EC Number   |
General Information |
Reference |
|---|
   5.1.3.17 | evolution |
D-glucuronyl C5-epimerase activity and presence of L-iduronic acid seem to be intrinsic properties of cells from prokaryotes to humans |
749412 |
| 5.1.3.17 | malfunction |
complex deregulation of GLCE expression in prostatic diseases compared with healthy prostate tissue |
727266 |
| 5.1.3.17 | 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 |
727967 |
| 5.1.3.17 | metabolism |
D-glucuronyl C5-epimerase is a crucial modifying enzyme in the heparan sulfate biosynthesis pathway |
748202 |
| 5.1.3.17 | 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 |
714635 |
| 5.1.3.17 | metabolism |
the enzyme catalyzes a step in the heparan sulfate biosynthesis |
704486 |
| 5.1.3.17 | 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 |
727955 |
| 5.1.3.17 | more |
disaccharide analyses of chondroitin sulfate from enzyme wild-type and mutant strains, with or without additional mutation of heparan sulfate 2-O-sulfotransferase, overview |
727967 |
| 5.1.3.17 | more |
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 |
748202 |
| 5.1.3.17 | more |
the biphasic mode of C5-epi offers a mechanism to regulate the biosynthesis of heparan sulfate with the desired biological functions |
727904 |
