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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
Altronate hydrolase, Altronic hydro-lyase,
CCNA_00566 , D-mannonate dehydratase, D-mannonate hydrolase, D-Mannonate hydrolyase, Dehydratase, mannonate, EcManD, ManD, mannonate dehydratase,
more
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Altronate hydrolase
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Altronic hydro-lyase
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D-mannonate hydrolase
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D-Mannonate hydrolyase
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Dehydratase, mannonate
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Mannonate hydrolyase
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Mannonic hydrolase
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CCNA_00566
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D-mannonate dehydratase
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D-mannonate dehydratase
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ManD
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UxuA
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D-Mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
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D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
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D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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?
D-mannonate
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enzyme is involved in mannuronate catabolism
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D-mannonate
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enzyme is involved in mannuronate catabolism
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D-mannonate
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enzyme is involved in uronic acid metabolism
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D-mannonate
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inducible by glucuronate and fructuronate
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?
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D-mannonate
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enzyme is involved in mannuronate catabolism
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?
D-mannonate
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enzyme is involved in mannuronate catabolism
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D-mannonate
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inducible by glucuronate and fructuronate
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D-mannonate
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enzyme is involved in uronic acid metabolism
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?
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Mn2+
each ManD monomer roughly has one Mn2+ ion-binding site
Fe2+
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maximal activation at 0.8 mM FeSo4
Fe2+
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required, upon inactivation the enzyme incorporates a single Fe atom, it contains no Fe-S core, the incorporated iron is losely bound
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D-glucuronate
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competitive
D-Glucuronic amide
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noncompetitive
D-Mannonic amide
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noncompetitive
nitrilotriacetic acid
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sulfhydryl compounds
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required for maintenance of activity
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Dehydration
Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium.
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4.55
D-mannonate
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mutant E185G, pH 7.5, 37°C
5.3
D-mannonate
mutant E186G, pH 7.5, 37°C
5.21
D-mannonate
mutant H32G, pH 7.5, 37°C
4.79
D-mannonate
wild-type, pH 7.5, 37°C
4.67
D-mannonate
mutant N36G, pH 7.5, 37°C
1.9
D-mannonate
mutant enzyme H311A, at pH 7.5 and 37°C
4.55
D-mannonate
mutant E185G, pH 7.5, 37°C
4.08
D-mannonate
mutant N103A/D109A, pH 7.5, 37°C
3.6
D-mannonate
mutant E186D, pH 7.5, 37°C
3
D-mannonate
wild type enzyme, at pH 7.5
2.31
D-mannonate
mutant E185D, pH 7.5, 37°C
1.9
D-mannonate
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mutant enzyme H311A, at pH 7.5 and 37°C
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0.94
D-mannonate
mutant E185G, pH 7.5, 37°C
5.88
D-mannonate
wild type enzyme, at pH 7.5 and 37°C
1.6
D-mannonate
pH 7.9, 25°C
1.4
D-mannonate
mutant N36G, pH 7.5, 37°C
1.29
D-mannonate
mutant H32G, pH 7.5, 37°C
1.1
D-mannonate
mutant E186G, pH 7.5, 37°C
0.94
D-mannonate
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mutant E185G, pH 7.5, 37°C
0.09
D-mannonate
mutant enzyme H311A, at pH 7.5 and 37°C
0.81
D-mannonate
wild-type, pH 7.5, 37°C
0.29
D-mannonate
mutant E186D, pH 7.5, 37°C
0.23
D-mannonate
mutant E185D, pH 7.5, 37°C
0.1
D-mannonate
mutant N103A/D109A, pH 7.5, 37°C
0.09
D-mannonate
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mutant enzyme H311A, at pH 7.5 and 37°C
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0.047
D-mannonate
mutant enzyme H311A, at pH 7.5 and 37°C
1.5
D-mannonate
pH 7.9, 25°C
1.96
D-mannonate
wild type enzyme, at pH 7.5 and 37°C
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additional information
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additional information
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8.3
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glycylglycine buffer, in presence of FeSO4 and 2-mercaptoethanol as activator and protector
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brenda
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UniProt
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UniProt
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UniProt
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UniProt
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serotype 2
UniProt
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UniProt
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ATCC 9637
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malfunction
gene knockout shows no growth on D-glucoronate. Complementation of the knockout with an isopropyl beta-D-1-thiogalactopyranoside-inducible gene encoding ManD restored growth on D-glucuronate
physiological function
a gene knockout muant shows no growth on D-glucuronate
physiological function
knockout of the UxuA gene results in slower growth with both L-gulonate and D-mannonate as carbon sources
physiological function
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knockout of the UxuA gene results in slower growth with both L-gulonate and D-mannonate as carbon sources
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physiological function
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a gene knockout muant shows no growth on D-glucuronate
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41000
2 * 41000, SDS-PAGE
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homodimer
2 * 41000, SDS-PAGE
monomer
crystal structure
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crystal structures of ManD and its complex with D-mannonate is solved. It shows that the insert sequence forms two alpha helices locating above the active site. The two insert alpha helices introduce a loop that forms a cap covering the substrate binding pocket, which restricts the tunnels of substrate entering and product releasing from the active site
hanging drop method at room temperature. Structures of the wild type ManD from are determined at pH 7.5 in the presence of Mg2+ and also in the presence of Mg2+ and the 2-keto-3-keto-D-gluconate dehydration product. The structure of the catalytically active K271E mutant is determined at pH 5.5 in the presence of the D-mannonate substrate
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ManD in native form and in complex with its substrate D-mannonate and Mn2+ ion, hanging drop vapor diffusion method, using 0.2 M potassium-sodium tartrate, 0.1 M sodium citrate (pH 6.5), and 1 M ammonium sulfate (native form) or using 0.2 M potassium sodium tartrate tetrahydrate, 0.1 M trisodium citrate dehydrate (pH 6.5), 1 M ammonium sulfate, and 15 mM D-mannonate
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E185D
kcat decreased compared to wild-type, Km decreased compared to wild-type
N36G
kcat increased compared to wild-type, Km slightly decreased compared to wild-type
N103A/D109A
kcat decreased compared to wild-type, Km slightly decreased compared to wild-type
H32G
kcat and Km increased compared to wild-type
E63A/S64A
inactive mutant
E186G
kcat and Km increased compared to wild-type
E186D
kcat decreased compared to wild-type, Km decreased compared to wild-type
E185G
kcat increased compared to wild-type, Km slightly decreased compared to wild-type
E185D
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kcat decreased compared to wild-type, Km decreased compared to wild-type
Y325F
catalytically inactive
H311A
the activity of H311A is only 2.4% that of the native wild type enzyme
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7 - 8.5
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maximal stability
5900
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4
ManD exhibits no enzymatic activity at 4°C
52
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2 min, about 50% loss of activity
59
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1 min, 90% loss of activity
additional information
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D-gluconate protects against heat denaturation
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4°C, 10 mM Tris buffer, pH 7.0, 10% loss of activity after 1 month
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Ni-NTA column chromatography, Superdex 200 gel filtration
using Ni-NTA chromatography
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expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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compared to growth on D-xylose, expression is induced more than 1000fold by growth on D-glucuronate as a carbon source
expression is induced more than 1000fold when Caulobacter crescentus NA1000 is grown on D-glucuronate as a carbon source
compared to growth on D-xylose, expression is induced more than 1000fold by growth on D-glucuronate as a carbon source
compared to growth on D-xylose, expression is induced more than 1000fold by growth on D-glucuronate as a carbon source
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Robert-Baudouy, J.M.; Stoeber, F.R.
Purification et proprietes de la D-mannonate hydrolase d'Escherichia coli'
Biochim. Biophys. Acta
309
473-485
1973
Escherichia coli
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Robert-Baudouy, J.; Jimeno-Abendano, J.; Stoeber, F.
D-Mannonate and D-altronate dehydratases of Escherichia coli K12
Methods Enzymol.
90
288-294
1982
Escherichia coli
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Dreyer, J.L.
The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases
Eur. J. Biochem.
166
623-630
1987
Escherichia coli
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Farmer, J.J.; Eagon, R.G.
Aldohexuronic acid catabolism by a soil Aeromonas
J. Bacteriol.
97
97-106
1969
Aeromonas sp., Aeromonas sp. C11-2B
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Ashwell, G.; Wahba, A.J.; Hickman, J.
A new pathway of uronic acid metabolism
Biochim. Biophys. Acta
30
186-187
1958
Escherichia coli
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Rakus, J.F.; Fedorov, A.A.; Fedorov, E.V.; Glasner, M.E.; Vick, J.E.; Babbitt, P.C.; Almo, S.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans
Biochemistry
46
12896-12908
2007
Novosphingobium aromaticivorans
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Zhang, Q.; Gao, F.; Peng, H.; Cheng, H.; Liu, Y.; Tang, J.; Thompson, J.; Wei, G.; Zhang, J.; Du, Y.; Yan, J.; Gao, G.F.
Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism
J. Bacteriol.
191
5832-5837
2009
Streptococcus suis (A4VVI4), Streptococcus suis
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Wichelecki, D.J.; Graff, D.C.; Al-Obaidi, N.; Almo, S.C.; Gerlt, J.A.
Identification of the In vivo Function of the High Efficiency D-Mannonate Dehydratase in Caulobacter crescentus NA1000 from the Enolase Superfamily
Biochemistry
53
4087-4089
2014
Caulobacter vibrioides (A0A0H3C643)
brenda
Qiu, X.; Tao, Y.; Zhu, Y.; Yuan, Y.; Zhang, Y.; Liu, H.; Gao, Y.; Teng, M.; Niu, L.
Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium
J. Struct. Biol.
180
327-334
2012
Escherichia coli (P24215), Escherichia coli
brenda
Wichelecki, D.J.; Graff, D.C.; Al-Obaidi, N.; Almo, S.C.; Gerlt, J.A.
Identification of the in vivo function of the high-efficiency D-mannonate dehydratase in Caulobacter crescentus NA1000 from the enolase superfamily
Biochemistry
53
4087-4089
2014
Caulobacter vibrioides (A0A0H3C643), Caulobacter vibrioides NA1000 (A0A0H3C643), Caulobacter vibrioides NA1000
brenda
Wichelecki, D.J.; Vendiola, J.A.; Jones, A.M.; Al-Obaidi, N.; Almo, S.C.; Gerlt, J.A.
Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily pathways for the catabolism of L-gulonate and L-idonate
Biochemistry
53
5692-5699
2014
Chromohalobacter salexigens (Q1QT83), Chromohalobacter salexigens DSM 3043 (Q1QT83), Chromohalobacter salexigens DSM 3043
brenda
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