Information on EC 4.2.1.8 - Mannonate dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.8
-
RECOMMENDED NAME
GeneOntology No.
Mannonate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-fructuronate degradation
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
degradation of sugar acids
-
-
SYSTEMATIC NAME
IUBMB Comments
D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-31-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain C11-2B
-
-
Manually annotated by BRENDA team
strain C11-2B
-
-
Manually annotated by BRENDA team
-
B8GZZ7
UniProt
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
serotype 2
UniProt
Manually annotated by BRENDA team
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
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
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
each ManD monomer roughly has one Mn2+ ion-binding site
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
alpha-picolinate
-
-
D-glucuronate
-
competitive
D-Glucuronic amide
-
noncompetitive
D-mannitol
-
competitive
D-Mannonic amide
-
noncompetitive
D-sorbitol
-
competitive
iodoacetate
-
-
nitrilotriacetic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfhydryl compounds
-
required for maintenance of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9 - 20
D-mannonate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 5.88
D-mannonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 1.96
D-mannonate
3998
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
-
-
8.3
-
glycylglycine buffer, in presence of FeSO4 and 2-mercaptoethanol as activator and protector
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Caulobacter crescentus (strain ATCC 19089 / CB15)
Caulobacter crescentus (strain ATCC 19089 / CB15)
Enterococcus faecalis (strain ATCC 700802 / V583)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Streptococcus suis (strain 05ZYH33)
Streptococcus suis (strain 05ZYH33)
Streptococcus suis (strain 05ZYH33)
Streptococcus suis (strain 05ZYH33)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
2 * 41000, SDS-PAGE
80000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 41000, SDS-PAGE
monomer
crystal structure
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
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
-
maximal stability
5900
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
ManD exhibits no enzymatic activity at 4C
52
-
2 min, about 50% loss of activity
59
-
1 min, 90% loss of activity
additional information
-
D-gluconate protects against heat denaturation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 10 mM Tris buffer, pH 7.0, 10% loss of activity after 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Superdex 200 gel filtration
using Ni-NTA chromatography
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced more than 1000fold when Caulobacter crescentus NA1000 is grown on D-glucuronate as a carbon source
B8GZZ7
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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