EC Number   |
General Information |
Reference |
|---|
   4.2.2.7 | more |
free sulfohydryl groups of cysteine residues are necessary for catalytic activity of the enzyme |
-, 713782 |
| 4.2.2.7 | physiological function |
differential effects of heparitinase I, EC 4.2.2.8, and heparitinase III on endothelial tube formation. The enzymes inhibit tube formation and reduce tumor-derived neovascularization in vivo by reducing bFGF binding and subsequent signaling, HepIII has a stronger effect than Hep I. Heparitinases, isolated from Flavobacterium heparinum, cleave heparan sulfate chains at defined locations, Hep III cleaves near sulfated iduronic acid residues and at highly sulfated regions. Hep III therefore may disrupt the growth factor binding domains that are important for angiogenesis |
714027 |
| 4.2.2.7 | physiological function |
heparin and heparan sulfate contain a rare 3-O-sulfoglucosamine residue critical for anticoagulation and virus recognition, respectively. The glycosidic linkage proximate to this 3-O-sulfoglucosamine is resistant to cleavage by all heparin lyases |
715037 |
| 4.2.2.7 | physiological function |
HepP plays a crucial role in the pathogenesis of Pseudomonas aeruginosa PA14 during burn wound infection |
-, 747935 |
| 4.2.2.7 | physiological function |
mutation of hepP results in delay of pellicle formation at the air-liquid interface under static growth conditions. Biofilm formation by the mutant is also significantly reduced. In the Caenorhabditis elegans model of slow killing, mutation of hepP results in a significantly lower rate of killing than that of the parent wild-type strain |
-, 747419 |
