Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | 1 mM EDTA completely inactivates heparinase I in the presence of 2 mM Ca2+. Inhibition is reversible, the reintroduction of calcium ions into the system completely restores the enzymatic activity of heparinase I | Pedobacter heparinus | |
heparin with reduced carboxylate group | competitive inhibitor | Pedobacter heparinus | |
additional information | specific desulfation of the alpha-L-iduronic acid, 2-O-sulfate ring or the desulfation of the acid alpha-L-iduronic, 2-O-sulfate ring, followed by epimerization of its iduronic to galacturonic acid abolishes its degradation by heparinase I, as well as leading to the formation of competitive inhibitors | Pedobacter heparinus | |
Na+-heparin | - |
Pedobacter heparinus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required. Ca2+ is sequestered from the medium to achieve effective catalysis, and there is only very weak residual catalysis when Ca2+ ions are excluded from the medium | Pedobacter heparinus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pedobacter heparinus | - |
- |
- |
Pedobacter heparinus ATCC 13125 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
heparin | presence of Ca+ is required. Heparin-Na+ is not a substrate for heparinase I in the absence of Ca2+ ions. The binding of Ca2+ to the heparin substrate prior to enzymatic action determines the products of digestion, independently of the presence of Ca2+ in the digestion buffer | Pedobacter heparinus | ? | - |
? | |
heparin | presence of Ca+ is required. Heparin-Na+ is not a substrate for heparinase I in the absence of Ca2+ ions. The binding of Ca2+ to the heparin substrate prior to enzymatic action determines the products of digestion, independently of the presence of Ca2+ in the digestion buffer | Pedobacter heparinus ATCC 13125 | ? | - |
? | |
additional information | heparinase I specificity and efficiency depend on the cationic form of the substrate. Ca2+-heparin, in which a-L-iduronate-2-O-sulfate residues adopt 1C4 conformation preferentially, is a substrate, while Na+-heparin is an inhibitor. A model based on molecular dynamics and docking proposes that deprotonated residue His203 initiates beta-elimination by abstracting the C5 proton of the alpha-L-iduonate-2-O-sulfate residue in the substrate, and protonated Tyr357 provides the donor to the hexosamine leaving group | Pedobacter heparinus | ? | - |
? | |
additional information | heparinase I specificity and efficiency depend on the cationic form of the substrate. Ca2+-heparin, in which a-L-iduronate-2-O-sulfate residues adopt 1C4 conformation preferentially, is a substrate, while Na+-heparin is an inhibitor. A model based on molecular dynamics and docking proposes that deprotonated residue His203 initiates beta-elimination by abstracting the C5 proton of the alpha-L-iduonate-2-O-sulfate residue in the substrate, and protonated Tyr357 provides the donor to the hexosamine leaving group | Pedobacter heparinus ATCC 13125 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
heparinase I | - |
Pedobacter heparinus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.7 | - |
- |
Pedobacter heparinus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00008 | - |
heparin with reduced carboxylate group | pH not specified in the publication temperature not specified in the publication | Pedobacter heparinus |