Polysaccharide lyase family 8, central domain <p>Proteins containing this central domain consist of a group of secreted bacterial lyase enzymes capable of acting on a variety of substrates. One such enzyme is hyaluronate lyase, a Streptococcal surface enzyme that degrades hyaluronan and chondroitin, thereby helping to spread the bacteria throughout host tissues [<cite idref="PUB00014309"/>]. Hyaluronate lyase (<db_xref db="EC" dbkey="4.2.2.1"/>) is a four-domain enzyme containing an N-terminal carbohydrate-binding domain, a spacer domain, a catalytic domain, and a C-terminal domain that modulates access to the catalytic cleft of the enzyme. The central domain has a beta-sandwich topology, with 18 strands in two sheets. Other bacterial enzymes that display this structure include the central domain of chondroitin AC lyase (<db_xref db="EC" dbkey="4.2.2.5"/>) [<cite idref="PUB00014311"/>], the central domain of xanthan lyase (<db_xref db="EC" dbkey="4.2.2.12"/>) [<cite idref="PUB00014314"/>], and the third domain of chondroitin ABC lyase (<db_xref db="EC" dbkey="4.2.2.4"/>) [<cite idref="PUB00014313"/>]. This entry represents these domains of hyaluronate lyase, chondroitin AC lyase, xanthan lyase and chondroitin ABC lyase. This domain if almost always associated with the polysaccharide lyase family 8 C-terminal domain (<db_xref db="INTERPRO" dbkey="IPR004103"/>).</p>