Information on EC 4.2.1.8 - Mannonate dehydratase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.2.1.8
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RECOMMENDED NAME
GeneOntology No.
Mannonate dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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-
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-fructuronate degradation
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degradation of sugar acids
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Pentose and glucuronate interconversions
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Metabolic pathways
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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 hide
9024-31-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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B8GZZ7
UniProt
Manually annotated by BRENDA team
serotype 2
UniProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
B8GZZ7;
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Mannonate
2-Dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
D-mannonate
?
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-mannonate
?
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
each ManD monomer roughly has one Mn2+ ion-binding site
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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alpha-picolinate
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D-glucuronate
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competitive
D-Glucuronic amide
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noncompetitive
D-mannitol
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competitive
D-Mannonic amide
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noncompetitive
D-sorbitol
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competitive
iodoacetate
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nitrilotriacetic acid
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-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfhydryl compounds
-
required for maintenance of activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 20
D-mannonate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 5.88
D-mannonate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 1.96
D-mannonate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
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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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Caulobacter vibrioides (strain ATCC 19089 / CB15);
Q82ZC9
Enterococcus faecalis (strain ATCC 700802 / V583);
Escherichia coli (strain K12);
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199);
Streptococcus suis (strain 05ZYH33);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
2 * 41000, SDS-PAGE
80000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 41000, SDS-PAGE
monomer
crystal structure
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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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
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maximal stability
5900
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM Tris buffer, pH 7.0, 10% loss of activity after 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Superdex 200 gel filtration
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced more than 1000fold when Caulobacter crescentus NA1000 is grown on D-glucuronate as a carbon source
B8GZZ7;
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E185D
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
E186D
kcat decreased compared to wild-type, Km decreased compared to wild-type
E186G
kcat and Km increased compared to wild-type
E63A/S64A
inactive mutant
H32G
kcat and Km increased compared to wild-type
N103A/D109A
kcat decreased compared to wild-type, Km slightly decreased compared to wild-type
N36G
kcat increased compared to wild-type, Km slightly decreased compared to wild-type
W110F
inactive mutant
H311A
the activity of H311A is only 2.4% that of the native wild type enzyme
Y325F
catalytically inactive
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.1.8)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)