Hyaluronan Lyase Protein, S. agActiae (His)

Hyaluronate lyase belongs to the polysaccharide lyase family and degrades acidic polysaccharides to generate unsaturated oligosaccharides through an elimination enzyme mechanism. Hyaluronate lyase is a prokaryotic elimination enzyme type of hyaluronidase, primarily derived from microorganisms such as bacteria, fungi, and bacteriophages. Most hyaluronate lyases cleave the β-1,4 glycosidic bonds of hyaluronic acid, chondroitin, and chondroitin sulfate via a β-elimination reaction. A few strains of this enzyme can act on both β-1,4 and β-1,3 glycosidic bonds simultaneously, producing different oligosaccharide products. Hyaluronate lyase specifically cleaves the β-D-GalNAc-(1→4)-β-D-GlcA glycosidic bond of hyaluronic acid, degrading it into specific unsaturated disaccharides and activating downstream reaction pathways. In bacteriophages, hyaluronate lyase binds to the bacterial cell particles and is not secreted, facilitating bacteriophage infection of streptococci and assisting streptococci in invading host tissues. Hyaluronate lyase is expressed in Streptococcus equi subsp. porcineus, where it helps the bacteria obtain nutrients and mediates pathogenicity. Hyaluronate lyase belongs to a different enzyme family than other types of hyaluronidase, exhibits low sequence homology, and shows significant differences in cleavage sites, catalytic mechanisms, and products^[1][2].

Hyaluronan Lyase (HylB) (0.05 mg/mL; 37 °C, different pH conditions) exhibits enzymatic activity for hyaluronan degradation, with the optimal activity at pH 6.5, and lower activity than HylD at pH 6.0 while higher activity at pH 7.5^[2].
Hyaluronan Lyase (inoculated on hyaluronic acid agar plates) mediates the degradation of hyaluronic acid, and its degradation ability is weaker than that of HylD from Streptococcus equi subsp. veterinary; it also regulates the expression of related metabolic genes, assisting the strain in using hyaluronic acid as a carbon source for growth^[2].