EC                 Enzyme                                 

heparosan-N-sulfate-glucuronate 5-epimerase;
heparosan epimerase;
heparosan-N-sulfate-D-glucuronosyl 5-epimerase;
C-5 uronosyl epimerase;
polyglucuronate epimerase;
D-glucuronyl C-5 epimerase;
poly[(1,4)-beta-D-glucuronosyl-(1,4)-N-sulfo-alpha-D-glucosaminyl] glucurono-5-epimerase
Racemases and epimerases;
Acting on carbohydrates and derivatives
BRITE hierarchy
poly[(1->4)-beta-D-glucuronosyl-(1->4)-N-sulfo-alpha-D-glucosaminyl] glucurono-5-epimerase
Epimerization of D-glucuronate in heparosan-N-sulfate to L-iduronate. [RN:R04389]
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 chondroitin-glucuronate 5-epimerase or with EC, heparosan-glucuronate 5-epimerase.
EC created 1984, modified 2015
ec00534  Glycosaminoglycan biosynthesis - heparan sulfate / heparin
ec01100  Metabolic pathways
K01793  heparosan-N-sulfate-glucuronate 5-epimerase
HSA: 26035(GLCE)
PTR: 453542(GLCE)
PPS: 100975106(GLCE)
GGO: 101148037(GLCE)
PON: 100457760(GLCE)
NLE: 100592444(GLCE)
MCC: 694999(GLCE)
MCF: 102130661(GLCE)
CSAB: 103245410(GLCE)
RRO: 104662604(GLCE)
RBB: 108514748(GLCE)
CJC: 100402503(GLCE)
SBQ: 101034113(GLCE)
MMU: 93683(Glce)
RNO: 363073(Glce)
CGE: 100754874(Glce)
NGI: 103736825(Glce)
HGL: 101703064(Glce)
CCAN: 109698168(Glce)
OCU: 100341828(GLCE)
TUP: 102502937(GLCE)
CFA: 487622(GLCE)
AML: 100478227(GLCE)
UMR: 103679039(GLCE)
ORO: 101386831(GLCE)
FCA: 101095983(GLCE)
PTG: 102952073(GLCE)
AJU: 106980561(GLCE)
BTA: 281195(GLCE)
BOM: 102274550(GLCE)
BIU: 109564721(GLCE)
PHD: 102324957(GLCE)
CHX: 102172900(GLCE)
OAS: 101106592(GLCE)
SSC: 100154444(GLCE)
CFR: 102504983(GLCE)
CDK: 105087308(GLCE)
BACU: 103008441(GLCE)
LVE: 103080354(GLCE)
OOR: 101271197(GLCE)
ECB: 100052581(GLCE)
EPZ: 103543875(GLCE)
EAI: 106835661(GLCE)
MYB: 102262970(GLCE)
MYD: 102752823(GLCE)
HAI: 109385253(GLCE)
RSS: 109444334(GLCE)
PALE: 102891481(GLCE)
LAV: 100673589(GLCE)
TMU: 101347909
MDO: 100019166(GLCE)
SHR: 100925822(GLCE)
OAA: 100085653(GLCE)
GGA: 415566(GLCE)
MGP: 100546915(GLCE)
CJO: 107318962(GLCE)
APLA: 101789857(GLCE)
ACYG: 106043673(GLCE)
TGU: 100230821(GLCE)
SCAN: 103816259(GLCE)
GFR: 102034065(GLCE)
FAB: 101818992(GLCE)
PHI: 102113112(GLCE)
PMAJ: 107209523(GLCE)
CCAE: 111933852(GLCE)
FPG: 101915406(GLCE)
FCH: 102054462(GLCE)
CLV: 102093041(GLCE)
EGZ: 104133817(GLCE)
NNI: 104017037(GLCE)
ACUN: 113484044(GLCE)
AAM: 106495389
ASN: 102386367(GLCE)
AMJ: 102568999(GLCE)
PSS: 102453691(GLCE)
CMY: 102937568(GLCE)
CPIC: 101943859(GLCE)
ACS: 100556549(glce)
PVT: 110086904(GLCE)
PBI: 103064301(GLCE)
PMUR: 107283920(GLCE)
GJA: 107116570(GLCE)
XLA: 108712794(glce.S) 432242(glce.L)
XTR: 100489303(glce)
NPR: 108796035(GLCE)
DRE: 100007670(glceb) 405776(glcea)
IPU: 108259276(Glce) 108274589
TRU: 101074194(glce)
LCO: 104920418(glce)
NCC: 104944436(glce)
MZE: 101468415(glce)
OLA: 101168104(glce)
XMA: 102220367(glce)
PRET: 103462118(glce)
NFU: 107381748(glce)
KMR: 108234798(glce)
CSEM: 103398539(glce)
LCF: 108887864(glce)
SDU: 111223714(glce)
HCQ: 109514358(glce)
BPEC: 110174517(glce)
MALB: 109963362(glce)
OTW: 112238029
SALP: 111980622(glce)
ELS: 105013975(glce)
SFM: 108934585(glce)
PKI: 111845625(glce)
LCM: 102357523(GLCE)
CMK: 103190379(glce)
SPU: 575562
APLC: 110979098
SKO: 100370244
DME: Dmel_CG3194(Hsepi)
DER: 6541647
DPE: 6591115
DSI: Dsimw501_GD10315(Dsim_GD10315)
DWI: 6652210
MDE: 101895364
AAG: 5565650
AME: 410118
BIM: 100746913
BTER: 100648289
SOC: 105205016
MPHA: 105839326
AEC: 105152283
ACEP: 105621248
PBAR: 105428344
HST: 105180547
DQU: 106743638
CFO: 105252887
LHU: 105667459
PGC: 109856517
OBO: 105275234
PCF: 106785179
NVI: 100123867
MDL: 103572179
TCA: 663342
DPA: 109539260
NVL: 108565207
BMOR: 101736603
PRAP: 110999574
HAW: 110374867
TNL: 113504444
PXY: 105382951
API: 100164972
DNX: 107166129
CLEC: 106670169
ZNE: 110840150
FCD: 110862144
DPTE: 113793709
CEL: CELE_B0285.5(hse-5)
CBR: CBG18086(Cbr-hse-5)
BMY: Bm1_18165
TSP: Tsp_05727
MYI: 110455274
OBI: 106876518
SHX: MS3_00809
EGL: EGR_02731
EPA: 110241410
ADF: 107346476
PDAM: 113672224
SPIS: 111329368
HMG: 100207938
 » show all
1  [PMID:107165]
Backstrom G, Hook M, Lindahl U, Feingold DS, Malmstrom A, Roden L, Jacobsson I.
Biosynthesis of heparin. Assay and properties of the microsomal uronosyl C-5 epimerase.
J Biol Chem 254:2975-82 (1979)
2  [PMID:6420398]
Jacobsson I, Lindahl U, Jensen JW, Roden L, Prihar H, Feingold DS
Biosynthesis of heparin. Substrate specificity of heparosan N-sulfate D-glucuronosyl 5-epimerase.
J Biol Chem 259:1056-63 (1984)
3  [PMID:10642607]
Hagner-McWhirter A, Hannesson HH, Campbell P, Westley J, Roden L, Lindahl U, Li JP
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.
Glycobiology 10:159-71 (2000)
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 112567-86-9

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