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Enzyme Nomenclature
Information on EC 5.1.3.6 - UDP-glucuronate 4-epimerase
for references in articles please use BRENDA:EC5.1.3.6
Word Map on EC 5.1.3.6
- 5.1.3.6
- polysaccharide
- udp-xylose
-
udp-galacturonic
- pectin
- udp-xyl
- ump
- seedlings
- pneumoniae
-
acid-containing
- nad+
-
4-epimerases
-
interconverts
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
5.1.3.6
-
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RECOMMENDED NAME
GeneOntology No.
UDP-glucuronate 4-epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate = UDP-D-galacturonate
-
-
-
-
UDP-glucuronate = UDP-D-galacturonate
formation of a 4-keto intermediate
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
epimerization
-
-
specific for C-4 of the glycuronosyl moiety
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
syncytia induced by nematode Heterodera schachtii
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
GAE is necessary for Arabidopsis root hair growth
physiological function
-
GAE delivers the main substrate for pectin biosynthesis
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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 SUBSTRATES
NATURAL PRODUCTS
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+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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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
0.2473
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; 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
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
assay at; recombinant AtUGlcAE2, lacking the amino acid position 1-68; recombinant AtUGlcAE2, lacking the amino acid position 1-68
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
-
isoform GAE3 is highly preferentially expressed in fast elongating fiber cells
additional information
-
enzyme activity decreases during the differentiation of cambial cells to xylem
-
enzyme activity decreases during the differentiation of cambial cells to xylem
expressed in root hair zone; expression of GAE4 is confined to root tips; GAE1 is expressed throughout the root; GAE2 is expressed throughout the root; GAE3 is expressed in root hair zone
-
differentiated and differentiating cells, enzyme activity decreases during the differentiation of cambial cells to xylem
-
differentiated and differentiating cells, enzyme activity decreases during the differentiation of cambial cells to xylem
additional information
moderate expression throughout the plant; moderate expression throughout the plant; moderate expression throughout the plant; no expression in root or inflorescence
additional information
moderate expression throughout the plant; moderate expression throughout the plant; moderate expression throughout the plant; no expression in root or inflorescence
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
exclusively localized in microsomal fraction, anchored to membrane
-
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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
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
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SUBUNITS
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; 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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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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
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
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 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
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 5.1.3.6)
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