Information on EC 1.1.1.203 - uronate dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.203
-
RECOMMENDED NAME
GeneOntology No.
uronate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-D-galacturonate + NAD+ = D-galactaro-1,5-lactone + NADH + H+
show the reaction diagram
(1)
-
-
-
beta-D-glucuronate + NAD+ = D-glucaro-1,5-lactone + NADH + H+
show the reaction diagram
(2)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
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D-galacturonate degradation II
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D-glucuronate degradation II
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degradation of sugar acids
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SYSTEMATIC NAME
IUBMB Comments
uronate:NAD+ 1-oxidoreductase
Requires Mg2+. The enzyme, characterized from the bacterium Agrobacterium fabrum, participates in oxidative degradation pathways for galacturonate and glucuronate. The enzyme can only accept the beta anomeric form of the substrate [4]. The 1,5-lactone product is rather stable at cytosolic pH and does not hydrolyse spontaneously at a substantial rate.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-98-9
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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-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
show the reaction diagram
D-glucuronate + NAD+
D-glucaric acid 3,6-lactone + NADH + H+
show the reaction diagram
-
weak reversible reaction, 3% of the activity compared to the forward reaction
-
r
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
show the reaction diagram
D-glucuronic acid + NAD+ + H2O
D-glucaric acid + NADH + H+
show the reaction diagram
assay at pH 8.0
-
-
?
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-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
show the reaction diagram
D-glucuronate + NAD+
D-glucaric acid 3,6-lactone + NADH + H+
show the reaction diagram
-
weak reversible reaction, 3% of the activity compared to the forward reaction
-
r
D-glucuronate + NAD+ + H2O
D-glucaric acid + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
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complete inhibition at 1 mM
KCN
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15% inhibition at 1 mM
N-ethylmaleimide
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inhibition at 1 mM, reversal by an excess of L-cysteine
NADH
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competitive inhibition, Ki: 0.06 mM
p-chloromercuribenzoic acid
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60% inhibition at 1 mM, reversal by an excess of L-cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.16
D-galacturonate
0.15 - 0.37
D-glucuronate
0.08 - 5.3
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 26.7
D-galacturonate
0.55 - 80
D-glucuronate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
value about, culture condition 1-3 days, 30C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Agrobacterium fabrum (strain C58 / ATCC 33970)
Agrobacterium fabrum (strain C58 / ATCC 33970)
Agrobacterium fabrum (strain C58 / ATCC 33970)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30500
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2 * 30500, SDS-PAGE, subunits alone inactive
32000
x * 32000, SDS-PAGE
59000
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gel filtration, ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 30500, SDS-PAGE, subunits alone inactive
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of an apo-form, a ternary form in complex with NADH and product, and an inactive Y136A mutant in complex with NAD+. Enzyme is a homohexamer. The monomer contains a Rossmann fold, essential for nucleotide binding. The ternary complex structure reveals a product, D-galactaro-1,5-lactone, which is bound above the nicotinamide ring. This product rearranges in solution to D-galactaro-1,4-lactone
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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50% remaining activity
286230
9.4
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50% remaining activity
286230
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 15
-
stable for 24 h
30 - 35
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loss of activity after 30 min
37
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90% loss of activity within 60 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT and dithioerythritol have protective function against thermal destruction
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NAD+ increases stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, 50 mM Tris-HCl, pH 7.2, 2.9 mM NAD+, less then 10% loss of activity up to 6 months
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-20C, 50 mM sodium diphosphate-HCl, pH 8.0, 0.1% bovine serum albumin, no loss of activity
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4C, 50 mM sodium diphosphate-HCl, pH 8.0, 30% glycerol, 5% loss of activity within 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration
to homogeneity, chromatography techniques
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; Udh subcloned into vector pTrc99A to produce pT1053 and transformed into Escherichia coli BL21 Star (DE3) to construct an Escherichia coli strain carrying INO1, MIOX, and udh
udh gene from genomic DNA amplified and inserted into pET21b containing a six-His tag and expressed in Escherichia coli BL21(DE3) or inserted into vector pTrc99SE and transformed into Escherichia coli mutant strain MG1655 DELTAuxaC
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
treatment with 8 M urea and 24 h dialysis: 10% of initial activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation