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InterPro: IPR008929 Chondroitin AC/alginate lyase
Protein matches
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UniProtKB Matches: 790 proteins |
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Accession
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IPR008929 Chondroitin_lyas |
Type
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Signatures
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InterPro Relationships
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Children
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IPR012329 Polysaccharide lyase family 8, N-terminal
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Found in
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IPR006934 Baculovirus occlusion-derived virus envelope, E66
IPR008397 Alginate lyase
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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].
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Structural links
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Database links
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Additional Reading
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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
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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
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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
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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
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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
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