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4.8 - 15
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
0.013 - 0.069
KDN 9-phosphate
4.8
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
at pH 7.0 and 25°C
15
2-oxo-3-deoxy-D-manno-octulosonate 8-phosphate
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at pH 7.0 and 25°C
0.013
KDN 9-phosphate
at pH 7.0 and 25°C
0.069
KDN 9-phosphate
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at pH 7.0 and 25°C
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4.7 - 4.8
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isoelectric focusing
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UniProt
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UniProt
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UniProt
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Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
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19900
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4 * 23000, SDS-PAGE, 4 * 19900, mass spectrometry
23000
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4 * 23000, SDS-PAGE, 4 * 19900, mass spectrometry
90000
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dynamic light scattering
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dimer
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x-ray crystallography
dimer
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2 * 40000-43000, SDS-PAGE
dimer
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2 * 40000-43000, SDS-PAGE
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dimer
x-ray crystallography
tetramer
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4 * 20000, SDS-PAGE
tetramer
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4 * 23000, SDS-PAGE, 4 * 19900, mass spectrometry
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enzyme bound to Mg2+ and metavanadate, hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol MME 550, 40 mM MgCl2 and 100 mM HEPES (pH 7.5), at 18°C
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to 2.25 A resolution, space group P212121. Four protomers of YrbI in the asymmetric unit form a tetramer
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enzyme bound to Mg2+ and metavanadate, hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol MME 550, 40 mM MgCl2 and 100 mM HEPES (pH 7.5), at 18°C
structures of KdsC in complex with Mg2+, citrate and products and capturing of transition states of the enzyme. The binding of ligands does not cause any specific conformational changes in the active site. The conformation of substrate 3-deoxy-D-manno-octulosonic acid is different from ist conformation when it binds as a cleaved product. An intersubunit tunnel is observed
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loss of activity upon repeated freezing and thawing
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-90°C, stable for up to 2 months in 0.02 M Tris-acetate buffer
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4°C, stable for at least 2 weeks
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TALON metal affinity resin column chromatography
recombinant protein
TALON metal affinity resin column chromatography
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TALON metal affinity resin column chromatography
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
KDO-phosphatase knockout
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli
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Ray, P.H.; Benedict, C.D.
Purification and characterization of a specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B
J. Bacteriol.
142
60-68
1980
Escherichia coli, Escherichia coli B / ATCC 11303
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Baasov, T.; Jakob, A.
Anomeric specificity of 3-deoxy-D-manno-2-octulosonate 8-phosphate phosphatase from Escherichia coli
J. Am. Chem. Soc.
112
4972-4974
1990
Escherichia coli
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brenda
Wu, J.; Woodard, R.W.
Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
J. Biol. Chem.
278
18117-18123
2003
Escherichia coli
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Sperandeo, P.; Pozzi, C.; Deho, G.; Polissi, A.
Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus
Res. Microbiol.
157
547-558
2006
Escherichia coli
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Daughtry, K.D.; Huang, H.; Malashkevich, V.; Patskovsky, Y.; Liu, W.; Ramagopal, U.; Sauder, J.M.; Burley, S.K.; Almo, S.C.; Dunaway-Mariano, D.; Allen, K.N.
Structural basis for the divergence of substrate specificity and biological function within HAD phosphatases in lipopolysaccharide and sialic acid biosynthesis
Biochemistry
52
5372-5386
2013
Bacteroides thetaiotaomicron, Haemophilus influenzae, Haemophilus influenzae (P45314)
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Dhindwal, S.; Priyadarshini, P.; Patil, D.N.; Tapas, S.; Kumar, P.; Tomar, S.; Kumar, P.
Ligand-bound structures of 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Moraxella catarrhalis reveal a water channel connecting to the active site for the second step of catalysis
Acta Crystallogr. Sect. D
71
239-255
2015
Moraxella catarrhalis (A0A0J9X241), Moraxella catarrhalis BC8 (A0A0J9X241)
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Park, J.; Lee, D.; Kim, M.; Kim, D.; Shin, D.
A preliminary X-ray study of 3-deoxy-D-manno-oct-2-ulosonic acid 8-phosphate phosphatase (YrbI) from Burkholderia pseudomallei
Acta Crystallogr. Sect. F
71
790-793
2015
Burkholderia pseudomallei
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