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Information on EC 5.1.3.17 - heparosan-N-sulfate-glucuronate 5-epimerase and Organism(s) Mus musculus and UniProt Accession Q9EPS3
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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
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l-iduronic
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d-glucuronic
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epimerization
- proteoglycans
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idoa
- glycosaminoglycans
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glca
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n-sulfated
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2-o-sulfotransferase
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hexuronic
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hspgs
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2-o-sulfation
- mastocytoma
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mannuronan
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lindahl
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o-desulfated
- medicine
- diagnostics
- analysis
- synthesis
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
c5-epimerase, hsepi, d-glucuronyl c5-epimerase, glucuronyl c5-epimerase, c5-epi, hg-5epi, hs c5-epimerase, d-glucuronyl c-5 epimerase, heparosan n-sulfate d-glucuronosyl 5-epimerase, hnsg-5epi, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C5 uronosyl epimerase
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-
-
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D-Glucuronyl C-5 epimerase
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-
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Epimerase, polyglucuronate
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Heparosan N-sulfate D-glucuronosyl 5-epimerase
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Heparosan-N-sulfate-D-glucuronosyl-5-epimerase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
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-
-
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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.
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
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
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-
-
-
?
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
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?
Heparosan-N-sulfate D-glucuronate
Heparosan-N-sulfate L-iduronate
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the enzyme controle heparan sulfate chain flexibility, its activity, modifiying the substrate, is required for proper lymphoid organ development, overview
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?
additional information
?
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the enzyme is involved in the biosynthesis of heparin and heparan sulfate
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?
additional information
?
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the enzyme is involved in the biosynthesis of heparin and heparan sulfate
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?
additional information
?
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enzyme catalyzes formation of L-iduronic acid residues in the course of heparin biosynthesis
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?
additional information
?
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L-iduronosyl moieties are formed after N-sulfation but before O-sulfation
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-
?
additional information
?
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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
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the enzyme controle heparan sulfate chain flexibility, its activity, modifiying the substrate, is required for proper lymphoid organ development, overview
-
-
?
additional information
?
-
the enzyme is involved in the biosynthesis of heparin and heparan sulfate
-
?
additional information
?
-
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the enzyme is involved in the biosynthesis of heparin and heparan sulfate
-
?
additional information
?
-
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enzyme catalyzes formation of L-iduronic acid residues in the course of heparin biosynthesis
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?
additional information
?
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L-iduronosyl moieties are formed after N-sulfation but before O-sulfation
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLCE_MOUSE
618
1
70089
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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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
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Malmstrm, A.; Roden, L.; Feingold, D.S.; Jacobsson, I.; Bckstrm, G.; Lindahl, U.
Biosynthesis of heparin. Partial purification of the uronosyl C-5 epimerase
J. Biol. Chem.
255
3878-3883
1980
Mus musculus
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
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
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
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
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