KEGG   ENZYME: 5.1.3.17Help
Entry
EC 5.1.3.17                 Enzyme                                 

Name
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
Class
Isomerases;
Racemases and epimerases;
Acting on carbohydrates and derivatives
BRITE hierarchy
Sysname
poly[(1->4)-beta-D-glucuronosyl-(1->4)-N-sulfo-alpha-D-glucosaminyl] glucurono-5-epimerase
Reaction(IUBMB)
Epimerization of D-glucuronate in heparosan-N-sulfate to L-iduronate. [RN:R04389]
Reaction(KEGG)
Comment
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.
History
EC 5.1.3.17 created 1984, modified 2015
Pathway
Glycosaminoglycan biosynthesis - heparan sulfate / heparin
Metabolic pathways
Orthology
K01793  
heparosan-N-sulfate-glucuronate 5-epimerase
Genes
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)
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)
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)
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)
GFR: 
102034065(GLCE)
FAB: 
101818992(GLCE)
PHI: 
102113112(GLCE)
FPG: 
101915406(GLCE)
FCH: 
102054462(GLCE)
CLV: 
102093041(GLCE)
AAM: 
ASN: 
102386367(GLCE)
AMJ: 
102568999(GLCE)
PSS: 
102453691(GLCE)
CMY: 
102937568(GLCE)
CPIC: 
101943859(GLCE)
ACS: 
100556549(glce)
PBI: 
103064301(GLCE)
GJA: 
107116570(GLCE)
XLA: 
108712794(glce.S) 432242(glce.L)
XTR: 
100489303(glce)
NPR: 
108796035(GLCE)
DRE: 
100007670(glceb) 405776(glcea)
SRX: 
SANH: 
SGH: 
IPU: 
TRU: 
101074194(glce)
TNG: 
LCO: 
104920418(glce)
NCC: 
104944436(glce)
MZE: 
101468415(glce)
OLA: 
101168104(glce)
XMA: 
102220367(glce)
CSEM: 
103398539(glce)
LCF: 
108887864(glce)
SASA: 
ELS: 
105013975(glce)
SFM: 
108934585(glce)
LCM: 
102357523(GLCE)
CMK: 
103190379(glce)
BFO: 
CIN: 
SPU: 
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD10315(Dsim_GD10315)
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
BIM: 
BTER: 
SOC: 
AEC: 
ACEP: 
PBAR: 
HST: 
CFO: 
LHU: 
NVI: 
TCA: 
DPA: 
NVL: 
BMOR: 
DPL: 
PXY: 
API: 
DNX: 
PHU: 
DPX: 
ISC: 
TUT: 
CEL: 
CBR: 
CBG18086(Cbr-hse-5)
NAI: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
CRG: 
OBI: 
LAK: 
SMM: 
NVE: 
ADF: 
HMG: 
TAD: 
LAO: 
 » show all
Taxonomy
Reference
1  [PMID:107165]
  Authors
Backstrom G, Hook M, Lindahl U, Feingold DS, Malmstrom A, Roden L, Jacobsson I.
  Title
Biosynthesis of heparin. Assay and properties of the microsomal uronosyl C-5 epimerase.
  Journal
J. Biol. Chem. 254 (1979) 2975-82.
Reference
2  [PMID:6420398]
  Authors
Jacobsson I, Lindahl U, Jensen JW, Roden L, Prihar H, Feingold DS
  Title
Biosynthesis of heparin. Substrate specificity of heparosan N-sulfate D-glucuronosyl 5-epimerase.
  Journal
J. Biol. Chem. 259 (1984) 1056-63.
Reference
3  [PMID:10642607]
  Authors
Hagner-McWhirter A, Hannesson HH, Campbell P, Westley J, Roden L, Lindahl U, Li JP
  Title
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.
  Journal
Glycobiology. 10 (2000) 159-71.
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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