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Information on EC 5.1.3.17 - heparosan-N-sulfate-glucuronate 5-epimerase
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EC Tree
5.1.3.17 heparosan-N-sulfate-glucuronate 5-epimeraseIUBMB Comments
The enzyme acts on D-glucosyluronate residues in N-sulfated heparosan polymers, converting them to L-iduronate, thus modifying the polymer to heparan-N-sulfate. The enzyme requires that at least the N-acetylglucosamine residue linked to C-4 of the substrate has been deacetylated and N-sulfated, and activity is highest with fully N-sulfated substrate. It does not act on glucuronate residues that are O-sulfated or are adjacent to N-acetylglucosamine residues that are O-sulfated at the 6 position. Thus the epimerization from D-glucuronate to L-iduronate occurs after N-sulfation of glucosamine residues but before O-sulfation. Not identical with EC 5.1.3.19 chondroitin-glucuronate 5-epimerase or with EC 5.1.3.36, heparosan-glucuronate 5-epimerase.
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Word Map
- 5.1.3.17
-
l-iduronic
-
d-glucuronic
-
epimerization
- proteoglycans
-
idoa
- glycosaminoglycans
-
glca
-
n-sulfated
-
2-o-sulfotransferase
-
hexuronic
-
hspgs
-
2-o-sulfation
- mastocytoma
-
mannuronan
-
lindahl
-
o-desulfated
- medicine
- diagnostics
- analysis
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
c5-epimerase, d-glucuronyl c5-epimerase, hsepi, glucuronyl c5-epimerase, c5-epi, hg-5epi, hs c5-epimerase, d-glucuronyl c-5 epimerase, heparosan n-sulfate d-glucuronosyl 5-epimerase, hnsg-5epi, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C5 uronosyl epimerase
-
-
-
-
C5-epi
C5-epimerase
D-Glucuronyl C-5 epimerase
-
-
-
-
D-glucuronyl C5-epimerase
Epimerase, polyglucuronate
-
-
-
-
Glce
glucuronyl C5-epimerase
Heparan sulfate C5-epimerase
Heparosan N-sulfate D-glucuronosyl 5-epimerase
-
-
-
-
Heparosan-N-sulfate-D-glucuronosyl-5-epimerase
-
-
-
-
HS C5-epimerase
Hsepi
D-glucuronyl C5-epimerase
Vibrio cholerae serotype O1 CO845
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate
-
-
-
-
heparosan-N-sulfate D-glucuronate = heparosan-N-sulfate L-iduronate
proposed catalytic mechanisms of C5-epi, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
poly[(1->4)-beta-D-glucuronosyl-(1->4)-N-sulfo-alpha-D-glucosaminyl] glucurono-5-epimerase
The enzyme acts on D-glucosyluronate residues in N-sulfated heparosan polymers, converting them to L-iduronate, thus modifying the polymer to heparan-N-sulfate. The enzyme requires that at least the N-acetylglucosamine residue linked to C-4 of the substrate has been deacetylated and N-sulfated, and activity is highest with fully N-sulfated substrate. It does not act on glucuronate residues that are O-sulfated or are adjacent to N-acetylglucosamine residues that are O-sulfated at the 6 position. Thus the epimerization from D-glucuronate to L-iduronate occurs after N-sulfation of glucosamine residues but before O-sulfation. Not identical with EC 5.1.3.19 chondroitin-glucuronate 5-epimerase or with EC 5.1.3.36, heparosan-glucuronate 5-epimerase.
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CAS REGISTRY NUMBER
COMMENTARY
112567-86-9
-
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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
GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Octa-4
i.e. epi-Octa-4
-
ir
GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Octa-3, two GlcA units in Octa-1 are susceptible to C5-epi modification, and both epimerization sites are reversible
i.e. epi-Octa-3
-
ir
GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Deca-8 with GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA(irreversible site)-beta-(1->4)-GlcNS-beta-(1->4)-GlcA (reversible site)-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
i.e. epi-Deca-8
-
?
GlcA-beta-(1->4)-GlcNH2-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-GlcNH2-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Octa-6
i.e. epi-Octa-6
-
r
GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Hexa-7
i.e. epi-Hexa-7
-
r
GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-beta-(1->4)-GlcNS-beta-(1->4)-L-IdoA-alpha-(1->4)-GlcNS-beta-(1->4)-L-IdoA-alpha-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Octa-1, two GlcA units in Octa-1 are susceptible to C5-epi modification, and both epimerization sites are reversible
i.e. epi-Octa-1
-
r
GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
GlcA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNS-beta-(1->4)-IdoA-beta-(1->4)-GlcNS-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol
-
i.e. Octa-2
i.e. epi-Octa-2
-
r
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
heparosan N-sulfate prepared by metabolic labeling of a capsular polysaccharide from E. coli K5 and subsequent chemical partial N-deacetylation and N-sulfation. Approximately 30% of the D-glucuronyl residues located between two N-sulfated glucosamine units are converted to L-iduronyl units
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
C5-epimerization is irreversible in vivo
-
-
ir
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
development of a coupled assay method using the enzyme and a 2-O-sulfotransferase mutant 2OST Y94I, overview
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
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a D-glucuronosyl residue is recognized as a substrate if it is linked at C-1 to an N-acetyl glucosamine residue and at C-4 to a N-sulfated unit. Large substrates are preferred
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
the enzyme controle heparan sulfate chain flexibility, its activity, modifiying the substrate, is required for proper lymphoid organ development, overview
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
the enzyme controle heparan sulfate chain flexibility, its activity, modifiying the substrate, is required for proper lymphoid organ development, overview
-
-
?
additional information
?
-
-
enzyme catalyzes formation of L-iduronic acid residues in the course of heparin biosynthesis
-
-
?
additional information
?
-
-
enzyme is involved in the biosynthesis of heparan sulfate in liver
-
-
?
additional information
?
-
-
key heparan sulfate modifying enzyme, a biosynthetic step that enhances biological activity of heparan sulfate. The enzyme is an important determinant of dorso-ventral axis formation and patterning in zebrafish
-
-
?
additional information
?
-
heparin hexasaccharide is product of Glce following O-sulfation, structure of the Glce dimer in complex with heparin hexasaccharide, detailed overview
-
-
?
additional information
?
-
-
limiting factor in dermatan sulfate biosynthesis
-
?
additional information
?
-
the D-glucuronyl C5-epimerase gene is transcriptionally activated through the beta-catenin-TCF4 pathway
-
-
?
additional information
?
-
-
the D-glucuronyl C5-epimerase gene is transcriptionally activated through the beta-catenin-TCF4 pathway
-
-
?
additional information
?
-
-
the enzyme is known for being a two-way catalytic enzyme, displaying a reversible catalytic mode by converting a glucuronic acid to an iduronic acid residue, and vice versa. The enzyme can also serve as a one-way catalyst to convert a glucuronic acid to an iduronic acid residue, displaying an irreversible catalytic mode. The reversible or irreversible catalytic mode strictly depends on the saccharide substrate structures
-
-
?
additional information
?
-
-
oligosaccharides containing a nonreducing end GlcNS residue immediately adjacent to the EPS residue are reactive to the enzyme. In contrast, when the GlcNS is replaced with GlcNAc, the oligosaccharide is no longer a substrate of the enzyme, substrate specificity, overview. No activity with GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-GlcNAc-beta-(1->4)-GlcA-beta-(1->4)-2,5-andydro-D-mannitol. Determination of epimerization sites in different substrates and reaction reversibility using D2O and tandem mass spectrometry, critical role of N-sulfated glucosamine at the nonreducing end of the epimerization site
-
-
?
additional information
?
-
development and evaluation of a rapid, nonradioactive assay for measuring heparan sulfate C-5 epimerase activity using hydrogen/deuterium exchange-mass spectrometry, overview. The method involves the following steps: H/D exchange upon epimerization of the substrate with HS C5-epimerase, low-pH nitrous acid treatment of the substrate, the separation of low-pH nitrous acid-cleaved disaccharides using HPLC, and mass spectrometry analysis
-
-
?
additional information
?
-
-
development and evaluation of a rapid, nonradioactive assay for measuring heparan sulfate C-5 epimerase activity using hydrogen/deuterium exchange-mass spectrometry, overview. The method involves the following steps: H/D exchange upon epimerization of the substrate with HS C5-epimerase, low-pH nitrous acid treatment of the substrate, the separation of low-pH nitrous acid-cleaved disaccharides using HPLC, and mass spectrometry analysis
-
-
?
additional information
?
-
recombinant enzyme HG-5epi, expressed in insect cells, epimerizes GlcA residues in heparosan, but not in N-sulfated-heparosan. Conversion of IdoA to GlcA is also catalyzed by HG-5epi when completely desulfated N-acetylated heparin is used as the substrate, indicating a reversible reaction mechanism. At equilibrium of the epimerization, the proportion of IdoA in the reaction product reaches up to 30% of total hexuronic acid. The recombinant enzyme catalyzes the epimerization of non-sulfated heparosan, product identification by using a combination of anion-exchange HPLC and postcolumn fluorescent labeling system
-
-
?
additional information
?
-
-
recombinant enzyme HG-5epi, expressed in insect cells, epimerizes GlcA residues in heparosan, but not in N-sulfated-heparosan. Conversion of IdoA to GlcA is also catalyzed by HG-5epi when completely desulfated N-acetylated heparin is used as the substrate, indicating a reversible reaction mechanism. At equilibrium of the epimerization, the proportion of IdoA in the reaction product reaches up to 30% of total hexuronic acid. The recombinant enzyme catalyzes the epimerization of non-sulfated heparosan, product identification by using a combination of anion-exchange HPLC and postcolumn fluorescent labeling system
-
-
?
additional information
?
-
-
enzyme catalyzes formation of L-iduronic acid residues in the course of heparin biosynthesis
-
-
?
additional information
?
-
-
L-iduronosyl moieties are formed after N-sulfation but before O-sulfation
-
-
?
additional information
?
-
the enzyme is involved in the biosynthesis of heparin and heparan sulfate
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of heparin and heparan sulfate
-
?
additional information
?
-
-
analysis of N-sulfation and glycosylation patterns, as well as chain lengths of heparan sulfate samples from wild-type and mutant cells, overview
-
-
?
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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
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
C5-epimerization is irreversible in vivo
-
-
ir
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
the enzyme controle heparan sulfate chain flexibility, its activity, modifiying the substrate, is required for proper lymphoid organ development, overview
-
-
?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
-
the enzyme controle heparan sulfate chain flexibility, its activity, modifiying the substrate, is required for proper lymphoid organ development, overview
-
-
?
additional information
?
-
-
enzyme catalyzes formation of L-iduronic acid residues in the course of heparin biosynthesis
-
-
?
additional information
?
-
-
enzyme is involved in the biosynthesis of heparan sulfate in liver
-
-
?
additional information
?
-
-
key heparan sulfate modifying enzyme, a biosynthetic step that enhances biological activity of heparan sulfate. The enzyme is an important determinant of dorso-ventral axis formation and patterning in zebrafish
-
-
?
additional information
?
-
-
limiting factor in dermatan sulfate biosynthesis
-
?
additional information
?
-
the D-glucuronyl C5-epimerase gene is transcriptionally activated through the beta-catenin-TCF4 pathway
-
-
?
additional information
?
-
-
the D-glucuronyl C5-epimerase gene is transcriptionally activated through the beta-catenin-TCF4 pathway
-
-
?
additional information
?
-
-
the enzyme is known for being a two-way catalytic enzyme, displaying a reversible catalytic mode by converting a glucuronic acid to an iduronic acid residue, and vice versa. The enzyme can also serve as a one-way catalyst to convert a glucuronic acid to an iduronic acid residue, displaying an irreversible catalytic mode. The reversible or irreversible catalytic mode strictly depends on the saccharide substrate structures
-
-
?
additional information
?
-
-
enzyme catalyzes formation of L-iduronic acid residues in the course of heparin biosynthesis
-
-
?
additional information
?
-
-
L-iduronosyl moieties are formed after N-sulfation but before O-sulfation
-
-
?
additional information
?
-
the enzyme is involved in the biosynthesis of heparin and heparan sulfate
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of heparin and heparan sulfate
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heparin hexasaccharide
mechanism of product inhibition of the enzyme: 2-O- and 6-O-sulfation of heparan sulfate keeps the C5 carbon of L-iduronic acid away from the active-site tyrosine residues, binding structure, detailed overview
-
additional information
CHAPS and n-octyl beta-D-glucoside slightly inhibite the activity, the effect of Triton X-100 is negligible
-
additional information
-
CHAPS and n-octyl beta-D-glucoside slightly inhibite the activity, the effect of Triton X-100 is negligible
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Antiproliferative effect of D-glucuronyl C5-epimerase in human breast cancer cells.
Breast Neoplasms
The TCF4/?-catenin pathway and chromatin structure cooperate to regulate D-glucuronyl C5-epimerase expression in breast cancer.
Carcinogenesis
D-glucuronyl C5-epimerase cell type specifically affects angiogenesis pathway in different prostate cancer cells.
Carcinogenesis
GLCE rs3865014 (Val597Ile) polymorphism is associated with breast cancer susceptibility and triple-negative breast cancer in Siberian population.
Lung Neoplasms
D-glucuronyl C5-epimerase suppresses small-cell lung cancer cell proliferation in vitro and tumour growth in vivo.
Mastocytoma
Biosynthesis of heparin. Substrate specificity of heparosan N-sulfate D-glucuronosyl 5-epimerase.
Mastocytoma
Biosynthesis of heparin/heparan sulfate: kinetic studies of the glucuronyl C5-epimerase with N-sulfated derivatives of the Escherichia coli K5 capsular polysaccharide as substrates.
Neoplasms
D-glucuronyl C5-epimerase cell type specifically affects angiogenesis pathway in different prostate cancer cells.
Neoplasms
D-glucuronyl C5-epimerase suppresses small-cell lung cancer cell proliferation in vitro and tumour growth in vivo.
Neoplasms
miRNA-218 contributes to the regulation of D-glucuronyl C5-epimerase expression in normal and tumor breast tissues.
Prostatic Neoplasms
D-glucuronyl C5-epimerase cell type specifically affects angiogenesis pathway in different prostate cancer cells.
Prostatic Neoplasms
Heterogeneity of d-glucuronyl C5-epimerase expression and epigenetic regulation in prostate cancer.
Pulmonary Atelectasis
Glucuronyl C5-epimerase is crucial for epithelial cell maturation during embryonic lung development.
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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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
activity range, low activity below and above, recombinant FLAG-tagged enzyme mutant
6.1 - 7.9
-
pH 6.1: about 60% of maximal activity, pH 7.9: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
decreased GLCE expression is observed in 10% of benign prostate hyperplasia tissues and 53% of prostate tumors, and increased GLCE mRNA levels are detected in 49% of benign prostate hyperplasia tissues and 21% of tumors, intratumoral heterogeneity of GLCE protein levels both in benign prostate hyperplasia and prostate cancer cells, resulting in a mixed population of GLCE-expressing and nonexpressing epithelial cells in vivo
brenda
-
decreased GLCE expression is observed in 10% of benign prostate hyperplasia tissues and 53% of prostate tumors, and increased GLCE mRNA levels are detected in 49% of benign prostate hyperplasia tissues and 21% of tumors, intratumoral heterogeneity of GLCE protein levels both in benign prostate hyperplasia and prostate cancer cells, resulting in a mixed population of GLCE-expressing and nonexpressing epithelial cells in vivo
brenda
additional information
additional information
-
quantitative RT-PCR enzyme expression analysis in benign and malign prostate tissues, overview
brenda
additional information
cDNA transcriptional microarray analysis of normal (PNT2) and prostate cancer (LNCaP, PC3, DU145) cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
D-glucuronyl C5-epimerase activity and presence of L-iduronic acid seem to be intrinsic properties of cells from prokaryotes to humans
malfunction
metabolism
physiological function
additional information
malfunction
-
complex deregulation of GLCE expression in prostatic diseases compared with healthy prostate tissue
malfunction
-
homozygous enzyme mutant flies are viable and fertile with only minor morphological defects, including the formation of an ectopic crossvein in the wing, but they have a short lifespan. Loss of Hsepi results in a significant impairment of 2-O-sulfation and induces compensatory increases in N- and 6-O-sulfation. Simultaneous block of Hsepi glucuronyl C5-epimerase and heparan sulfate 6-O-sulfotransferase activity disrupted tracheoblast formation, a well established FGF-dependent process. The increase in 6-O-sulfation in Hsepi mutants is critical for the rescue of FGF signaling
metabolism
D-glucuronyl C5-epimerase is a key enzyme involved in the biosynthesis of heparan sulfate proteoglycans, which has an important role in cell-cell and cell-matrix interactions and signaling
metabolism
the enzyme is probably involved in bacterial capsular polysaccharide biosynthesis, it shows catalytic properties similar to murine heparan sulfate D-glucuronyl C5-epimerase. The biosynthesis of these complex polysaccharides involves complicated reactions that turn the simple glycosaminoglycan backbone into highly heterogeneous structures. One of the modification reactions is the epimerization of D-glucuronic acid to its C5-epimer L-iduronic acid, which is essential for the function of heparan sulfate
metabolism
D-glucuronyl C5-epimerase is a crucial modifying enzyme in the heparan sulfate biosynthesis pathway
physiological function
-
heparan sulfate modification by the enzyme is essential for controlling activity of molecules that are instructive for early lymphoid tissue morphogenesis, but may be dispensable in later developmental stages or for lymphocyte maturation and differentiation, overview
physiological function
D-glucuronyl C5-epimerase inhibits U2020 tumor xenograft growth in vivo, the enzyme affects lung cancer cell proliferation and tumor growth by inhibiting tumor angiogenesis and invasion/metastasis pathways
physiological function
-
during the biosynthesis of heparan sulfate, glucuronyl C5-epimerase catalyzes C5-epimerization of glucuronic acid, converting it to iduronic acid. C5-epimerization is required for normal heparan sulfate sulfation. Role of Hsepi in development, overview. Genetic interactions between the enzyme and HSPG core protein genes during wing margin formation
physiological function
-
heparansulfate proteoglycans play an important role in cell-cell and cell-matrix interactions and signaling, and one of the key enzymes in heparansulfate biosynthesis is D-glucuronyl C5-epimerase. The enzyme has a tumor suppressor function in breast and lung carcinogenesis
physiological function
D-glucuronyl C5-epimerase (GLCE) is one of the key heparan sulfate biosynthetic enzymes, responsible for the epimerization of D-glucuronic acid (GlcA) to L-iduronic acid (IdoA) in the heparan sulfate proteoglycans (HSPGs). IdoA presence increases a flexibility of HS chains and facilitates interaction of HSPGs with numerous extracellular and cell surface ligands including growth factors. The dynamic cooperation of proteoglycans, growth factor receptors, and integrins determines cell behavior, polarity, migration, differentiation, proliferation, and survival both in physiological and pathological conditions. D-glucuronyl C5-epimerase (GLCE) is involved in breast and lung carcinogenesis as a potential tumor suppressor gene, acting through inhibition of tumor angiogenesis and invasion/metastasis pathways. In prostate tumors, increased GLCE expression is associated with advanced disease, suggesting versatile effects of GLCE in different cancers, potential cancer-promoting effect of GLCE in prostate cancer and involvement of GLCE in carcinogenesis. GLCE up-regulation plus expression pattern of a panel of six genes, discriminating morphologically different prostate cancer cell sub-types, is suggested as a potential marker of aggressive prostate cancer
physiological function
heparan sulfate (HS) is a glycosaminoglycan present on the cell surface and in the extracellular matrix, which interacts with diverse signal molecules and is essential for many physiological processes including embryonic development, cell growth, inflammation, and blood coagulation. D-Glucuronyl C5-epimerase (Glce) is a crucial enzyme in HS synthesis, converting D-glucuronic acid to L-iduronic acid to increase HS flexibility. This modification of HS is important for protein ligand recognition
physiological function
heparin and heparan sulfate (HS) glycosaminoglycans have important roles in anticoagulation, human development, and human diseases. HS C5-epimerase, which catalyzes the reversible epimerization of GlcA to IdoA, is a crucial enzyme involved in the biosynthesis of heparin-related biomolecules
physiological function
iduronic acid (IdoA) is a critical component of heparan sulfate in its interaction with functional proteins. Heparosan-N-sulfate-glucuronate 5-epimerase (HNSG-5epi) converts D-glucuronic acid (GlcA) residues in N-sulfated heparosan (NS-heparosan), as an intermediate in heparan sulfate biosynthesis, to IdoA. HG-5epi (heparosan-glucuronate 5-epimerase) is involved in acharan sulfate biosynthesis possesia distinct substrate specificity in Achatina fulica
physiological function
the enzyme is involved in heparan sulfate biosynthesis
physiological function
-
heparan sulfate modification by the enzyme is essential for controlling activity of molecules that are instructive for early lymphoid tissue morphogenesis, but may be dispensable in later developmental stages or for lymphocyte maturation and differentiation, overview
-
additional information
-
disaccharide analyses of chondroitin sulfate from enzyme wild-type and mutant strains, with or without additional mutation of heparan sulfate 2-O-sulfotransferase, overview
additional information
-
the biphasic mode of C5-epi offers a mechanism to regulate the biosynthesis of heparan sulfate with the desired biological functions
additional information
-
the enzyme may be used as a potential model to study the functional role of intratumor cell heterogeneity in prostate cancer progression
additional information
enzyme structure-function relationship, active site structure and function, overview. Three tyrosine residues, Tyr468, Tyr528, and Tyr546, in the active site are crucial for the enzymatic activity
Show AA Sequence and Transmembrane Helices (1524 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51914
x * 51914, sequence calculation, x * 52000, recombinant enzyme, SDS-PAGE
52000
52000
x * 51914, sequence calculation, x * 52000, recombinant enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer or tetramer
x * 51914, sequence calculation, x * 52000, recombinant enzyme, SDS-PAGE
additional information
?
x * 68000, about, sequence calculation, x * 75000, recombinant FLAG-tagged enzyme mutant, SDS-PAGE
additional information
RED-C5-epimerase is present in a dimeric/tetrameric form, in approximately a 2:1 ratio, and appears to be in a dynamic equilibrium
additional information
-
RED-C5-epimerase is present in a dimeric/tetrameric form, in approximately a 2:1 ratio, and appears to be in a dynamic equilibrium
additional information
the enzyme forms a dimer with two catalytic sites, each at a positively charged cleft in C-terminal alpha-helical domains binding one negatively charged hexasaccharide
additional information
-
the human epimerase is a 617-amino acid protein that consists of three domains, cytoplasmic comprising residues Met1-Lys11, transmembrane with Thr12-Trp28, and catalytic domain formed by Asn29-Asn617
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the recombinant FLAG-tagged enzyme mutant is probably N-glycosylated. The enzyme contains four possible N-glycosylation sites
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in apo-form and in complex with heparin hexasaccharide, both in a stable dimer conformation, hanging drop vapour diffusion method, mixing of 0.001 ml of 15-20 mg/ml protein in in 20 mM Tris, pH 8.0, 200 mM ammonium acetate, 1 mM dithiothreitol, and 1 mM EDTA, with 0.001 ml of 16% w/v PEG 3350, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 2% v/v Tacsimate, pH 5.0 for the unlabeled enzyme and 16% w/v PEG 3350, 0.06 M citric acid, and 0.04 M Bis-Tris propane, pH 4.1, for the SeMet-labeled enzyme, a concentration of 5.0 mg/ml is used for the enzyme complex with heparin oligosaccharide at a molar ratio of 1:5, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.9-2.2 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H584A
site-directed mutagenesis, the mutant shows 80% reduced activity compared to wild-type
N585A
site-directed mutagenesis, the mutant shows 90% reduced activity compared to wild-type
R154A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to wild-type
R156A
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
R396A
site-directed mutagenesis, the mutant shows 90% reduced activity compared to wild-type
R531A
site-directed mutagenesis, the mutant shows about 90% reduced activity compared to wild-type
R543A
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y149F
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y177F
site-directed mutagenesis, the mutant shows 40% reduced activity compared to wild-type
Y179F
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
Y468A
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y468F
site-directed mutagenesis, the mutant shows 75% reduced activity compared to wild-type
Y482F
site-directed mutagenesis, the mutant shows 20% reduced activity compared to wild-type
Y528A
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y528F
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y546A
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y546F
site-directed mutagenesis, the mutant shows over 90% reduced activity compared to wild-type
Y146A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y162A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y210A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
additional information
-
construction of enzyme deficient strains ussing P-element transposase exscision mutagenesis, removal of the entire Hsepi coding sequence, generation of viable and fertile homozygous mutants for Hsepid12 and Hsepid13
additional information
high cell density fed-batch cultivation of recombinant Escherichia coli strains expressing 2-O-sulfotransferase and C5-epimerase at high level for the production of bioengineered heparin, method, overview. The first enzymatic step in this process uses heparan sulfate biosynthetic enzymes, 2-O-sulfotransferase (2-OST) and C5-epimerase (C5-epi), expressed as MBP-tagged proteins in Escherichia coli, to convert N-sulfo heparosan into an intermediate polysaccharide rich in -GlcNS(1->4)IdoA2S- sequences (where S is sulfo and IdoA is alpha-L-iduronic acid). This critical step in bioengineered heparin preparation relies on the use of recombinant arylsulfotransferase IV (AST-IV) to regenerate 3'-phospho adenosine-5'-phosphosulfate (PAPS) using p-nitrophenylsulfate as a sacrificial sulfur donor, one-pot reaction
additional information
generation of a soluble form of the enzyme HG-5epi by replacement of the transmembrane domain (N-terminal 33 amino acids) with the immunoglobulin Kappa signal sequence and a FLAG tag
additional information
-
generation of a soluble form of the enzyme HG-5epi by replacement of the transmembrane domain (N-terminal 33 amino acids) with the immunoglobulin Kappa signal sequence and a FLAG tag
additional information
-
generation of Glce null mutant mice, that show a strongly reduced size of the fetal spleen and a spectrum of defects in thymus and lymph node development ranging from dislocation to complete loss of the organ, overview. Transplantation of wild-type lymph nodes allows undisturbed lymphocyte maturation, phenotype, overview
additional information
-
generation of Hsepi null mutant mice showing a lethal phenotype with selective organ defects but remarkably little effect on other organ systems, phenotype, overview. Heparan sulfate produced by enzyme-deficient MEF cells is devoid of L-iduronic acid residues, but shows up-regulated N- and 6-O-sulfation compared with wild-type, Hsepi-/- MEF cells proliferate and migrate similarly to wild-type cells. Restricted proliferation and migration of Hsepi mutant cells in response to FGF2 stimulation
additional information
-
generation of Glce null mutant mice, that show a strongly reduced size of the fetal spleen and a spectrum of defects in thymus and lymph node development ranging from dislocation to complete loss of the organ, overview. Transplantation of wild-type lymph nodes allows undisturbed lymphocyte maturation, phenotype, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rossetta(DE3)/pWUR537 by cobalt affinity chromatography
recombinant His6-SUMO-tagged enzyme mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, tag cleavage, another step of nickel affinity chromatography, and gel filtration of the eluate
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into a baculovirus expression vector and expressed in Sf9 insect cells
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree, recombinant expression of soluble FLAG-tagged enzyme mutant lacking the transmembrane domain (N-terminal 33 amino acids) in insect cells using the baculovirus expression system
enzyme GLCE is ectopically re-expressed in morphologically different LNCaP and PC3 prostate cancer cells, quantitative real-time PCR enzyme expression analysis
gene glce, recombinant expression of enzyme mutant comprising residues Arg50-Asn585 as N-terminally His6-SUMO-tagged enzyme in Escherichia coli strain BL21(DE3), expression of N-terminally His6-SUMO-tagged SeMet-substituted Glce protein in Escherichia coli strain B834, expression of diverse enzyme point mutants
gene RED65_08024, design and synthesis of a synthetic based on hypothetical protein RED65_08024, codon optimized for the codon usage bias of Escherichia coli, expression of the recombinant His-tagged enzyme in Escherichia coli strain Rossetta(DE3)/pWUR537
recombinant MBP-tagged enzyme in Escherichia coli strain Rosetta-gami B (DE3), coexpression with 2-O-sulfotransferase
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the overall transcriptional activity of the main heparan sulfate biosynthesis-involved genes (EXT1, EXT2, NDST1, NDST2, GLCE, HS2ST1, HS3ST1, HS3ST2, HS6ST1, HS6ST2, SULF1, SULF2, HPSE) is decreased by 1.5-2fold in Grade II-III glioma (p < 0.01) and by 3fold in Grade IV glioma (glioblastoma multiforme, GBM) (p < 0.05), as compared with the para-tumourous tissue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
assay procedure for heparosan-N-sulfate-glucuronate 5-epimerase, which is based on the use of a two-phase system for liquid scintillation counting
diagnostics
GLCE upregulation plus expression pattern of a panel of six genes, discriminating morphologically different prostate cancer cell subtypes, is a potential marker of aggressive prostate cancer
medicine
synthesis
the enzyme, coexpressed with 2-O-sulfotransferase in bacteria, can be used for production of bioengineered heparin as a potential substitute for the animal-sourced anticoagulant drug
medicine
-
in 82-84% of human breast tumors there is either downregulation or loss of D-glucuronyl C5-epimerase mRNA expression and significant decrease of the protein content. In 77% of cases, GLCE expression is decreased also in the normal-appearing tissue surrounding the tumor node but the protein amount is comparable to normal breast tissue
medicine
the anti-tumour effects associated with ectopic GLCE re-expression suggest that it may be a potential tumour-suppressor gene and a possible target for lung cancer diagnosis and treatment
medicine
-
the enzyme is a candidate molecular marker for advanced prostate cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacobsson, I.; Lindahl, U.; Jensen, J.W.; Roden, L.; Prihar, H.; Feingold, D.S.
Biosynthesis of heparin. Substrate specificity of heparosan N-sulfate D-glucuronosyl 5-epimerase
J. Biol. Chem.
259
1056-1063
1984
Mus musculus
brenda
Jensen, J.W.; Roden, L.; Jacobsson, I.; Lindahl, U.; Prihar, H.; Feingold, D.S.
Biosynthesis of heparin. A new substrate for heparosan-N-sulfate-D-glucopyranosyluronate 5-epimerase
Carbohydr. Res.
117
241-253
1983
Bos taurus
-
brenda
Campbell, P.; Feingold, D.S.; Jensen, J.W.; Malmström, A.; Roden, L.
New assay for uronosyl 5-epimerase
Anal. Biochem.
131
146-152
1983
Bos taurus
brenda
Malmström, A.; Roden, L.; Feingold, D.S.; Jacobsson, I.; Bäckström, G.; Lindahl, U.
Biosynthesis of heparin. Partial purification of the uronosyl C-5 epimerase
J. Biol. Chem.
255
3878-3883
1980
Mus musculus
brenda
Campbell, P.; Hannesson, H.H.; Sandbäck, D.; Roden, L.; Lindahl, U.; Li, J.
Biosynthesis of heparin/heparan sulfate. Purification of the D-glucuronyl C-5 epimerase from bovine liver
J. Biol. Chem.
269
26953-26958
1994
Bos taurus
brenda
Li, J.; Hagner-McWhirter, A.; Kjellen, L.; Palgi, J.; Jalkanen, M.; Lindahl, U.
Biosynthesis of heparin/heparan sulfate. cDNA cloning and expression of D-glucuronyl C5-epimerase from bovine lung
J. Biol. Chem.
272
28158-28163
1997
Bos taurus (O18756), Bos taurus
brenda
Tiedemann, K.; Larsson, T.; Heinegard, D.; Malmstrom, A.
The glucuronyl C5-epimerase activity is the limiting factor in the dermatan sulfate biosynthesis
Arch. Biochem. Biophys.
391
65-71
2001
Homo sapiens
brenda
Li, J.P.; Gong, F.; El Darwish, K.; Jalkanen, M.; Lindahl, U.
Characterization of the D-glucuronyl C5-epimerase involved in the biosynthesis of heparin and heparan sulfate
J. Biol. Chem.
276
20069-20077
2001
Mus musculus (Q9EPS3), Mus musculus
brenda
Ghiselli, G.; Agrawal, A.
The human D-glucuronyl C5-epimerase gene is transcriptionally activated through the beta-catenin-TCF4 pathway
Biochem. J.
390
493-499
2005
Homo sapiens (O94923), Homo sapiens
brenda
Ghiselli, G.; Farber, S.A.
D-Glucuronyl C5-epimerase acts in dorso-ventral axis formation in zebrafish
BMC Dev. Biol.
5
19
2005
Danio rerio
brenda
Hagner-McWhirter, A.; Li, J.P.; Oscarson, S.; Lindahl, U.
Irreversible glucuronyl C5-epimerization in the biosynthesis of heparan sulfate
J. Biol. Chem.
279
14631-14638
2004
Homo sapiens
brenda
Lopes, C.C.; Toma, L.; Pinhal, M.A.; Porcionatto, M.A.; Sogayar, M.C.; Dietrich, C.P.; Nader, H.B.
EJ-ras oncogene transfection of endothelial cells upregulates the expression of syndecan-4 and downregulates heparan sulfate sulfotransferases and epimerase
Biochimie
88
1493-1504
2006
Oryctolagus cuniculus
brenda
Cadwallader, A.B.; Yost, H.J.
Combinatorial expression patterns of heparan sulfate sulfotransferases in zebrafish: III. 2-O-sulfotransferase and C5-epimerases
Dev. Dyn.
236
581-586
2007
Danio rerio (Q29RD8), Danio rerio (Q6TS32), Danio rerio
brenda
Feyerabend, T.B.; Li, J.; Lindahl, U.; Rodewald, H.
Heparan sulfate C5-epimerase is essential for heparin biosynthesis in mast cells
Nat. Chem. Biol.
2
195-196
2006
Mus musculus
brenda
Grigorieva, E.; Eshchenko, T.; Rykova, V.I.; Chernakov, A.; Zabarovsky, E.; Sidorov, S.V.
Decreased expression of human D-glucuronyl C5-epimerase in breast cancer
Int. J. Cancer
122
1172-1176
2008
Homo sapiens
brenda
Jia, J.; Maccarana, M.; Zhang, X.; Bespalov, M.; Lindahl, U.; Li, J.P.
Lack of L-iduronic acid in heparan sulfate affects interaction with growth factors and cell signaling
J. Biol. Chem.
284
15942-15950
2009
Mus musculus
brenda
Li, K.; Bethea, H.N.; Liu, J.
Using engineered 2-O-sulfotransferase to determine the activity of heparan sulfate C5-epimerase and its mutants
J. Biol. Chem.
285
11106-11113
2010
Homo sapiens
brenda
Reijmers, R.M.; Vondenhoff, M.F.; Roozendaal, R.; Kuil, A.; Li, J.P.; Spaargaren, M.; Pals, S.T.; Mebius, R.E.
Impaired lymphoid organ development in mice lacking the heparan sulfate modifying enzyme glucuronyl C5-epimerase
J. Immunol.
184
3656-3664
2010
Mus musculus, Mus musculus C57BL/6
brenda
Grigorieva, E.; Prudnikova, T.; Domanitskaya, N.; Mostovich, L.; Pavlova, T.; Kashuba, V.; Zabarovsky, E.
D-Glucuronyl C5-epimerase suppresses small-cell lung cancer cell proliferation in vitro and tumour growth in vivo
Br. J. Cancer
105
74-82
2011
Homo sapiens (O94923), Homo sapiens
brenda
Raedts, J.; Kengen, S.; Van Der Oost, J.
Occurrence of L-iduronic acid and putative D-glucuronyl C5-epimerases in prokaryotes
Glycoconj. J.
28
57-66
2011
Bacillus cereus, Bacteroides sp., Clostridium kluyveri, Escherichia coli, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanococcus voltae, Ruminococcus sp., Shigella boydii, Vibrio cholerae, Caldanaerobacter subterraneus subsp. tengcongensis, Methanothermobacter marburgensis, Thermococcus onnurineus, Photorhabdus laumondii subsp. laumondii, Candidatus Korarchaeum cryptofilum, Campylobacter hominis, Nautilia profundicola, Bermanella marisrubri, Photorhabdus asymbiotica, Methanocaldococcus fervens, Methanocaldococcus infernus, Methanocaldococcus vulcanius, Thermococcus sibiricus, Thermococcus barophilus, Candidatus Koribacter versatilis, Candidatus koribacter, Sanguibacter keddieii, Conexibacter woesei, Clostridium ljungdahlii, Vibrio cholerae serotype O1, Escherichia coli O112ab, Vibrio cholerae serotype O1 CO845, Clostridium ljungdahlii ATCC 49587, Bacteroides sp. 1_1_6, Vibrio cholerae VL426, Ruminococcus sp. 18P13, Candidatus Korarchaeum cryptofilum OPF8, Methanothermobacter thermautotrophicus DELTAH, Sanguibacter keddieii DSM 10542, Photorhabdus laumondii subsp. laumondii TTO1, Methanocaldococcus fervens AG86, Methanocaldococcus jannaschii DSM 2661, Bacillus cereus R309803, Thermococcus sibiricus MM 739, Methanococcus voltae A3, Conexibacter woesei DSM 14684, Campylobacter hominis ATCC BAA-381, Clostridium kluyveri NBRC 12016, Methanocaldococcus infernus ME, Nautilia profundicola AmH, Methanocaldococcus vulcanius M7, Bermanella marisrubri RED65, Thermococcus barophilus MP, Clostridium kluyveri DSM 555
brenda
Prudnikova, T.Y.; Soulitzis, N.; Kutsenko, O.S.; Mostovich, L.A.; Haraldson, K.; Ernberg, I.; Kashuba, V.I.; Spandidos, D.A.; Zabarovsky, E.R.; Grigorieva, E.V.
Heterogeneity of D-glucuronyl C5-epimerase expression and epigenetic regulation in prostate cancer
Cancer Med.
2
654-661
2013
Homo sapiens
brenda
Sheng, J.; Xu, Y.; Dulaney, S.B.; Huang, X.; Liu, J.
Uncovering biphasic catalytic mode of C5-epimerase in heparan sulfate biosynthesis
J. Biol. Chem.
287
20996-21002
2012
Homo sapiens
brenda
Raedts, J.; Lundgren, M.; Kengen, S.W.; Li, J.P.; van der Oost, J.
A novel bacterial enzyme with D-glucuronyl C5-epimerase activity
J. Biol. Chem.
288
24332-24339
2013
Bermanella marisrubri (Q1N097), Bermanella marisrubri
brenda
Dejima, K.; Takemura, M.; Nakato, E.; Peterson, J.; Hayashi, Y.; Kinoshita-Toyoda, A.; Toyoda, H.; Nakato, H.
Analysis of Drosophila glucuronyl C5-epimerase: implications for developmental roles of heparan sulfate sulfation compensation and 2-O-sulfated glucuronic acid
J. Biol. Chem.
288
34384-34393
2013
Drosophila melanogaster
brenda
Zhang, J.; Suflita, M.; Li, G.; Zhong, W.; Li, L.; Dordick, J.S.; Linhardt, R.J.; Zhang, F.
High cell density cultivation of recombinant Escherichia coli strains expressing 2-O-sulfotransferase and C5-epimerase for the production of bioengineered heparin
Appl. Biochem. Biotechnol.
175
2986-2995
2015
Homo sapiens (O94923)
brenda
Mochizuki, H.; Yamagishi, K.; Suzuki, K.; Kim, Y.S.; Kimata, K.
Heparosan-glucuronate 5-epimerase molecular cloning and characterization of a novel enzyme
Glycobiology
25
735-744
2015
Lissachatina fulica (O94923), Lissachatina fulica
brenda
Qin, Y.; Ke, J.; Gu, X.; Fang, J.; Wang, W.; Cong, Q.; Li, J.; Tan, J.; Brunzelle, J.S.; Zhang, C.; Jiang, Y.; Melcher, K.; Li, J.P.; Xu, H.E.; Ding, K.
Structural and functional study of D-glucuronyl C5-epimerase
J. Biol. Chem.
290
4620-4630
2015
Danio rerio (F1QR43)
brenda
Babu, P.; Victor, X.V.; Raman, K.; Kuberan, B.
A rapid, nonradioactive assay for measuring heparan sulfate C-5 epimerase activity using hydrogen/deuterium exchange-mass spectrometry
Methods Mol. Biol.
1229
209-219
2015
Homo sapiens (O94923), Homo sapiens
brenda
Rosenberg, E.; Prudnikova, T.; Zabarovsky, E.; Kashuba, V.; Grigorieva, E.
D-Glucuronyl C5-epimerase cell type specifically affects angiogenesis pathway in different prostate cancer cells
Tumor Biol.
35
3237-3245
2014
Homo sapiens (O94923)
brenda
Ushakov, V.; Tsidulko, A.; De La Bourdonnaye, G.; Kazanskaya, G.; Volkov, A.; Kiselev, R.; Kobozev, V.; Kostromskaya, D.; Gaytan, A.; Krivoshapkin, A.; Aidagulova, S.; Grigorieva, E.
Heparan sulfate biosynthetic system is inhibited in human glioma due to EXT1/2 and HS6ST1/2 down-regulation
Int. J. Mol. Sci.
18
2301
2017
Homo sapiens (O94923)
brenda
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