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InterPro: IPR008929 Chondroitin AC/alginate lyase

Protein matchesHelp
UniProtKB
Matches:
790 proteins
AccessionHelp IPR008929 Chondroitin_lyas
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR012329 Polysaccharide lyase family 8, N-terminal
Found in IPR006934 Baculovirus occlusion-derived virus envelope, E66
IPR008397 Alginate lyase
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Glycosaminoglycans (GAGs) are highly negatively charged polysaccharides, formed from disaccharide repeating units. For a number of bacterial species, including Flavobacterium heparinum synthesize GAG lyases, these enzymes are used to degrade and utilise glycosaminoglycans as a source of carbon in the bacterium's natural environment. In topological terms, the known structures of polysaccharide lyases fall within two protein fold families. Pectin and pectate lyases, as well as chondroitin lyase B belong to the right-handed parallel beta-helix family and have the substrate-binding site in roughly the same topological location. The second topological family, all of which contain a domain consisting of an incomplete (alpha/alpha)5 toroid, includes chondroitin AC lyase family, and alginate lyase A1-III family from Sphingomonas species A1 [1].

Structural linksHelp
PDB - click here
Database linksHelp
Enzyme: EC:4.2.2

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008929 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O10305 Occlusion-derived virus envelope protein E66

P59807 Chondroitin ABC endolyase 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR014718 Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR012329 Polysaccharide lyase family 8, N-terminal
IPR004103 Polysaccharide lyase family 8, C-terminal
IPR011013 Glycoside hydrolase-type carbohydrate-binding
IPR008929 Chondroitin AC/alginate lyase
IPR011071 Polysaccharide lyase family 8-like, C-terminal
IPR015177 Lyase, catalytic
IPR008979 Galactose-binding domain-like
IPR015176 Lyase, N-terminal
IPR003159 Polysaccharide lyase family 8, central domain
IPR006934 Baculovirus occlusion-derived virus envelope, E66
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Huang W, Boju L, Tkalec L, Su H, Yang HO, Gunay NS, Linhardt RJ, Kim YS, Matte A, Cygler M.
Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis.
Biochemistry 40 2359-72 2001 [PubMed: 11327856]
http://dx.doi.org/10.1021/bi0024254

Additional ReadingHelp
Maruyama Y, Mikami B, Hashimoto W, Murata K.
A structural factor responsible for substrate recognition by Bacillus sp. GL1 xanthan lyase that acts specifically on pyruvated side chains of xanthan.
Biochemistry 46 2007 781-91 [PubMed: 17223699]
http://dx.doi.org/10.1021/bi0619775
Rigden DJ, Littlejohn JE, Joshi HV, de Groot BL, Jedrzejas MJ.
Alternate structural conformations of Streptococcus pneumoniae hyaluronan lyase: insights into enzyme flexibility and underlying molecular mechanism of action.
J. Mol. Biol. 358 2006 1165-78 [PubMed: 16569416]
http://dx.doi.org/10.1016/j.jmb.2006.02.066
Lunin VV, Li Y, Linhardt RJ, Miyazono H, Kyogashima M, Kaneko T, Bell AW, Cygler M.
High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism.
J. Mol. Biol. 337 2004 367-86 [PubMed: 15003453]
http://dx.doi.org/10.1016/j.jmb.2003.12.071
Rigden DJ, Botzki A, Nukui M, Mewbourne RB, Lamani E, Braun S, von Angerer E, Bernhardt G, Dove S, Buschauer A, Jedrzejas MJ.
Design of new benzoxazole-2-thione-derived inhibitors of Streptococcus pneumoniae hyaluronan lyase: structure of a complex with a 2-phenylindole.
Glycobiology 16 2006 757-65 [PubMed: 16638841]
http://dx.doi.org/10.1093/glycob/cwj116
Maruyama Y, Hashimoto W, Mikami B, Murata K.
Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: insights into the enzyme reaction mechanism.
J. Mol. Biol. 350 2005 974-86 [PubMed: 15979090]
http://dx.doi.org/10.1016/j.jmb.2005.05.055
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InterPro 23.1