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Literature summary for 4.2.2.7 extracted from

  • Cordula, C.R.; Lima, M.A.; Shinjo, S.K.; Gesteira, T.F.; Pol-Fachin, L.; Coulson-Thomas, V.J.; Verli, H.; Yates, E.A.; Rudd, T.R.; Pinhal, M.A.; Toma, L.; Dietrich, C.P.; Nader, H.B.; Tersariol, I.L.
    On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2+ (2014), Mol. Biosyst., 10, 54-64.
    View publication on PubMed

Inhibitors

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

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

Organism UniProt Comment Textmining
Pedobacter heparinus
-
-
-
Pedobacter heparinus ATCC 13125
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
heparinase I
-
Pedobacter heparinus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
-
Pedobacter heparinus

Ki Value [mM]

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