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Information on EC 4.1.1.35 - UDP-glucuronate decarboxylase
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EC Tree
4.1.1.35 UDP-glucuronate decarboxylaseIUBMB Comments
Requires NAD+.
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Word Map
- 4.1.1.35
- udp-xylose
- polysaccharide
- xylans
- udp-xyl
- xylem
-
xylosylation
- xyloglucan
-
xylose-containing
-
xylosyltransferases
- neoformans
The enzyme appears in viruses and cellular organisms
Synonyms
udp-glucuronic acid decarboxylase, udp-glucuronate decarboxylase, hvuxs1, udp-glca decarboxylase, osuxs2, osuxs3, hvuxs4, hvuxs2, hvuxs3, udp-d-glucuronate carboxy-lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, uridine diphosphoglucuronate
-
-
-
-
PelgB_010100016590
PelgB_010100037712
UDP-GlcA decarboxylase
UDP-glucuronate decarboxylase
UDP-glucuronic acid decarboxylase
UDPglucuronate carboxy-lyase
-
-
-
-
Uridine diphosphate glucuronate carboxy-lyase
-
-
-
-
Uridine-diphospho glucuronate decarboxylase
-
-
-
-
UXS
Uxs1
Uxs2
UXS3
UXS4
UXS5
UXS6
UDP-glucuronate decarboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-D-glucuronate = UDP-D-xylose + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-D-glucuronate carboxy-lyase (UDP-D-xylose-forming)
Requires NAD+.
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CAS REGISTRY NUMBER
COMMENTARY
9024-68-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-glucuronate
UDP-D-xylose + CO2
-
specific substrate
-
-
?
UDP-D-glucuronate
UDP-D-xylose + CO2
Micromonospora echinospora subsp. calichensis
-
-
-
-
?
UDP-D-glucuronate
UDP-D-xylose + CO2
-
biosynthesis of cell wall polysaccharides and glycosylation of proteins
-
ir
UDP-D-glucuronate
UDP-D-xylose + CO2
-
-
-
?
additional information
?
-
-
the enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
increase in activity at the final stage of differentation of cambium to xylem
-
-
?
additional information
?
-
-
no activity with UDP-galacturonate
-
-
?
additional information
?
-
-
the enzyme is directly involved in the production of some of the precursors of hemicellulose and pectin. Close correlation between UDP-D-glucuronate decarboxylase activity and secondary wall formation
-
-
?
additional information
?
-
-
the enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
increase in activity at the final stage of differentation of cambium to xylem
-
-
?
additional information
?
-
key enzyme in proteoglycan synthesis
-
?
additional information
?
-
-
synthesis of UDPxylose is controlled both by substrate activation and product inhibition of UDPglucuronate carboxy-lyase
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-glucuronate
UDP-D-xylose + CO2
Micromonospora echinospora subsp. calichensis
-
-
-
-
?
UDP-D-glucuronate
UDP-D-xylose + CO2
-
biosynthesis of cell wall polysaccharides and glycosylation of proteins
-
ir
UDP-D-glucuronate
UDP-D-xylose + CO2
-
-
-
?
additional information
?
-
-
the enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
increase in activity at the final stage of differentation of cambium to xylem
-
-
?
additional information
?
-
-
the enzyme is directly involved in the production of some of the precursors of hemicellulose and pectin. Close correlation between UDP-D-glucuronate decarboxylase activity and secondary wall formation
-
-
?
additional information
?
-
-
the enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
increase in activity at the final stage of differentation of cambium to xylem
-
-
?
additional information
?
-
key enzyme in proteoglycan synthesis
-
?
additional information
?
-
-
synthesis of UDPxylose is controlled both by substrate activation and product inhibition of UDPglucuronate carboxy-lyase
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GDP-mannose
0.2 mM, 17% inhibition; 0.2 mM, 19% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
pH 6.0: about 20% of maximal activity, pH 8.0: about 40% of maximal activity
6.5 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity increases from the early stages of elongation growth, doubled in activity by the time the hypocotyl is differentiating
brenda
-
brenda
additional information
-
increase in activity at the final stage of differentiation of cambium to xylem
brenda
-
increase in activity at the final stage of differentiation of cambium to xylem
brenda
-
in tissue culture, enzyme activity increases up to mid-log phase and decreases rapidly as the growth rate declines
brenda
-
transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues
brenda
-
transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues
brenda
-
transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
highest expression of isoform UXS1 in mature leaf
brenda
highest expression of isoform UXS5 in mature leaf
brenda
-
the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues
brenda
-
transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues
brenda
expression level of OsUXS2 is high during development of seed
brenda
expression level of OsUXS3 is consitently high during development of seed
brenda
-
the abundance of HvUXS1 mRNA is 10fold higher in mature roots and stems than in leaves, developing grains, or floral tissues
brenda
-
transcriptional activity of enzyme HvUXS2 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
transcriptional activity of enzyme HvUXS4 is relatively high in mature root, coleoptiles, and stems, compared with root tips, leaves and floral tissues
brenda
-
increase in activity at the final stage of differentiation of cambium to xylem
brenda
highest expression of isoform UXS3 in immature xylem
brenda
-
increase in activity at the final stage of differentiation of cambium to xylem
brenda
additional information
-
enzyme HvUXS1 is most abundant among the 4HvUXs genes, accounting for more than 80% of total HvUXS transcripts in most of the tissues examined
brenda
additional information
-
mRNA concentration is highest in tissues associated with secondary wall formation
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
occurs as a membrane-associated form as well as a soluble form
brenda
enzyme contains a putative membrane-binding region
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
deletion of genes Uxs1 and Uxs2 separately does not result in the loss of a detectable phenotype, but deletion of both genes abrogates polysaccharide F synthesis
malfunction
-
deletion of genes Uxs1 and Uxs2 separately does not result in the loss of a detectable phenotype, but deletion of both genes abrogates polysaccharide F synthesis
-
physiological function
UDP-glucuronate decarboxylase is a key enzyme in the synthesis of UDP-xylose for the formation of xylans during cell wall biosynthesis
physiological function
a triple mutant lacking the cytosolic isoform Uxs3 Uxs5 Uxs6 triple mutant has an irregular xylem phenotype. Xylose levels decrease in the Uxs3 Uxs5 Uxs6 triple mutant and the xylan content declines. The molecular weight of noncellulosic polysaccharides in the triple mutant is lower than that in the wild type. Upon saccharification treatment stems of the Uxs3 Uxs5 Uxs6 triple mutant release monosaccharides with a higher efficiency than those of the wild type
physiological function
a triple mutant lacking the Golgi isoforms Uxs1 Usx2 Uxs4 shows no obvious phenotype
physiological function
-
expression in an antisense orientation in Arabidopsis thaliana. Transgenic plant show shorter roots, earlier blossom formation, and delayed senescence. Levels of rhamnose, mannose, galactose, glucose, xylose, and cellulose are reduced in some of the down-regulated antisense plants
physiological function
-
the intracellular UDP-xylose and UDP-glucuronic acid levels are affected in isoform Uxs1 or Uxs2 knockout strains. The knockout of either Uxs1 or Uxs2 reduces the polysaccharide production and changes the monosaccharide ratio. No polysaccharide is found in the Uxs1/Uxs2 double knockout strain
physiological function
-
the intracellular UDP-xylose and UDP-glucuronic acid levels are affected in isoform Uxs1 or Uxs2 knockout strains. The knockout of either Uxs1 or Uxs2 reduces the polysaccharide production and changes the monosaccharide ratio. No polysaccharide is found in the Uxs1/Uxs2 double knockout strain
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
40000
47000
47500
x * 47500, isoform UXS4, calculated from amino acid sequence
48300
49400
x * 49400, isoform UXS5, calculated from amino acid sequence
49700
x * 49700, isoform UXS2, calculated from amino acid sequence
60000
48300
x * 48300, isoform UXS1, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 38500, isoform UXS3, calculated from amino acid sequence
?
x * 39000, isoform UXS7, calculated from amino acid sequence
?
x * 39100, isoform UXS6, calculated from amino acid sequence
?
x * 47500, isoform UXS4, calculated from amino acid sequence
?
x * 48300, isoform UXS1, calculated from amino acid sequence
?
x * 49400, isoform UXS5, calculated from amino acid sequence
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
by using Tn5 transposon mutagenesis, a gene, PpmrI, is identified which plays important roles in controlling lipopolysaccharides modification, polymyxin B susceptibility, biofilm formation, and cell invasion in Proteus mirabilis. The 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
additional information
-
by using Tn5 transposon mutagenesis, a gene, PpmrI, is identified which plays important roles in controlling lipopolysaccharides modification, polymyxin B susceptibility, biofilm formation, and cell invasion in Proteus mirabilis. The 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
additional information
-
by using Tn5 transposon mutagenesis, a gene, PpmrI, is identified which plays important roles in controlling lipopolysaccharides modification, polymyxin B susceptibility, biofilm formation, and cell invasion in Proteus mirabilis. The 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
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freeze and thawing of samples results in significant loss of activity
-
stable when stored at -90°C and thawed and frozen three times, at days 0, 50 and 100
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
-
expressed in Escherichia coli BL21 (DE3) pLysS cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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
-
gene AtUXS1 cDNA cloned and expressed in Escherichia coli BL21(DE3) pLysS
Q9LFG7
gene UXS1 cloned and expressed in Escherichia coli BL21 (DE3)pLysS
uxs gene cloned by RT-PCR and expressed in Escherichia coli BL21(DE3) pLys
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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
UXS transcripts are preferentially expressed during fiber development, from elongation through the stage of secondary cell wall synthesis
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
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
the enzyme is 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
-
-
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
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dalessandro, G.; Northcote, D.H.
Changes in enzymic activities of UDP-D-glucuronate decarboxylase and UDP-D-xylose 4-epimerase during cell division and xylem differentiation in cultured explants of Jerusalem artichoke
Phytochemistry
16
853-859
1977
Helianthus tuberosus
-
brenda
Dalessandro, G.; Northcote, D.H.
Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in pine and fir
Biochem. J.
162
281-288
1977
Abies grandis, Pinus sylvestris
brenda
Dalessandro, G.; Northcote, D.H.
Changes in enzymic activities of nucleoside diphosphate sugar interconversions during differentiation of cambium to xylem in sycamore and poplar
Biochem. J.
162
267-279
1977
Acer pseudoplatanus, Populus x canadensis
brenda
Ankel, H.; Feingold, D.S.
Biosynthesis of uridine diphosphate D-xylose. I. Uridine diphosphate glucuronate carboxy-lyase of wheat germ
Biochemistry
4
2468-2475
1965
Triticum aestivum
-
brenda
Fan, D.F.; Feingold, D.S.
Biosynthesis of uridine diphosphate D-xylose. V. UDP-D-glucuronate and UDP-D-galacturonate carboxy-lyase of Ampullariella digitata
Arch. Biochem. Biophys.
148
576-580
1972
Actinoplanes digitatis, Actinoplanes digitatis 399
brenda
Ankel, H.; Feingold, D.S.
UDP-glucuronic acid decarboxylase
Methods Enzymol.
8
287-292
1966
Papiliotrema laurentii, Triticum aestivum
-
brenda
Gustine, D.L.; Hso-Freng Yuan, D.; Kindel, P.K.
Uridine diphosphate D-glucuronic acid cyclase and uridine diphosphate D-glucuronic acid carboxy-lyase I from Lemna minor. Purification, characterization, and separation from uridine diphosphate D-glucuronic acid carboxy-lyase II
Arch. Biochem. Biophys.
170
82-91
1975
Lemna minor
brenda
John, K.V.; Schwartz, N.B.; Ankel, H.
UDP-glucuronate carboxy-lyase in cultured chondrocytes
J. Biol. Chem.
252
6707-6710
1977
Gallus gallus
brenda
John, K.V.; Schutzbach, J.S.; Ankel, H.
Separation and allosteric properties of two forms of UDP-glucuronate carboxy-lyase
J. Biol. Chem.
252
8013-8017
1977
Triticum aestivum
brenda
Jacobson, E.S.; Payne, W.R.
UDP glucuronate decarboxylase and synthesis of capsular polysaccharide in Cryptococcus neoformans
J. Bacteriol.
152
932-934
1982
Cryptococcus neoformans
brenda
Hayashi, T.; Koyama, T.; Matsuda, K.
Formation of UDP-xylose and xyloglucan in soybean Golgi membranes
Plant Physiol.
87
341-345
1988
Glycine max
brenda
Robertson, D.; Beech, I.; Bolwell, G.P.
Regulation of the enzymes of UDP-sugar metabolism during differentiation of french bean
Phytochemistry
39
21-28
1995
Phaseolus vulgaris
-
brenda
Kyossev, Z.N.; Drake, R.R.; Kyosseva, S.V.; Elbein, A.D.
Synthesis of a new photoaffinity probe, 5-azido-[32P]UDPxylose, by UDPglucuronate carboxylyase from wheat germ
Eur. J. Biochem.
228
109-112
1995
Triticum aestivum
brenda
Kearns, A.E.; Vertel, B.M.; Schwartz, N.B.
Topography of glycosylation and UDP-xylose production
J. Biol. Chem.
268
11097-11104
1993
Gallus gallus
brenda
Moriarity, J.L.; Hurt, K.J.; Resnick, A.C.; Storm, P.B.; Laroy, W.; Schnaar, R.L.; Snyder, S.H.
UDP-glucuronate decarboxylase, a key enzyme in proteoglycan synthesis: cloning, characterization, and localization
J. Biol. Chem.
277
16968-16975
2002
Rattus norvegicus (Q5PQX0)
brenda
Suzuki, K.; Suzuki, Y.; Kitamura, S.
Cloning and expression of a UDP-glucuronic acid decarboxylase gene in rice
J. Exp. Bot.
54
1997-1999
2003
Oryza sativa (Q8W3J1), Oryza sativa
brenda
Wheatley, E.R.; Davies, D.R.; Bolwell, G.P.
Characterisation and immunolocation of an 87 kDa polypeptide associated with UDP-glucuronic acid decarboxylase activity from differentiating tobacco cells (Nicotiana tabacum L.)
Phytochemistry
61
771-780
2002
Nicotiana tabacum
brenda
Kobayashi, M.; Nakagawa, H.; Suda, I.; Miyagawa, I.; Matoh, T.
Purification and cDNA cloning of UDP-D-glucuronate carboxy-lyase (UDP-D-xylose synthase) from pea seedlings
Plant Cell Physiol.
43
1259-1265
2002
Pisum sativum (Q9AV98), Pisum sativum
brenda
Harper, A.D.; Bar-Peled, M.
Biosynthesis of UDP-xylose. Cloning and characterization of a novel Arabidopsis gene family, UXS, encoding soluble and putative membrane-bound UDP-glucuronic acid decarboxylase isoforms
Plant Physiol.
130
2188-2198
2002
Arabidopsis thaliana (Q9LFG7)
brenda
Bar-Peled, M.; Griffith, C.L.; Doering, T.L.
Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis
Proc. Natl. Acad. Sci. USA
98
12003-12008
2001
Cryptococcus neoformans (Q96V00), Cryptococcus neoformans
brenda
Suzuki, K.; Watanabe, K.; Masumura, T.; Kitamura, S.
Characterization of soluble and putative membrane-bound UDP-glucuronic acid decarboxylase (OsUXS) isoforms in rice
Arch. Biochem. Biophys.
431
169-177
2004
Oryza sativa (Q75PK6), Oryza sativa (Q75PK7), Oryza sativa (Q8W3J0), Oryza sativa
brenda
Bindschedler, L.V.; Wheatley, E.; Gay, E.; Cole, J.; Cottage, A.; Bolwell, G.P.
Characterisation and expression of the pathway from UDP-glucose to UDP-xylose in differentiating tobacco tissue
Plant Mol. Biol.
57
285-301
2005
Nicotiana tabacum
brenda
Zhang, Q.; Shirley, N.; Lahnstein, J.; Fincher, G.B.
Characterization and expression patterns of UDP-D-glucuronate decarboxylase genes in barley
Plant Physiol.
138
131-141
2005
Hordeum vulgare
brenda
Bindschedler, L.V.; Tuerck, J.; Maunders, M.; Ruel, K.; Petit-Conil, M.; Danoun, S.; Boudet, A.M.; Joseleau, J.P.; Bolwell, G.P.
Modification of hemicellulose content by antisense down-regulation of UDP-glucuronate decarboxylase in tobacco and its consequences for cellulose extractability
Phytochemistry
68
2635-2648
2007
Nicotiana tabacum (Q6IVK5), Nicotiana tabacum
brenda
Jiang, S.S.; Liu, M.C.; Teng, L.J.; Wang, W.B.; Hsueh, P.R.; Liaw, S.J.
Proteus mirabilis pmrI, an RppA-regulated gene necessary for polymyxin B resistance, biofilm formation, and urothelial cell invasion
Antimicrob. Agents Chemother.
54
1564-1571
2010
Proteus mirabilis (C9E3L0), Proteus mirabilis, Proteus mirabilis N2 (C9E3L0)
brenda
Simkhada, D.; Oh, T.J.; Pageni, B.B.; Lee, H.C.; Liou, K.; Sohng, J.K.
Characterization of CalS9 in the biosynthesis of UDP-xylose and the production of xylosyl-attached hybrid compound
Appl. Microbiol. Biotechnol.
83
885-895
2009
Micromonospora echinospora subsp. calichensis
brenda
Simkhada, D.; Kim, E.; Lee, H.C.; Sohng, J.K.
Metabolic engineering of Escherichia coli for the biological synthesis of 7-O-xylosyl naringenin
Mol. Cells
28
397-401
2009
Micromonospora echinospora subsp. calichensis
brenda
Coyne, M.J.; Fletcher, C.M.; Reinap, B.; Comstock, L.E.
UDP-glucuronic acid decarboxylases of Bacteroides fragilis and their prevalence in bacteria
J. Bacteriol.
193
5252-5259
2011
Bacteroides fragilis, Bacteroides fragilis NCTC 9343
brenda
Pan, Y.; Wang, X.; Liu, H.; Zhang, G.; Ma, Z.
Molecular cloning of three UDP-glucuronate decarboxylase genes that are preferentially expressed in Gossypium fibers from elongation to secondary cell wall synthesis
J. Plant Biol.
53
367-373
2010
Gossypium barbadense, Gossypium hirsutum, Gossypium hirsutum (G8XR12), Gossypium hirsutum (G8XR13), Gossypium hirsutum (G8XR16), Gossypium barbadense Pima90-53, Gossypium hirsutum CRI-8
-
brenda
Du, Q.; Pan, W.; Tian, J.; Li, B.; Zhang, D.
The UDP-glucuronate decarboxylase gene family in Populus: structure, expression, and association genetics
PLoS ONE
8
e60880
2013
Populus tomentosa (N0A0C4), Populus tomentosa (N0A0D3), Populus tomentosa (N0A414), Populus tomentosa (N0A422), Populus tomentosa (N0A8N3), Populus tomentosa (N0A8N8), Populus tomentosa (N0A9U2), Populus tomentosa
brenda
Li, O.; Qian, C.D.; Zheng, D.Q.; Wang, P.M.; Liu, Y.; Jiang, X.H.; Wu, X.C.
Two UDP-glucuronic acid decarboxylases involved in the biosynthesis of a bacterial exopolysaccharide in Paenibacillus elgii
Appl. Microbiol. Biotechnol.
99
3127-3139
2015
Paenibacillus elgii, Paenibacillus elgii B69
brenda
Zhang, D.; Pan, Y.; Zhang, Y.; Li, Z.; Wu, L.; Liu, H.; Zhang, G.; Wang, X.; Ma, Z.
Antisense expression of Gossypium hirsutum UDP-glucuronate decarboxylase in Arabidopsis leads to changes in cell wall components
Genet. Mol. Res.
15
FEHLT
2016
Gossypium hirsutum
brenda
Kuang, B.; Zhao, X.; Zhou, C.; Zeng, W.; Ren, J.; Ebert, B.; Beahan, C.T.; Deng, X.; Zeng, Q.; Zhou, G.; Doblin, M.S.; Heazlewood, J.L.; Bacic, A.; Chen, X.; Wu, A.M.
Role of UDP-glucuronic acid decarboxylase in xylan biosynthesis in Arabidopsis
Mol. Plant
9
1119-1131
2016
Arabidopsis thaliana, Arabidopsis thaliana (Q8VZC0), Arabidopsis thaliana (Q9FIE8), Arabidopsis thaliana (Q9LZI2), Arabidopsis thaliana (Q9SN95), Arabidopsis thaliana (Q9ZV36)
brenda
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