Information on EC 5.1.3.6 - UDP-glucuronate 4-epimerase

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

EC NUMBER
COMMENTARY hide
5.1.3.6
-
RECOMMENDED NAME
GeneOntology No.
UDP-glucuronate 4-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate = UDP-D-galacturonate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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L-ascorbate biosynthesis V
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Metabolic pathways
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UDP-alpha-D-galacturonate biosynthesis I (from UDP-D-glucuronate)
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ascorbate metabolism
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronate 4-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-17-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Xuzhou 142
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
type 1
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
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-galacturonate
show the reaction diagram
UDP-glucuronate
UDP-D-galacturonate
show the reaction diagram
UDPglucuronate
UDP-D-galacturonate
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-glucuronate
UDP-D-galacturonate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
GAE1 expressed in Pichia pastoris already contains tightly bound NAD+ or NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP-Ara
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2 mM, about 55% inhibition
KCl
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above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
p-hydroxymercuribenzoate
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reactivation by NAD+ and 2-mercaptoethanol
UDP-galactose
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UDP-Xyl
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2 mM, about 60% inhibition
UDP-xylose
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 0.72
UDP-D-glucuronate
0.19 - 0.426
UDP-glucuronate
0.037
UDPglucuronate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 37.4
UDP-glucuronate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0632 - 0.1436
UDP
0.0731 - 0.3051
UDP-xylose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.8
optimal pH in phosphate buffer for the activity of recombinant enzyme ZmUGlcAE1-47 lacking the transmembrane domain
7.4 - 7.6
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recombinant AtUGlcAE1DELTA1-64
8.5
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epimerization of UDPglucuronate to UDPgalacturonate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
the activity of ZmUGlcAE1-47 is completely abolished when assays are conducted at pH value below 4 or above 10
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
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pH 6.5: about 50% of maximal activity, pH 10.0: about 25% of maximal activity
7 - 10
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about 50% of maximal activity at pH 7 and 10, epimerization of UDPglucuronate to UDPgalacturonate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 42
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recombinant AtUGlcAE1DELTA1-64
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
Manually annotated by BRENDA team
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isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
Manually annotated by BRENDA team
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
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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2 * 40000, SDS-PAGE
42900
2 * 42900, recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
43500
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2 * 43500
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
54000
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gel filtration
80000
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gel filtration
81400
recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, determined by gel filtration
88000
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recombinant AtUGlcAE1DELTA1-64, gel filtration
88500
recombinant AtUGlcAE2, lacking the putative transmembrane domain at amino acid position 1-68, determined by gel filtration; recombinant AtUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
92200
recombinant OsUGlcAE3, lacking the putative transmembrane domain at amino acid position 1-53, determined by gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
recombinant enzyme is still fully active after 1 year in storage
-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 ZmUGlcAE lacking the putative transmembrane domain is stable (more than 6 months) when stored as a crude extract at 20°C
25
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60 min, about 35% loss of activity
30
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60 min, about 50% loss of activity
37
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60 min, about 75% loss of activity
42
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60 min, about 20% loss of activity
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
-10°C, stable for at least 1 year
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-20°C or -80°C in 50% v/v glycerol, 7 days, enzyme retains approximately 80% of its activity
-20°C, recombinant enzyme ZmUGlcAE lacking the putative transmembrane domain is stable (more than 6 months) when stored as a crude extract
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by using gel filtration and anion exchange chromatography
by using gel filtration and anion exchange chromatography; 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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens; expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expression in Pichia pastoris
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isoform GAE3 is expressed in Escherichia coli BL21(DE3) cells
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isoform GAE6 is expressed in Escherichia coli BL21(DE3) cells
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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
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overexpression in Escherichia coli
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recombinant ZmUGlcAE, lacking the putative transmembrane domain at amino acid position 1-47, is expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GAE mRNA level decreases after Fusarium oxysporum infection
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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