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Information on EC 4.2.1.8 - mannonate dehydratase
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4.2.1.8 mannonate dehydrataseSpecify your search results
Word Map
- 4.2.1.8
-
mands
- dehydration
- enolase
- d-glucuronate
- mandelate
-
high-efficiency
- 2-keto-3-deoxy-d-gluconate
- racemase
- 2-keto-3-deoxygluconate
-
dissimilation
-
barrel
-
low-efficiency
- cap
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Altronate hydrolase
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-
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Altronic hydro-lyase
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-
-
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CCNA_00566
D-mannonate dehydratase
D-mannonate hydrolase
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-
-
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D-Mannonate hydrolyase
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-
-
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Dehydratase, mannonate
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-
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ManD
Mannonate hydrolyase
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-
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Mannonic hydrolase
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-
-
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UxuA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9024-31-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
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-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
-
glycylglycine buffer, in presence of FeSO4 and 2-mercaptoethanol as activator and protector
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
kcat decreased compared to wild-type, Km decreased compared to wild-type
H311A
the activity of H311A is only 2.4% that of the native wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
brenda
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
brenda
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
brenda
Ashwell, G.; Wahba, A.J.; Hickman, J.
A new pathway of uronic acid metabolism
Biochim. Biophys. Acta
30
186-187
1958
Escherichia coli
brenda
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
brenda
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
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)
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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