Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site.
A synthetic pentasaccharide, containing an intact antithrombin III (ATIII) binding site that is in clinical studies a specific antifactor Xa agent, serves as a substrate for a heparin lyase (heparinase I, EC 4.2.2.7) from Flavobacterium heparinum. Heparinase I, currently being assessed as a heparin reversal agent, also reverses the antifactor Xa activity of this synthetic pentasaccharide by breaking it down to inactive disaccharide and trisaccharide products.
Yu
G
G
Division of Medicinal and Natural Products Chemistry, University of Iowa, Iowa City, IA 52242, USA.
LeBrun
L
L
Gunay
N S
NS
Hoppensteadt
D
D
Walenga
J M
JM
Fareed
J
J
Linhardt
R J
RJ
D000990:Antithrombin III / Q000737:chemistry; D001665:Binding Sites; D002240:Carbohydrate Sequence; D004305:Dose-Response Relationship, Drug; D065427:Factor Xa Inhibitors; D005417:Flavobacterium / Q000201:enzymology; D006493:Heparin / Q000737:chemistry / Q000378:metabolism*; D019763:Heparin Lyase / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry
D065427:Factor Xa Inhibitors; D009844:Oligosaccharides; D015842:Serine Proteinase Inhibitors; C049714:IC 831423; D000990:Antithrombin III; D006493:Heparin; D019763:Heparin Lyase