Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase.

Polysaccharide lyase family 8, super-sandwich domain. This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.

Polysaccharide lyase family 8, N terminal alpha-helical domain. This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.

Polysaccharide lyase family 8, C-terminal beta-sandwich domain. This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

Structureof Paenibacillus xanthan lyase to 2.6 A resolution [Paenibacillus]

CrystalStructure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan [Bacillus sp. GL1],1J0N_A Crystal Structure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan [Bacillus sp. GL1]

Crystalstructure of xanthan lyase in complex with mannose [Bacillus sp. GL1]

ChainA, Xanthan lyase [Bacillus sp. GL1]

ChainA, xanthan lyase [Bacillus sp. GL1],1X1I_A Chain A, xanthan lyase [Bacillus sp. GL1],1X1J_A Chain A, xanthan lyase [Bacillus sp. GL1]

Xanthan lyase OS=Bacillus sp. (strain GL1) OX=84635 GN=xly PE=1 SV=1

Hyaluronate lyase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=SP_0314 PE=1 SV=2

Hyaluronate lyase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=hysA PE=3 SV=1

Hyaluronate lyase OS=Streptococcus agalactiae serotype III (strain NEM316) OX=211110 GN=hylB PE=1 SV=2

Hyaluronate lyase OS=Cutibacterium acnes (strain DSM 16379 / KPA171202) OX=267747 GN=PPA0380 PE=3 SV=1