Table 1.
Enzyme class | Enzyme | Specificity |
---|---|---|
Heparinase | I | HNx6x(α1,4)-IdoA2S |
II | HNy6x(α1,4)-U2x | |
III | HNy6x(α1,4)-GlcA & HNAc(α1,4)-IdoA | |
Chondroitinase | AC | GalNAc4x6x(β1,4)-GlcA2x |
B | -GalNAc4x6x(β1,4)-IdoA2x- | |
ABC I | -GalNAc4x6x(β1,4)-U2x- | |
ABC II | GalNAc4x6x(β1,4)-U2x- | |
C | -GalNAc6x(β1,4)-GlcA- | |
Keratanase | I | HNAc6x-Gal(β1,4)-HNAc6x- |
II | HNAc6S(β1,3)-Gal6x-HNAc6S | |
Hyaluronate Lyase | -HNAc(β1,4)-GlcA- |
x Sulfated or unsubstituted; S Sulfated; y Acetylated or sulfated; Ac Acetylated; Gal Galactose; H Hexosamine; U Uronic acid of either the GlcA or IdoA epimer state. Heparinases I, II, and III are from Pedobacter heparinus. Chondroitinases AC, B, and C are also from Pedobacter heparinus. Hyaluronate lyases are available from a variety of sources including Peptostreptococcus, Staphylococcus, Streptococcus, and Apis mellifera, among others. Keratanases mediate the depolymerization of keratan sulfate and are not lyases, but rather hydrolases