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Information on EC 5.1.3.6 - UDP-glucuronate 4-epimerase
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5.1.3.6 UDP-glucuronate 4-epimeraseSpecify your search results
Word Map
- 5.1.3.6
-
udp-galacturonic
- polysaccharide
- udp-xylose
- nad+
- pectin
-
interconverts
-
4-epimerases
-
hydride
-
epimerization
-
acid-containing
- ump
-
hydrogen-bonding
- udp-xyl
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
AtUGlcAE1, AtUGlcAE2, AtUGlcAE3, Epimerase, uridine diphosphoglucuronate, GAE, GAE1, GAE2, GAE3, GAE4, GAE5, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GAE
GAE1
GAE2
GAE3
GAE4
GAE6
UDP-D-glucuronic acid 4-epimerase
UDP-GlcA 4-epimerase
UDP-GlcA 4-epimerase3
UDP-glucuronic acid 4-epimerase
-
UGlcAE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate = UDP-D-galacturonate
formation of a 4-keto intermediate
-
UDP-glucuronate = UDP-D-galacturonate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronate 4-epimerase
-
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CAS REGISTRY NUMBER
COMMENTARY
9024-17-3
-
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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-galacturonate
recombinant AtUGlcAE1DELTA1-64 favors the formation of UDP-D-galacturonate over UDP-glucuronate
-
-
r
UDP-D-glucuronate
UDP-D-galacturonate
-
equilibrium constant in direction of UDP-galacturonate formation is 1.3
-
r
UDP-glucuronate
UDP-D-galacturonate
-
-
-
?
UDP-glucuronate
UDP-D-galacturonate
the recombinant enzyme establishes a 1.3:1 equilibrium between UDP-D-galacturonate and UDP-glucuronate
-
-
r
additional information
?
-
-
enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
no epimerization of UDP-D-glucose and UDP-D-xylulose
-
-
?
additional information
?
-
no epimerization of UDP-D-glucose and UDP-D-xylulose
-
-
?
additional information
?
-
no epimerization of UDP-D-glucose and UDP-D-xylulose
-
-
?
additional information
?
-
no epimerization of UDP-D-glucose and UDP-D-xylulose
-
-
?
additional information
?
-
-
enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
the enzyme is required for capsular biosynthesis
-
?
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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
additional information
?
-
-
enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
enzyme is required for the nucleoside diphosphate sugar interconversion
-
-
?
additional information
?
-
-
the enzyme is required for capsular biosynthesis
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
NAD+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
additional information
recombinant OcUGlcAE3 does not require exogenous NAD+, suggesting the recombinant OcUGlcAE3 contains tightly bound NAD+
-
additional information
-
recombinant OcUGlcAE3 does not require exogenous NAD+, suggesting the recombinant OcUGlcAE3 contains tightly bound NAD+
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KCl
above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
p-hydroxymercuribenzoate
-
reactivation by NAD+ and 2-mercaptoethanol
NaCl
above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
NaCl
-
progressive decrease in activity above 100 mM NaCl, activity drops below 50% at 250 mM
additional information
no inhibition: UDP, UDP-D-glucose or UDP-D-galactose
-
additional information
no inhibition: UDP, UDP-D-glucose or UDP-D-galactose
-
additional information
no inhibition: UDP, UDP-D-glucose or UDP-D-galactose
-
additional information
no inhibition: UDP, UDP-D-glucose or UDP-D-galactose
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.259
UDP-glucuronate
recombinant OsUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
0.358
UDP-glucuronate
recombinant AtUGlcAE2, lacking the amino acid position 1-68, in 0.1 M sodium phosphate, pH 7.6
0.397
UDP-glucuronate
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, in 0.1 M sodium phosphate, pH 7.6
0.426
UDP-glucuronate
recombinant AtUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9
UDP-glucuronate
recombinant AtUGlcAE2, lacking the amino acid position 1-68, in 0.1 M sodium phosphate, pH 7.6
10
UDP-glucuronate
recombinant AtUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
10.1
UDP-glucuronate
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, in 0.1 M sodium phosphate, pH 7.6
37.4
UDP-glucuronate
recombinant OsUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1107
UDP
recombinant AtUGlcAE3, position 1-53 is lacking
0.1341
UDP
recombinant AtUGlcAE2, position 1-68 is lacking
0.1436
UDP
recombinant AtUGlcAE1, position 1-64 is lacking
0.2473
UDP-xylose
recombinant AtUGlcAE3, position 1-53 is lacking
0.2972
UDP-xylose
recombinant AtUGlcAE1, position 1-64 is lacking
0.3051
UDP-xylose
recombinant AtUGlcAE2, position 1-68 is lacking
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.8
optimal pH in phosphate buffer for the activity of recombinant enzyme ZmUGlcAE1-47 lacking the transmembrane domain
7.6
7.6
recombinant AtUGlcAE2, lacking the amino acid position 1-68
7.6
recombinant AtUGlcAE3, lacking the amino acid position 1-53
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
the activity of ZmUGlcAE1-47 is completely abolished when assays are conducted at pH value below 4 or above 10
4 - 11
activity range, enzyme activity increases gradually with the increase of pH. When pH reaches the range of pH 8-8.5, the enzyme displays the highest activity. With the further increase of pH to about pH 9, the activity of the enzyme decreases slightly. At pH 9-10, the activity of OcUGlcAE3 increases gradually, and reaches the highest activity again at pH value of 10. Above the pH 10.0, the activity decreases, 80% of maximal activity at pH 12.0. M-type pH profile
5 - 8.9
pH 5.0: about 75% of maximal activity, pH 8.9: 93% of maximal activity
5 - 9
pH 5.0: about 65% of maximal activity, pH 9.0: about 95% of maximal activity
6.5 - 10
-
pH 6.5: about 50% of maximal activity, pH 10.0: about 25% of maximal activity
7 - 10
-
about 50% of maximal activity at pH 7 and 10, epimerization of UDPglucuronate to UDPgalacturonate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
recombinant AtUGlcAE2, lacking the amino acid position 1-68
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
syncytia induced by nematode Heterodera schachtii
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
brenda
-
isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
brenda
additional information
-
enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
-
enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
-
differentiated and differentiating cells, enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
-
differentiated and differentiating cells, enzyme activity decreases during the differentiation of cambial cells to xylem
brenda
additional information
negligible activity in non-sterile bulbs and flowers
brenda
additional information
-
negligible activity in non-sterile bulbs and flowers
brenda
additional information
moderate expression throughout the plant
brenda
additional information
moderate expression throughout the plant
brenda
additional information
moderate expression throughout the plant
brenda
additional information
moderate expression throughout the plant
brenda
additional information
no expression in root or inflorescence
brenda
additional information
no expression in root or inflorescence
brenda
additional information
no expression in root or inflorescence
brenda
additional information
no expression in root or inflorescence
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the UGlcAE family, a subfamily of the the SDR enzyme superfamily. The only three family members are OcUGlcAE1, OcUGlcAE2, and OcUGlcAE3, isolated from Ornithogalum caudatum. Phylogenetic relationships of OcUGlcAE with other UGlcAE, UGE (UDP-D-glucose 4-epimerase) and UXE (UDP-D-xylose 4-epimerase) enzymes are analyzed
malfunction
deletion of the conversed GxxGxxG motif result in the activity loss of OcUGlcAE3
physiological function
additional information
physiological function
-
GAE delivers the main substrate for pectin biosynthesis
physiological function
-
GAE is necessary for Arabidopsis root hair growth
physiological function
UDP-D-glucuronic acid 4-epimerase OcUGlcAE3 is involved in the biosynthesis of root polysaccharides
additional information
the N-terminus of UGlcAEs plays important roles in their soluble expression and 4-epimerase activity
additional information
-
the N-terminus of UGlcAEs plays important roles in their soluble expression and 4-epimerase activity
Show AA Sequence and Transmembrane Helices (216 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42900
2 * 42900, recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
44100
2 * 44100, recombinant enzyme, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
44300
2 * 44300, recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
45500
2 * 45500, recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration
81400
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
88500
92200
recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
88500
recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration
88500
recombinant AtUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
2 * 44100, recombinant enzyme, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
dimer
2 * 45500, recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration
dimer
2 * 44300, recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA1-47
recombinant product ZmUGlcAE, lacking the putative transmembrane domain, converts UDP-glucuronic acid to UDP-alpha-D-galacturonic acid while control Escherichia coli cells containing empty vector have no enzyme activity
additional information
additional information
deletion of a putative transmembrane domain of 128 aa in the N-terminus, allowing the recombinant expression of a soluble enzyme. Deletion of the conversed GxxGxxG motif in turn results in the activity loss of OcUGlcAE3
additional information
-
deletion of a putative transmembrane domain of 128 aa in the N-terminus, allowing the recombinant expression of a soluble enzyme. Deletion of the conversed GxxGxxG motif in turn results in the activity loss of OcUGlcAE3
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-20
-20 - 65
the activity of ZmUGlcAE lacking the putative transmembrane domain is completely abolished when assays are conducted at pH value below 4 or above 10, or when the assay temperature is above 65°C
-20
recombinant enzyme is still fully active after 1 year in storage
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing of the crude extract in absence of cryoprotectants abolishes enzymatic activity entirely
KCl or NaCl, above 300 mM, completly inactivates the enzyme, when stored at -20°C for 2 weeks
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -80°C in 50% v/v glycerol, 7 days, enzyme retains approximately 80% of its activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using gel filtration and anion exchange chromatography
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
by using gel filtration and anion exchange chromatography
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
-
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Pichia pastoris
gene UGlcAE3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time quantitative PCR enzyme expression analysis, recombinant expression in Pichia pastoris strain GS115 in the microsomal fraction. The recombinant OcUGlcAE3 can form a microsomal protein by the N-terminal membrane anchor sequence, or can be secrete into the extracellular space through the guidance of the signal peptide. OcUGlcAE3 can be expressed in Escherichia coli strain Transetta (DE3) only as truncated enzyme with deletion of a putative transmembrane domain of 128 aa in the N-terminus
no recovery of active recombinant enzyme when full-length AtUGlcAE1 is expressed in Escherichia coli due to the hydrophobic domain that results in un- or misfolded protein in inclusion bodies within Escherichia coli. Recombinant AtUGlcAE1DELTA1-64, lacking the putative transmembrane domain, can be expressed in Escherichia coli
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, is expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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 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
Bolwell, G.P.; Dalessandro, G.; Northcote, D.H.
Decrease of polygalacturonic acid synthase during xylem differentiation in sycamore
Phytochemistry
24
699-702
1985
Acer pseudoplatanus
-
brenda
Maitra, U.S.; Gaunt, M.A.; Ankel, H.
The mechanism of uridine diphosphate sugar-4-epimerase reactions. Isotope discrimination with 4-tritiated substrates
J. Biol. Chem.
249
3075-3078
1974
Dolichospermum flos-aquae
brenda
Gaunt, M.A.; Maitra, U.S.; Ankel, H.
Uridine diphosphate galacturonate 4-epimerase from the blue-green alga Anabaena flos-aquae
J. Biol. Chem.
249
2366-2372
1974
Dolichospermum flos-aquae
brenda
Davidson, E.A.
UDP-D-galacturonic acid 4-epimerase from radish roots
Methods Enzymol.
8
276-277
1966
Raphanus sativus
-
brenda
Feingold, D.S.; Neufeld, E.F.; Hassid, W.Z.
The 4-epimerization and decarboxylation of uridine diphosphate D-glucuronic acid by extracts from Phaseolus aureus seedlings
J. Biol. Chem.
235
910-913
1960
Vigna radiata var. radiata
brenda
Munoz, R.; Lopez, R.; De Frutos, M.; Garcia, E.
First molecular characterization of a uridine diphosphate galacturonate 4-epimerase: an enzyme required for capsular biosynthesis in Streptococcus pneumoniae type 1
Mol. Microbiol.
31
703-713
1999
Streptococcus pneumoniae
brenda
Usadel, B.; Schluter, U.; Molhoj, M.; Gipmans, M.; Verma, R.; Kossmann, J.; Reiter, W.D.; Pauly, M.
Identification and characterization of a UDP-D-glucuronate 4-epimerase in Arabidopsis
FEBS Lett.
569
327-331
2004
Arabidopsis thaliana, Arabidopsis thaliana (Q9LIS3)
brenda
Molhoj, M.; Verma, R.; Reiter, W.D.
The biosynthesis of D-galacturonate in plants. functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis
Plant Physiol.
135
1221-1230
2004
Arabidopsis thaliana (O22141), Arabidopsis thaliana (Q67ZJ4), Arabidopsis thaliana (Q9M0B6), Arabidopsis thaliana (Q9STI6)
brenda
Gu, X.; Bar-Peled, M.
The biosynthesis of UDP-galacturonic acid in plants. Functional cloning and characterization of Arabidopsis UDP-D-glucuronic acid 4-epimerase
Plant Physiol.
136
4256-4264
2004
Arabidopsis thaliana (O22141)
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (O22141), Arabidopsis thaliana (O81312), Arabidopsis thaliana (Q9LIS3), Arabidopsis thaliana (Q9LPC1), Arabidopsis thaliana (Q9M0B6), Arabidopsis thaliana (Q9STI6)
brenda
Gu, X.; Wages, C.; Davis, K.; Guyett, P.; Bar-Peled, M.
Enzymatic characterization and comparison of various poaceae UDP-GlcA 4-epimerase isoforms
J. Biochem.
146
527-534
2009
Arabidopsis thaliana (O22141), Arabidopsis thaliana (Q9LIS3), Arabidopsis thaliana (Q9M0B6), Zea mays (Q304Y2), Zea mays, Oryza sativa (Q6K9M5), Oryza sativa
brenda
Pang, C.Y.; Wang, H.; Pang, Y.; Xu, C.; Jiao, Y.; Qin, Y.M.; Western, T.L.; Yu, S.X.; Zhu, Y.X.
Comparative proteomics indicates that biosynthesis of pectic precursors is important for cotton fiber and Arabidopsis root hair elongation
Mol. Cell. Proteomics
9
2019-2033
2010
Arabidopsis thaliana, Gossypium hirsutum
brenda
Wojtasik, W.; Kulma, A.; Kostyn, K.; Szopa, J.
The changes in pectin metabolism in flax infected with Fusarium
Plant Physiol. Biochem.
49
862-872
2011
Linum usitatissimum
brenda
Yin, S.; Sun, Y.J.; Liu, M.; Li, L.N.; Kong, J.Q.
cDNA isolation and functional characterization of UDP-D-glucuronic acid 4-epimerase family from Ornithogalum caudatum
Molecules
21
1505
2016
Albuca bracteata (A0A1J0KK43), Albuca bracteata
brenda
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