3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid 2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O more than 95% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid 2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399636 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid 2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-3-O-sulfate-6-O-sulfate + H2O 26% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid 2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-3-O-sulfate-6-O-sulfate - ? 399635 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid 2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O 85% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid 2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399637 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O 40% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399638 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O more than 95% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399639 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-3-O-sulfate + H2O 21% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-3-O-sulfate - ? 399640 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O 44% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399641 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O more than 95% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399642 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate + H2O 59% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate - ? 399643 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-3-O-sulfate + H2O 60% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-(beta-1,4)-GlcNAc-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-3-O-sulfate - ? 399644 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-2-O-sulfate-(beta-1,4)-GlcNAc-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O 30% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-O-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-IdoUA-2-O-sulfate-(beta-1,4)-GlcNAc-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399645 3.2.1.166 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate + H2O 56% cleavage Homo sapiens 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid-2-sulfate-(beta-1,4)-GlcN-2-N-sulfate-6-O-sulfate-(alpha-1,4)-GlcUA + GlcN-2-N-sulfate-6-O-sulfate - ? 399646 3.2.1.166 extracellular matrix + H2O - Homo sapiens ? - ? 416994 3.2.1.166 fondaparinux + H2O - Homo sapiens 2N-sulfo-6-O-sulfo-alpha-D-GlcN-(1->4)-beta-GlcA + a trisaccharide - ? 431856 3.2.1.166 fondaparinux + H2O a pentasaccharide substrate, heparanase is a retaining glycosidase, NMR spectroscopic analysis, overview Homo sapiens 2N-sulfo-6-O-sulfo-alpha-D-GlcN-(1->4)-beta-GlcA + a trisaccharide - ? 431856 3.2.1.166 fondaparinux + H2O - Homo sapiens ? - ? 431857 3.2.1.166 heparan sulfate + H2O - Burkholderia pseudomallei ? - ? 94461 3.2.1.166 heparan sulfate + H2O - Homo sapiens ? - ? 94461 3.2.1.166 heparan sulfate + H2O - Mus musculus ? - ? 94461 3.2.1.166 heparan sulfate + H2O heparanase is a strict endo-beta-glucuronidase with no exolytic glucuronidase activity. The enzyme only cleaves the glycosidic bond in the middle of the substrate. Heparan sulfate is a polysaccharide that has the disaccharide repeating unit of glucuronic acid or iduronic acid and glucosamine. Certain parts of heparan sulfate are occupied by the repeating disaccharide of -GlcA-GlcNAc-, known as the lowly sulfated domain. Other parts of HS are dominated by the highly sulfated disaccharide repeating unit of GlcA-GlcNS3S6S-IdoA2SGlcNS6S-, known as highly sulfated domain, overview Mammalia ? - ? 94461 3.2.1.166 heparan sulfate + H2O isolated from Escherichia coli K5 strain. heparanase is a strict endo-beta-glucuronidase with no exolytic glucuronidase activity. The enzyme only cleaves the glycosidic bond in the middle of the substrate. Second, heparanase not only cleaves the linkages of -GlcA-GlcNS6S-, but also degrades the linkage of -GlcA-GlcNAc6S. Third, the enzyme does not uniformly cleave the linkages of -GlcA-GlcNS6S-. Depending on the trisaccharide sequence at the nonreducing end of the nonasaccharide substrates, heparanase is able to choose to cleave the subsequent nonreducing end linkage of -GlcA-GlcNS6S- in the substrate or leave it intact. This unique observation suggests that heparanase displays two cleavage modes: consecutive cleavage and gapped cleavage. In the consecutive mode, heparanase cleaves the nonreducing trisaccharide at Step 1 digestion, and then cleaves the linkage between Residues 5 and 6 at Step 2 digestion. In the gapped cleavage, heparanase also cleaves the trisaccharide from the nonreducing end at Step 1 digestion, and then cleaves the linkage between Residues 7 and 9 Mammalia ? - ? 94461 3.2.1.166 heparan sulfate + H2O enzyme BpHep is specific for heparan sulfate Burkholderia pseudomallei ? - ? 94461 3.2.1.166 heparan sulfate + H2O enzyme HPSE catalyzes hydrolysis of internal GlcUA(beta1->4)GlcNS linkages in heparan sulfate, with net retention of anomeric configuration. HPSE breakdown of HS is not indiscriminate, but instead is restricted to a small subset of GlcUAs reflecting a requirement for specific N- and O-sulfation patterns on neighboring sugars Homo sapiens ? - ? 94461 3.2.1.166 heparan sulfate + H2O catalytic mechanism that involves two conserved acidic residues, a putative proton donor at Glu225 and a nucleophile at Glu343 Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 401121 3.2.1.166 heparan sulfate proteoglycan + H2O - Gallus gallus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O - Mus musculus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O - Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O - Rattus norvegicus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O - Bos taurus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O heparanase 1 has multiple physiologic functions in the epidermis. It plays an important role in epidermal differentiation, possibly by modulating the liberation of heparan sulfate bound (growth) factors. In the stratum corneum, the endoglycosidase activity of heparanase 1 might be indispensable and represent the first step in the desquamation process and in Langerhans cells, its catalytic activity is required for the trans-tissue migration of these cells Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O heparanase cleaves the heparan sulfate glycosaminoglycans from proteoglycan core proteins and degrades them to small oligosaccharides. Inside cells, the enzyme is important for the normal catabolism of heparan sulfate proteoglycans, generating glycosaminoglycan fragments that are then transported to lysosomes and completely degraded. When secreted, heparanase degrades basement membrane heparan sulfate glycosaminoglycans at sites of injury or inflammation, allowing extravasion of immune cells into nonvascular spaces and releasing factors that regulate cell proliferation and angiogenesis. At physiological pH the enzyme binds to the extracellular matrix of cell surface heparan sulfate proteolycan but is inactive. When the pH is lowered, which could occur at sites of inflammation or matrix damage, the bound enzyme becomes active and cleaves the heparan sulfate proteoglycan it is bound to Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O role for heparanase-1 in tissue morphogenesis, regeneration and repair during embryonic development and in the adult. Heparanase-1 may contribute to these processes by its effects on remodelling of extracellular matrix, cell migration, adhesion and proliferation. Heparanase-1 contributes to tumour growth by supporting cell survival under stress conditions Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O the heparanase enzyme may play a role in cell migration occurring both at the very early stages of embryogenesis and later on in morphogenesis of the cardiovascular and nervous systems Gallus gallus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O cleavage of the beta-1,4-glycosidic bond between a D-glucuronate and a D-glucosamine in heparan sulfate. Cleavage to short chains of 6000-8000 Da. 2-O-sulfate groups are not required for C1A heparanase to recognize and degrade the substrate Cricetulus griseus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O cleavage to 5000 Da oligosaccharides Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O heparan sulphate fragments generated are dependent on the pH of the reaction. at pH 6.5, both enzymes generate 9000 Da products, while at pH 5.5 the shorter 6000 Da glycosaminoglycans are produced Cricetulus griseus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O heparanase results in release of low-molecular-weight-labeled degradation fragments. The degradation products of heparan sulfate are 5- to 6fold smaller than intact HS side chains Nannospalax judaei heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O heparanase results in release of low-molecular-weight-labeled degradation fragments. The degradation products of heparan sulfate are 5- to 6fold smaller than intact HS side chains Nannospalax galili heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O HPSE may play a role in ovulation Bos taurus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O the average molecular mass of the degradation products is determined to be 20000–30000 Da Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O the enzyme is an endo-beta-D-glucuronidase producing glucuronic acid or an iduronic acid at the newly formed reducing terminus. Heparanase-1 cuts macromolecular heparin into fragments of 5000–20000 Da. Infrequent enzyme cleavage sites may be due to either the recognition of a single, unusual modification in the heparin/HS chains or the requirement of a specific extended carbohydrate sequence for the cleavage Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398904 3.2.1.166 heparan sulfate proteoglycan + H2O - Homo sapiens ? - ? 417086 3.2.1.166 heparan sulfate proteoglycan + H2O - Rattus norvegicus ? - ? 417086 3.2.1.166 heparan sulfate proteolycan + H2O - Cricetulus griseus heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 398905 3.2.1.166 heparan sulphate proteoglycan + H2O - Homo sapiens heparan sulfate fragment + truncated heparan sulfate proteoglycan - ? 401123 3.2.1.166 heparansulfate proteoglycan + H2O - Homo sapiens ? - ? 417087 3.2.1.166 heparin + H2O - Homo sapiens ? - ? 401124 3.2.1.166 heparin + H2O heparanase cleaves macromolecular heparin at multiple sites. Heparanase primarily cleaves target structures distinct from the antithrombin-binding sequence Homo sapiens ? - ? 401124 3.2.1.166 heparin octasaccharide + H2O cleavage of the single beta-D-glucuronidic linkage in a heparin-derived octasaccharide with high affinity for antithrombin Homo sapiens ? - ? 401126 3.2.1.166 heparin sulfate + H2O cleavage to 5000 Da oligosaccharides Homo sapiens ? - ? 401127 3.2.1.166 insulin-like growth factor 2 receptor + H2O - Homo sapiens ? - ? 417105 3.2.1.166 low density receptor-related protein-1 + H2O - Homo sapiens ? - ? 417223 3.2.1.166 methyl 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranosyl-(1,4)-beta-D-glucopyranuronosyl-(1,4)-2-deoxy-3,6-di-O-sulfo-2-(sulfoamino)-D-glucopyranosyl-(1,4)-2-O-sulfo-alpha-L-idopyranuronosyl-(1,4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranoside + H2O i.e. fondaparinux Homo sapiens 4-O-[2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranosyl]-D-glucopyranuronic acid + methyl 2-deoxy-3,6-di-O-sulfo-2-(sulfoamino)-D-glucopyranosyl-(1,4)-2-O-sulfo-alpha-L-idopyranuronosyl-(1,4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranoside - ? 409880 3.2.1.166 additional information a capsular polysaccharide from Escherichia coli K5, with the same (-GlcUA-(beta-1,4)-GlcNAc-(alpha-1,4)-)n structure as the unmodified backbone of heparan sulfate, resists heparanase degradation in its native state as well as after chemical N-deacetylation/N-sulfation or partial enzymatic C-5 epimerization of beta-D-GlcUA to alpha-L-idopyranuronic acid. By contrast, a chemically O-sulfated (but still N-acetylated) K5 derivative is susceptible to heparanase cleavage. O-Sulfate groups, but not N-sulfate or alpha-L-idopyranuronic acid residues are essential for substrate recognition by the heparanase. Selective O-desulfation of the heparin octasaccharide implicates a 2-O-sulfate group on a hexuronic acid residue located two monosaccharide units from the cleavage site, toward the reducing end Homo sapiens ? - ? 89 3.2.1.166 additional information endo-beta-D-glucuronidase activity of the heparanase is dependent on the size and high sulfation of the oligosaccharide substrates. The GlcN-2-N-sulfate residue on reducing side of the target GlcUA is an essential but not sufficient requirement. The GlcN-3-sulfate residue on the reducing side of the target GlcUA exhibits a promoting effect in a relatively low sulfated sequence but an inhibitory effect in a highly sulfated sequence. The 6-O-sulfated group on the nonreducing side GlcN residue of the target GlcUA is an important but not absolute requirement. A iduronic acid-2-sulfate residue located two sugar residues away from the target GlcUA residue toward the reducing side is not an absolute requirement Homo sapiens ? - ? 89 3.2.1.166 additional information the substrate that carries the repeating unit of IdoA2S-GlcNS is completely resistant to the heparanase digestion. The polysaccharide with repeating units of GlcA-GlcNAc6S is not a a substrate. No activity with heparosan Homo sapiens ? - ? 89 3.2.1.166 additional information the enzyme specifically cleaves the glycol-bond between D-glucuronic acid and N-sulfo glucosamine units leaving 4000-5000 Da stubs attached to the core protein Homo sapiens ? - ? 89 3.2.1.166 additional information heparanase is an endo-beta-glucuronidase that cleaves heparan sulfate and facilitates the passage of migrating cells through extra­cellular matrices, particularly basement membranes, as well as releasing heparan sulfate-bound growth factors from the extracellular matrices, whereby the released growth factors also aid wound heal­ing and angiogenesis Homo sapiens ? - ? 89 3.2.1.166 additional information heparanase is an endo-beta-glucuronidase that cleaves heparan sulfate side chains of proteoglycans in basement membranes and the extracellular matrix Homo sapiens ? - ? 89 3.2.1.166 additional information heparanase is an endo-glycosidase that cleaves the heparan sulfate polymers at a limited number of sites within the chain releasing smaller fragments of 10-20 sugar units from heparan sulfate proteoglycan complexes Homo sapiens ? - ? 89 3.2.1.166 additional information the enzyme is an endo-beta-glucuronidase that cleaves heparan sulfate proteoglycans in the extracellular matrix and basement membrane, releasing heparin/heparan sulfate oligosaccharides of appreciable size Homo sapiens ? - ? 89 3.2.1.166 additional information 6-O-sulfo heparosan and N-sulfo heparosan are resistant to cleavage by heparanase Homo sapiens ? - ? 89 3.2.1.166 additional information the enzyme hydrolyses the glycosidic bond between the (1->4)-alpha-GlcA and the 2-N-sulfo-3,6-di-O-sulfo-(1->4)-alpha-D-GlcN Homo sapiens ? - ? 89 3.2.1.166 additional information heparanase interacts with syndecans by virtue of the typical high affinity that exists between an enzyme and its substrate. This high affinity interaction directs rapid and efficient cellular uptake of the heparanase-syndecan complex Homo sapiens ? - ? 89 3.2.1.166 additional information heparanase, but not proheparanase, interacts directly with antithrombin in a non-covalent manner resulting in the activation of antithrombin. Complex formation and activity analysis, overview. The activation of Pro41Leu, Arg47Cys, Lys114Ala and Lys125Ala antithrombin mutants by heparanase is impaired Homo sapiens ? - ? 89 3.2.1.166 additional information activity assays using fluorescein isothiocyanate (FITC)-labeled glycosaminoglycans. NMR spectroscopic study of enzyme cleavage site specificity, overview Burkholderia pseudomallei ? - ? 89 3.2.1.166 additional information development of two heparanase activity assays to cover a whole range of applications, overview. The first is a fast and easy method based on commercial homogenous substrate, fondaparinux and usage of a fluorescent redox marker, resazurin. Resazurin reduction reaction at pH 5.5 and 45°C. The second method is a quantitative assay based on biotinylated heparan sulfate that uses an easier technique to immobilize the substrate in a 96-well plate via protamine sulfate. Biotinylated heparan sulfate is immobilized. The enzymatic assay is performed using chimeric recombinant heparanase at different concentrations. In sequence, the immobilized biotinylated heparan sulfate that is not digested by recombinant heparanase is bound to streptavidin conjugated with europium. Fluorescence is measured using a time-resolved fluorometer. Both methods have high sensitivity and can be used to detect heparanase activity Homo sapiens ? - ? 89 3.2.1.166 additional information fondaparinux assay method Homo sapiens ? - ? 89 3.2.1.166 additional information oligosaccharide complexes map the substrate-binding and sulfate recognition motifs. Analysis of the structural basis of HPSE substrate interactions, overview. HPSE interaction induces distortion of the substrate chain Homo sapiens ? - ? 89 3.2.1.166 sulfated PG545 + H2O - Homo sapiens ? - ? 432418 3.2.1.166 sulfated trisaccharide from PG545 + H2O - Homo sapiens ? - ? 432419 3.2.1.166 syndecan-1 + H2O - Homo sapiens ? - ? 393621 3.2.1.166 syndecan-1 + H2O heparanase promotes the activity of this mitogenic protein by removing the heparan sulfate chains from syndecan-1 leaving the deglycanated heparan sulfate proteoglycans as the active receptor for lacritin Homo sapiens ? - ? 393621 3.2.1.166 [GlcAbeta(1,4)GlcNSO3H-3SO3Halpha(1,4)]m-GlcAbeta(1,4)GlcNSO3H-3SO3Halpha(1,4)-[GlcAbeta(1,4)GlcNSO3H-3SO3H]n + H2O both N- and O-sulfations (either 6-O-sulfation or 3-O-sulfation) are required for the cleavage by heparanase. Structural moiety recognized by heparanase includes a GlcA unit and GlcNS unit carrying O-sulfations. The enzyme proves to be promiscuous in the aspect of the type and location of O-sulfation required for recognition Homo sapiens [GlcAbeta(1,4)GlcNSO3H-3SO3Halpha(1,4)]m-GlcA + GlcNSO3H-3SO3Halpha(1,4)-[GlcAbeta(1,4)GlcNSO3H-3SO3H]n - ? 410654 3.2.1.166 [GlcAbeta(1,4)GlcNSO3H-6SO3Halpha(1,4)]m-GlcAbeta(1,4)GlcNSO3H-6SO3Halpha(1,4)-[GlcAbeta(1,4)GlcNSO3H-6SO3H]n + H2O both N- and O-sulfations (either 6-O-sulfation or 3-O-sulfation) are required for the cleavage by heparanase. Structural moiety recognized by heparanase includes a GlcA unit and GlcNS unit carrying O-sulfations. The enzyme proves to be promiscuous in the aspect of the type and location of O-sulfation required for recognition Homo sapiens [GlcAbeta(1,4)GlcNSO3H-6SO3Halpha(1,4)]m-GlcA + GlcNSO3H-6SO3Halpha(1,4)-[GlcAbeta(1,4)GlcNSO3H-3SO3H]n - ? 410655 3.2.1.166 [GlcAbeta(1,4)GlcNSO3Halpha(1,4)]m-GlcAbeta(1,4)GlcNSO3Halpha(1,4)-[GlcAbeta(1,4)GlcNSO3H]n + H2O heparanase does not cleave the linkage of GlcA2S-GlcNS but rather cleaves the linkage of GlcA-GlcNS nearby Homo sapiens [GlcAbeta(1,4)-GlcNSO3Halpha(1,4)]m-GlcA + GlcNSO3Halpha(1,4)-[GlcAbeta(1,4)GlcNSO3H]n - ? 410656