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InterPro: IPR012329 Polysaccharide lyase family 8, N-terminal

Protein matchesHelp
UniProtKB
Matches:
338 proteins
AccessionHelp IPR012329 Lyase_8_N
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR008929 Chondroitin AC/alginate lyase
Children IPR012970 Polysaccharide lyase 8, N-terminal alpha-helical
IPR015177 Lyase, catalytic
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Proteins containing this N-terminal 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 [1]. Hyaluronate lyase (EC: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 N-terminal domain is multi-helical, with up to seven alpha-hairpins arranged in a closed circular array. Other bacterial enzymes that display this structure include the N-terminal domain of chondroitin AC lyase (EC:4.2.2.5) [2], and the N-terminal domain of xanthan lyase (EC:4.2.2.12) [3]. This entry represents the N-terminal domain of hyaluronate lyase, chondroitin AC lyase and xanthan lyase.

Structural linksHelp
CATH: 1.50.10.100
Database linksHelp
Enzyme: EC:4.2.2

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012329 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Rigden DJ, Jedrzejas MJ.
Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action.
J. Biol. Chem. 278 50596-606 2003 [PubMed: 14523022]
http://dx.doi.org/10.1074/jbc.M307596200
2. Fethiere J, Eggimann B, Cygler M.
Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes.
J. Mol. Biol. 288 635-47 1999 [PubMed: 10329169]
http://dx.doi.org/10.1006/jmbi.1999.2698
3. Hashimoto W, Nankai H, Mikami B, Murata K.
Crystal structure of Bacillus sp. GL1 xanthan lyase, which acts on the side chains of xanthan.
J. Biol. Chem. 278 7663-73 2003 [PubMed: 12475987]
http://dx.doi.org/10.1074/jbc.M208100200

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