 |
InterPro: IPR018077 Glycoside hydrolase, family 25 subgroup
Protein matches
|
UniProtKB Matches: 570 proteins |
|
Accession
|
IPR018077 Glyco_hydro_fam25_sg |
Type
|
Domain |
Signatures
|
|
InterPro Relationships
|
|
Parent
|
IPR002053 Glycoside hydrolase, family 25
|
|
Contains
|
IPR008270 Glycoside hydrolase, family 25, active site
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Glycoside hydrolase family 25 GH25 comprises enzymes with only one known activity; lysozyme (EC:3.2.1.17).
It has been shown [5, 6] that a number of cell-wall lytic enzymes are evolutionary related and can be classified into a single family.
Two residues, an aspartate and a glutamate, have been shown [7] to be
important for the catalytic activity of the Charalopsis enzyme. These residues
as well as some others in their vicinity are conserved in all proteins from
this family.
|
Structural links
|
|
Publications
|
|
1.
|
Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995
[PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
|
|
2.
|
Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995
[PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
|
|
3.
|
Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
|
|
4.
|
Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
|
|
5.
|
Croux C, Garcia JL.
Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC824: comparison with other lytic enzymes.
Gene 104 25-31 1991
[PubMed: 1916274]
http://dx.doi.org/10.1016/0378-1119(91)90460-S
|
|
6.
|
Henrissat B.
A classification of glycosyl hydrolases based on amino acid sequence similarities.
Biochem. J. 280 ( Pt 2) 309-16 1991
[PubMed: 1747104]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1747104
|
|
7.
|
Fouche PB, Hash JH.
The N,O-diacetylmuramidase of Chalaropsis species. Identificaiton of aspartyl and glutamyl residues in the active site.
J. Biol. Chem. 253 6787-93 1978
[PubMed: 567645]
http://intl.jbc.org/cgi/reprint/253/19/6787.pdf
|
Additional Reading
|
|
Monterroso B, Albert A, Martinez-Ripoll M, Garcia P, Garcia JL, Menendez M, Hermoso JA.
Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae.
Acta Crystallogr. D Biol. Crystallogr. 58 2002 1487-9
[PubMed: 12198311]
http://dx.doi.org/10.1107/S0907444902011563
|
|
Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M.
Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
Structure 11 2003 1239-49
[PubMed: 14527392]
http://dx.doi.org/10.1016/j.str.2003.09.005
|
|
Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA.
Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1.
J. Biol. Chem. 282 2007 24990-9
[PubMed: 17581815]
http://dx.doi.org/10.1074/jbc.M704317200
|
|
Rau A, Hogg T, Marquardt R, Hilgenfeld R.
A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution.
J. Biol. Chem. 276 2001 31994-9
[PubMed: 11427528]
http://dx.doi.org/10.1074/jbc.M102591200
|
|
|
InterPro 23.1
|