4.2.2.7: heparin lyase
This is an abbreviated version!
For detailed information about heparin lyase, go to the full flat file.
Word Map on EC 4.2.2.7
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4.2.2.7
-
heparan
-
proteoglycans
-
glycosaminoglycans
-
chondroitinase
-
endothelial
-
chondroitin
-
oligosaccharide
-
disaccharide
-
anticoagulant
-
coagulation
-
flavobacterium
-
heparin-like
-
heparin-binding
-
antithrombin
-
dermatan
-
heparinum
-
protamine
-
clot
-
depolymerization
-
hyaluronic
-
hspgs
-
hyaluronidase
-
chlorate
-
lyases
-
n-sulfated
-
thromboplastin
-
glycocalyx
-
heparanase
-
iduronic
-
tetrasaccharide
-
thromboelastography
-
teg
-
atiii
-
anti-xa
-
6-o-sulfate
-
heparin-derived
-
o-sulfation
-
decasaccharide
-
analysis
-
thromboelastometry
-
lmwhs
-
heptose
-
enoxaparin
-
syndecan-4
-
tinzaparin
-
medicine
-
trisulfated
-
synthesis
-
heparinoids
-
kaolin
-
octasaccharide
-
polybrene
-
beta-vldl
- 4.2.2.7
- heparan
- proteoglycans
- glycosaminoglycans
- chondroitinase
- endothelial
- chondroitin
- oligosaccharide
- disaccharide
-
anticoagulant
-
coagulation
- flavobacterium
-
heparin-like
-
heparin-binding
- antithrombin
- dermatan
- heparinum
- protamine
- clot
-
depolymerization
-
hyaluronic
-
hspgs
- hyaluronidase
- chlorate
- lyases
-
n-sulfated
- thromboplastin
-
glycocalyx
- heparanase
-
iduronic
- tetrasaccharide
-
thromboelastography
- teg
-
atiii
-
anti-xa
-
6-o-sulfate
-
heparin-derived
-
o-sulfation
- decasaccharide
- analysis
-
thromboelastometry
- lmwhs
-
heptose
- enoxaparin
- syndecan-4
- tinzaparin
- medicine
-
trisulfated
- synthesis
-
heparinoids
- kaolin
- octasaccharide
- polybrene
-
beta-vldl
Reaction
Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends =
Synonyms
Hep III, HepA, heparin degrading enzyme, Heparin eliminase, heparin lyase, heparin lyase 1, heparin lyase I, heparin lyase II, Heparinase, heparinase I, heparinase II, heparitinase II, heparitinase III, HepI, HepII, HepP, HMPREF1016_02668, Lyase, heparin, PA14_23430, Pedsa_1818, PL12a
ECTree
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Metals Ions
Metals Ions on EC 4.2.2.7 - heparin lyase
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Ba2+
Ca2+
Co2+
Cu2+
Mg2+
Mn2+
NaCl
Ni2+
Zn2+
Ca2+
-
purified GST fusion enzyme requires Ca2+. Activity of the GST-heparinase I is stimulated 7fold by 1 mM Ca2+. Mg2+ and Mn2+ are much less effective at the same concentrations while Cu2+ and Zn2+ are ineffective
Ca2+
-
essential for activity, two calcium-binding sites with different affinity
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
Zn2+
-
bound within the central domain and plays an essential structural role in the stabilization of a loop forming one wall of the substrate-binding site