Information on EC 4.1.1.35 - UDP-glucuronate decarboxylase

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

EC NUMBER
COMMENTARY hide
4.1.1.35
-
RECOMMENDED NAME
GeneOntology No.
UDP-glucuronate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-D-glucuronate = UDP-D-xylose + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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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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Metabolic pathways
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UDP-alpha-D-xylose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming)
Requires NAD+.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-68-4
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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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-
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Manually annotated by BRENDA team
strain 399
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Manually annotated by BRENDA team
strain 399
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-
Manually annotated by BRENDA team
Columbia
Q9LFG7
GenBank
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
; cultivar Pima90-53
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
enzyme HvUXS1; enzyme HvUXS2; enzyme HvUXS3; enzyme HvUXS4
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Micromonospora echinospora subsp. calichensis
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-
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pea
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain N2
TrEMBL
Manually annotated by BRENDA team
strain N2
TrEMBL
Manually annotated by BRENDA team
rat
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis; UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis; UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis; UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis; UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis; UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis; UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-azido-UDP-glucuronate
5-azido-UDP-xylose + CO2
show the reaction diagram
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-
-
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UDP-D-glucuronate
UDP-D-xylose + CO2
show the reaction diagram
UDP-glucuronate
UDP-xylose + CO2
show the reaction diagram
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-D-glucuronate
UDP-D-xylose + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
activates; activates
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine
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3-Formylpyridine
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3-Propionylpyridine
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-
CaCl2
slight inhibition
CDP
0.2 mM, 29% inhibition
CTP
0.2 mM, 15% inhibition
GDP
0.2 mM, 23% inhibition; 0.2 mM,% inhibition
GDP-mannose
0.2 mM, 17% inhibition; 0.2 mM, 19% inhibition
iodoacetamide
-
-
KCl
-
-
MgCl2
slight inhibition
MnCl2
slight inhibition
NEM
-
-
p-hydroxymercuribenzoate
-
-
TDP
0.2 mM, 64% inhibition; 0.2 mM, 93% inhibition
Thionicotinamide
-
-
TMP
0.2 mM, 33% inhibition
TTP
0.2 mM, 96% inhibition; 0.2 mM, 97% inhibition
UDP-D-Gal
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slight inhibition of enzyme HvUXS1
UDP-D-Glc
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slight inhibition of enzyme HvUXS1
UDP-D-Xyl
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feedback inhibition of HvUXS1, strong inhibition at 0.6 mM
UDP-glucose
0.2 mM, 28% inhibition
UDP-xylose
0.2 mM, 39% inhibition; 0.2 mM, 41% inhibition
UDParabinose
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UDPglucose
UDPxylose
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
0.2 mM, activates to 138% of control
D-glucose
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activation at low substrate concentrations
NADH
0.2 mM, activation to 126% of control; 0.2 mM, activation to 196% of control
NH4Cl
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activates
UDP-galactose
0.2 mM, activates to 117% of control
UDPglucuronate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0086 - 0.19
UDP-D-glucuronate
0.767
UDP-glucuronic acid
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pH 7.0, 37C
0.0083 - 1.1
UDPglucuronate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 2.7
UDP-D-glucuronate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.099
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enzyme HvUXS1
1.78
recombinant enzyme
3.02
purified enzyme
4.98
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
recombinant enzyme
7.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
Q9LFG7
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6 - 7.8
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about 75% of maximal activity at pH 6.0 and 7.8
6 - 8
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pH 6.0: about 20% of maximal activity, pH 8.0: about 40% of maximal activity
6.5 - 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 42
Q9LFG7
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
isoform UXS6, calculated from amino acid sequence
7.7
isoform UXS7, calculated from amino acid sequence
8.1
isoform UXS2, calculated from amino acid sequence
8.4
isoform UXS3, calculated from amino acid sequence
8.7
isoform UXS4, calculated from amino acid sequence
8.9
isoform UXS1, calculated from amino acid sequence
9.4
isoform UXS5, calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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activity increases from the early stages of elongation growth, doubled in activity by the time the hypocotyl is differentiating
Manually annotated by BRENDA team
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HvUXS3 mRNA is low in all tissues; the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues; transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues; transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
Manually annotated by BRENDA team
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transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues; transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
Manually annotated by BRENDA team
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HvUXS3 mRNA is low in all tissues; the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues; transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues; transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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occurs as a membrane-associated form as well as a soluble form
Manually annotated by BRENDA team
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lumenal orientation
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
Micromonospora echinospora subsp. calichensis
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SDS-PAGE
36100
deduced from amino acid sequence
38500
x * 38500, isoform UXS3, calculated from amino acid sequence
39000
x * 39000, isoform UXS7, calculated from amino acid sequence
39100
x * 39100, isoform UXS6, calculated from amino acid sequence
42000
6 * 42000, SDS-PAGE
42600
Q9LFG7
reombinant enzyme, SDS-PAGE
46500
predicted from amino acid sequence
47500
x * 47500, isoform UXS4, calculated from amino acid sequence
49400
x * 49400, isoform UXS5, calculated from amino acid sequence
49700
x * 49700, isoform UXS2, calculated from amino acid sequence
60000
x * 60000, isoform UXS1, SDS-PAGE; x * 60000, isoform UXS1, SDS-PAGE; x * 60000, isoform UXS3, SDS-PAGE; x * 60000, isoform UXS3, SDS-PAGE
60700
x * 60700, isoform UXS2, SDS-PAGE
66700
x * 66700, isoform UXS2, SDS-PAGE
87000
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? * 87000, SDS-PAGE
210000
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gel filtration
220000
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gel filtration
250000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 42000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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rapid inactivation without glycerol
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by repeated freezing and thawing
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repeated freeze and thawing of samples results in significant loss of activity
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stable when stored at -90C and thawed and frozen three times, at days 0, 50 and 100
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, retains activity for at least 1 month
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-20C or -90C, 60% w/v glycerol, stable for at least 100 days
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-20C, stable for at least 9 months
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-70C, activity is not effected by storage for several months
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-70C, stable for several months
4C, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Co2+-charged Talon Dynabead chromatography
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His Ni-Superflow resin column chromatography; His Ni-Superflow resin column chromatography; His Ni-Superflow resin column chromatography; His Ni-Superflow resin column chromatography
recombinant; recombinant; recombinant
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an Escherichia coli system containing the sugar biosynthetic pathway and the glycosyltransferase gene from Arabidopsis thaliana for the production of xylosylated naringenin is generated, Escherichia coli XL1-Blue (MRF) is used as a host cell for recombinant plasmid preparation and DNA manipulation, whereas Escherichia coli BL21 (DE3) DELTApgi is used for biotransformation of the recombinant
Micromonospora echinospora subsp. calichensis
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cDNA cloned and expressed in Escherichia coli, clone PsUXS1
cloned and expressed in bacteria and transfected HEK293T cells
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21 (DE3) pLysS cells
expression in Escherichia coli
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expression in Escherichia coli BL21 (DE3), the deoxysugar biosynthesis of Streptomyces sp. KCTC 0041BP is inactivated by gene replacement to generate Streptomyces sp. GerSM2 mutant, which is unable to produce dihydrochalcomycin, calS9 UDP-xylose biosynthetic genes are cloned in an integrative plasmid pSET152 to generate pBPDS, which is heterologously expressed in Streptomyces sp. GerSM2. A glycosylated product, a 5-O-xylosyl-chalconolide derivative, in the conjugal transformants is isolated
Micromonospora echinospora subsp. calichensis
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expression in Escherichia coli BL21 as His-tagged enzyme
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression of HvUXS1 cDNA in Escherichia coli
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gene AtUXS1 cDNA cloned and expressed in Escherichia coli BL21(DE3) pLysS
Q9LFG7
gene UXS1 cloned and expressed in Escherichia coli BL21 (DE3)pLysS
transformed with the ipt gene from Agrobacterium tumefaciens
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uxs gene cloned by RT-PCR and expressed in Escherichia coli BL21(DE3) pLys
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of PpmrI can be induced by polymyxin B via RppA, a response regulator of the bacterial two-component system. Together, these results reveal a mechanism by which Proteus mirabilis regulates polymyxin B resistance and virulence
the enzyme is preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis
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the enzyme is preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis; UXS transcripts are preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis
the enzyme is preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis; UXS transcripts are preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis; UXS transcripts are preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis; UXS transcripts are preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (207 entries)
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