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Information on EC 5.1.3.6 - UDP-glucuronate 4-epimerase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M0B6

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.6 UDP-glucuronate 4-epimerase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9M0B6 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
uglcae, udpgle, atuglcae1, udp-glca 4-epimerase, udp-glucuronic acid 4-epimerase, udp-d-glucuronic acid 4-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-GlcA 4-epimerase3
-
UDP-glucuronic acid 4-epimerase
-
Epimerase, uridine diphosphoglucuronate
-
-
-
-
UDP glucuronic epimerase
-
-
-
-
UDP-D-galacturonic acid 4-epimerase
-
-
-
-
UDP-D-glucuronic acid 4-epimerase
-
-
UDP-galacturonate 4-epimerase
-
-
-
-
UDP-GlcA 4-epimerase
-
UDP-GlcA 4-epimerase1
-
UDP-GlcA 4-epimerase2
-
UDP-glucuronic acid 4-epimerase
-
Uridine diphospho-D-galacturonic acid 4-epimerase
-
-
-
-
Uridine diphosphoglucuronate epimerase
-
-
-
-
Uridine diphosphoglucuronic epimerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronate 4-epimerase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9024-17-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucuronate
UDP-D-galacturonate
show the reaction diagram
UDP-D-glucuronate
UDP-D-galacturonate
show the reaction diagram
UDP-glucuronate
UDP-D-galacturonate
show the reaction diagram
additional information
?
-
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
UDP-glucuronate
UDP-D-galacturonate
show the reaction diagram
-
-
-
r
UDP-glucuronate
UDP-D-galacturonate
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
NADP+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP-Ara
2 mM, about 55% inhibition
KCl
above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
NaCl
above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
UDP-Xyl
2 mM, about 60% inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 0.426
UDP-glucuronate
0.23 - 0.72
UDP-D-glucuronate
0.358
UDP-glucuronate
recombinant AtUGlcAE2, lacking the amino acid position 1-68, in 0.1 M sodium phosphate, pH 7.6
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
UDP-glucuronate
recombinant AtUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6
0.9 - 24
UDP-glucuronate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1107
UDP
recombinant AtUGlcAE3, position 1-53 is lacking
0.2473
UDP-xylose
recombinant AtUGlcAE3, position 1-53 is lacking
0.1341 - 0.1436
UDP
0.2972 - 0.3051
UDP-xylose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.6
recombinant AtUGlcAE1DELTA1-64
7.6
recombinant AtUGlcAE2, lacking the amino acid position 1-68
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
recombinant AtUGlcAE2, lacking the amino acid position 1-68
30 - 42
recombinant AtUGlcAE1DELTA1-64
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
only detected after pollen maturation
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
exclusively localized in microsomal fraction, anchored to membrane
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
GAE is necessary for Arabidopsis root hair growth
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GAE1_ARATH
429
2
47458
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44100
2 * 44100, recombinant enzyme, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
88500
recombinant AtUGlcAE3, 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
88000
recombinant AtUGlcAE1DELTA1-64, gel filtration
88500
recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 44100, recombinant enzyme, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
dimer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
recombinant enzyme is still fully active after 1 year in storage
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or -80°C in 50% v/v glycerol, 7 days, enzyme retains approximately 80% of its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using gel filtration and anion exchange chromatography
by using gel filtration and anion exchange chromatography
nickel-charged His-Bind column chromatography and Superdex 200 gel filtration
-
partial, AtUGlcAE1DELTA1-64 expressed in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Pichia pastoris
expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Pichia pastoris
isoform GAE6 is expressed in Escherichia coli BL21(DE3) cells
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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), Oryza sativa (Q6K9M5), Oryza sativa, Zea mays (Q304Y2), Zea mays
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team