 |
InterPro: IPR012329 Polysaccharide lyase family 8, N-terminal
Protein matches
|
UniProtKB Matches: 338 proteins |
|
Accession
|
IPR012329 Lyase_8_N |
Type
|
Domain |
Signatures
|
|
InterPro Relationships
|
|
Parent
|
IPR008929 Chondroitin AC/alginate lyase
|
|
Children
|
IPR012970 Polysaccharide lyase 8, N-terminal alpha-helical
IPR015177 Lyase, catalytic
|
GO Term annotation
|
|
Process
|
GO:0005975 carbohydrate metabolic process
|
|
Function
|
GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
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 links
|
|
Database links
|
|
Additional Reading
|
|
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
|
|
|
InterPro 23.1
|