56177
Hyaluronate Lyase from Streptococcus pyogenes
≥8.0 units/mg protein (5.0-15.0 mg/mL)
Synonym(s):
Hyaluronidase from Streptococcus pyogenes
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
Recommended Products
recombinant
expressed in E. coli
form
liquid
specific activity
≥8.0 units/mg protein (5.0-15.0 mg/mL)
storage temp.
2-8°C
Biochem/physiol Actions
Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. It is important for the diffusion of toxins and proteins produced by S. pyogenes.
Unit Definition
1 U corresponds to the amount of enzyme which liberates 1 μmol unsaturated disaccharides per minute at pH 6.0 and 37°C from hyaluronic acid (Product No. 53747).
Physical form
ammonium sulfate suspension
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin III-binding site of porcine intestinal heparin.
Yamada, S., et al.
The Journal of Biological Chemistry, 4780-4787 (1993)
Renata K T Kobayashi et al.
Journal of microbiological methods, 68(3), 654-655 (2006-12-13)
The temperature-sensitive hemagglutinin (Tsh, 140 kDa) produced by Escherichia coli is cleaved into a fragment (106 kDa) containing mucinase activity, and an agglutinin fragment (33 kDa). By incorporating mucins into SDS-PAGE gels stained by Schiff's periodic acid, we could simultaneously
Parul Mishra et al.
The FEBS journal, 276(12), 3392-3402 (2009-05-15)
Hyaluronate lyases are a class of endoglycosaminidase enzymes with a high level of complexity and heterogeneity. The main function of the Streptococcus pyogenes bacteriophage protein hyaluronate lyase, HylP2, is to degrade hyaluronan into unsaturated disaccharide units. HylP2 was cloned, over-expressed
Clarise Rivera Starr et al.
Infection and immunity, 74(1), 40-48 (2005-12-22)
Group A streptococcus (GAS) depends on a hyaluronic acid (HA) capsule to evade phagocytosis and to interact with epithelial cells. Paradoxically, GAS also produces hyaluronidase (Hyl), an enzyme that cleaves HA. A common assumption is that Hyl digests structurally identical
Carlos Martinez-Fleites et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 65(Pt 10), 963-966 (2009-10-24)
The crystal structures of truncated forms of the Streptococcus pyogenes phage-encoded hyaluronate lyases HylP2 and HylP3 were determined by molecular replacement to 1.6 and 1.9 A resolution, respectively. The truncated forms crystallized in a hexagonal space group, forming a trimer
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