Information on EC 1.1.1.305 - UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.305
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RECOMMENDED NAME
GeneOntology No.
UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate + NAD+ = UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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polymyxin resistance
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronate:NAD+ oxidoreductase (decarboxylating)
The activity is part of a bifunctional enzyme also performing the reaction of EC 2.1.2.13 (UDP-4-amino-4-deoxy-L-arabinose formyltransferase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
gene RsU4kpxs
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
-
induced-fit conformational change associated with cofactor binding, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucuronate + NAD+
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
UDP-glucuronate + NAD+
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
UUDP-alpha-D-glucuronate + NAD+
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
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-
-
-
?
additional information
?
-
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
UDP-alpha-D-glucuronate + NAD+
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
UDP-glucuronate + NAD+
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
UUDP-alpha-D-glucuronate + NAD+
UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
show the reaction diagram
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-
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
induced-fit conformational change associated with cofactor binding, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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exogenous NAD+ stimulates enzyme activity, because a small fraction of hUXS releases the NADH and UDP-alpha-D-4-dehydroxylose intermediates as products during turnover. The resulting apoenzyme can be rescued by exogenous NAD+, explaining the apparent stimulatory effect of added cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1132 - 1.6
NAD+
0.054 - 0.7
UDP-glucuronate
0.0222
UDP-glucuronic acid
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pH 7.6, 37C, recombinant enzyme
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32
NAD+
Ralstonia solanacearum
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pH 7.6, 37C, recombinant enzyme
0.285
UDP-glucuronic acid
Ralstonia solanacearum
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pH 7.6, 37C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8
NAD+
Ralstonia solanacearum
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pH 7.6, 37C, recombinant enzyme
7
12.8
UDP-glucuronic acid
Ralstonia solanacearum
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pH 7.6, 37C, recombinant enzyme
1225
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 11
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activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 60
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activity range, profile overview
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000 - 120000
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gel filtration, recombinant enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB entry 1Z7E
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crystal structure of the ArnA decarboxylase domain
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crystallization of native and Se-Met decarboxylase protein. Good quality crystals are obtained with a precipitant solution of 3.2 M NaCl, 0.1 M Bistris, pH 5.2, using a drop containing 0.004 ml of protein and 0.004 ml of precipitant equilibrated against a reservoir of 0.1 ml of precipitant. Space group as P4(1)3(2), with cell dimensions a = b = c = 149.4 A, beta = gamma = 90
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hanging drop vapor diffusion method, crystal structure of the full-length bifunctional ArnA with UDP-glucuronic acid and ATP bound to the dehydrogenase domain. Binding of UDP-glucuronic acid triggers a 17 A conformational change in ArnA_DH that opens the NAD+ binding site while trapping UDP-glucuronic acid
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purified recombinant UXS85-420 lacking the N-terminal membrane-spanning domain, hanging drop vapor diffusion method, precipitant containing 1.3 M ammonium sulfate, 0.1 M magnesium formate, and 0.15% PEG at 26C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant
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recombinant His-tagged enzyme from Escherichia coli by nicke affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme in Escherichia coli
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overexpression of ArnA as a hexahistidine fusion protein, cloning and expression the separate domains in pET28b and pWSK29
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overexpression of native and selenomethionine decarboxylase and formyltransferase domains of ArnA
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E434Q
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mutant is inactive, suggesting that chemical rather than steric properties of this residue are crucial in the decarboxylation reaction
R610M
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activity is 800fold lower than wild-type activity
R619E
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no activity
R619Y
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no activity
S433A
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activity is 30fold lower than wild-type activity
S433T
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no activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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modification of the lipid A moiety of lipopolysaccharide by the addition of the sugar 4-amino-4-deoxy-L-arabinose is a strategy adopted by pathogenic Gram-negative bacteria to evade cationic antimicrobial peptides produced by the innate immune system. L-Ara4N biosynthesis is therefore a potential anti-infective target
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