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InterPro: IPR012970 Polysaccharide lyase 8, N-terminal alpha-helical

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UniProtKB

Matches:

283 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR012970 Lyase_8_alpha_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF08124	Lyase_8_N	283
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012329 Polysaccharide lyase family 8, N-terminal

InterPro annotation

Entry Details in BioMart

Abstract

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.

Structural links Help

PDB - click here

SCOP: a.102.3.2

CATH: 1.50.10.100

Database links Help

Enzyme: EC:4.2.2.1

PANDIT: PF08124

Blocks: IPB012970

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012970

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q53591 Hyaluronate lyase

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
IPR014756	Immunoglobulin E-set
IPR011013	Glycoside hydrolase-type carbohydrate-binding
IPR012970	Polysaccharide lyase 8, N-terminal alpha-helical
IPR008929	Chondroitin AC/alginate lyase
IPR011071	Polysaccharide lyase family 8-like, C-terminal
IPR008979	Galactose-binding domain-like
IPR003159	Polysaccharide lyase family 8, central domain
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	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
	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 1999 635-47 [PubMed: 10329169] http://dx.doi.org/10.1006/jmbi.1999.2698
	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