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Information on EC 1.1.1.203 - uronate dehydrogenase and Organism(s) Pseudomonas syringae pv. tomato and UniProt Accession Q888H1

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     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.203 uronate dehydrogenase
IUBMB Comments
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 . The 1,5-lactone product is rather stable at cytosolic pH and does not hydrolyse spontaneously at a substantial rate.
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This record set is specific for:
Pseudomonas syringae pv. tomato
UNIPROT: Q888H1
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The taxonomic range for the selected organisms is: Pseudomonas syringae pv. tomato
Synonyms
Atu3143, CsUDH, galacturonate acid reductase, GalUR, PfUDH, PmUDH, PnUDH, PSPTO_1053, PsUDH, Udh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PSPTO_1053
287792
gene name
uronate dehydrogenase
287792
-
uronate:NAD-oxidoreductase
-
-
-
-
uronic acid dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
-
?
D-galacturonate + NAD+ + H2O
D-galactarate + NADH + H+
show the reaction diagram
-
-
-
?
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
-
-
?
D-mannuronate + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
substrate and cofactor specificity of Udhs, overview
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-galacturonate + NAD+
D-galactaro-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
-
?
beta-D-glucuronate + NAD+
D-glucaro-1,5-lactone + NADH + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.107
beta-D-galacturonate
0.14 - 1.34
beta-D-glucuronate
0.04
D-galacturonate
-
-
0.28
D-glucuronate
-
-
7.3 - 22.05
D-Mannuronate
0.17 - 0.37
NAD+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21 - 29
beta-D-galacturonate
63 - 217
beta-D-glucuronate
0.24
D-galacturonate
-
-
0.74
D-glucuronate
-
-
6.4 - 7
D-Mannuronate
215
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260 - 794
beta-D-galacturonate
162 - 465
beta-D-glucuronate
0.3 - 9
D-Mannuronate
1262
NAD+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
value about, culture condition 1-3 days, 30°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
-
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
-
activity range, inactivation at 55°C, profile overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30000, SDS-PAGE
additional information
-
amino acid sequence comparisons with Rossmann fold, NAD+ and substrate binding sequences, and catalytic residues TyrxxxLys and S/T, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
purified recombinant His-tagged enzyme, inactivation within 50 min
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
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
gene udh, phylogenetic tree, recombinant soluble expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene udh, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moon, T.S.; Yoon, S.H.; Lanza, A.M.; Roy-Mayhew, J.D.; Prather, K.L.
Production of glucaric acid from a synthetic pathway in recombinant Escherichia coli
Appl. Environ. Microbiol.
75
589-595
2009
Pseudomonas syringae pv. tomato (Q888H1), Pseudomonas syringae pv. tomato DC3000 (Q888H1)
Manually annotated by BRENDA team
Yoon, S.H.; Moon, T.S.; Iranpour, P.; Lanza, A.M.; Prather, K.J.
Cloning and characterization of uronate dehydrogenases from two pseudomonads and Agrobacterium tumefaciens strain C58
J. Bacteriol.
191
1565-1573
2009
Agrobacterium tumefaciens, Agrobacterium tumefaciens (Q7CRQ0), Agrobacterium tumefaciens C58 / ATCC 33970 (Q7CRQ0), Pseudomonas putida KT2440, Pseudomonas putida KT2440 (Q88NN6), Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato (Q888H1), Pseudomonas syringae pv. tomato DC3000 (Q888H1)
Manually annotated by BRENDA team
Wagschal, K.; Jordan, D.B.; Lee, C.C.; Younger, A.; Braker, J.D.; Chan, V.J.
Biochemical characterization of uronate dehydrogenases from three pseudomonads, Chromohalobacter salixigens, and Polaromonas naphthalenivorans
Enzyme Microb. Technol.
69
62-68
2015
Chromohalobacter salexigens, Polaromonas naphthalenivorans, Pseudomonas fluorescens, Pseudomonas fluorescens Pf0-1, Pseudomonas mendocina, Pseudomonas syringae pv. tomato (Q888H1), Pseudomonas syringae pv. tomato ATCC BAA-871 / DC3000 (Q888H1)
Manually annotated by BRENDA team
Pick, A.; Schmid, J.; Sieber, V.
Characterization of uronate dehydrogenases catalysing the initial step in an oxidative pathway
Microb. Biotechnol.
8
633-643
2015
Agrobacterium tumefaciens, Agrobacterium tumefaciens (Q7CRQ0), Agrobacterium tumefaciens C58 / ATCC 33970 (Q7CRQ0), Fulvimarina pelagi, Oceanicola granulosus, Oceanicola granulosus DSM 15982, Pseudomonas syringae pv. tomato (Q888H1), Pseudomonas syringae pv. tomato DC3000 (Q888H1), Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
Manually annotated by BRENDA team
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