Summary: Phage lysozyme
This is the Wikipedia entry entitled "Glycoside hydrolase family 24". More...
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Glycoside hydrolase family 24 Edit Wikipedia article
lysozyme from bacteriophage lambda
Glycoside 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 glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 24 CAZY GH_24 comprises enzymes with only one known activity; lysozyme (EC 220.127.116.11). This family includes lambda phage lysozyme and Escherichia coli endolysin. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryotic cell walls. E. coli endolysin also functions in bacterial cell lysis and acts as a transglycosylase. The T4 lysozyme structure contains 2 domains, the interface between which forms the active-site cleft. The N-terminus of the 2 domains undergoes a 'hinge-bending' motion about an axis passing through the molecular waist. This mobility is thought to be important in allowing access of substrates to the enzyme active site.
- Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- Matthews BW, Weaver LH (1987). "Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution". J. Mol. Biol. 193 (1): 189–199. doi:10.1016/0022-2836(87)90636-X. PMID 3586019.
- Matthews BW, Faber HR (1990). "A mutant T4 lysozyme displays five different crystal conformations". Nature 348 (6298): 263–266. doi:10.1038/348263a0. PMID 2234094.
Phage lysozyme Provide feedback
This family includes lambda phage lysozyme and E. coli endolysin.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002196
O-Glycosyl hydrolases (EC) 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 [PUBMED:7624375, PUBMED:8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.
This entry includes Bacteriophage lambda lysozyme and Escherichia coli endolysin [PUBMED:3586019]. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryotic cell walls. E. coli endolysin also functions in bacterial cell lysis and acts as a transglycosylase. The Bacteriophage T4 lysozyme structure contains 2 domains, the interface between which forms the active-site cleft. The N terminus of the 2 domains undergoes a 'hinge-bending' motion about an axis passing through the molecular waist [PUBMED:3586019, PUBMED:2234094]. This mobility is thought to be important in allowing access of substrates to the enzyme active site.
|Molecular function||lysozyme activity (GO:0003796)|
|Biological process||cell wall macromolecule catabolic process (GO:0016998)|
|peptidoglycan catabolic process (GO:0009253)|
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Barley chitinase, bacterial chitosanase, and lysozymes from phage and animals all hydrolyse related polysaccharides. The proteins little amino-acid similarity, but have a structurally invariant core consisting of two helices and a three-stranded beta-sheet which form the substrate-binding and catalytic cleft .
The clan contains the following 12 members:Glucosaminidase Glyco_hydro_108 Glyco_hydro_19 Glyco_hydro_46 Lys Lysozyme_like Phage_lysozyme REGB_T4 SLT SLT_2 TraH_2 Transglycosylas
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Curation and family details
|Seed source:||Sarah Teichmann|
|Author:||Bateman A, Griffiths-Jones SR|
|Number in seed:||18|
|Number in full:||3255|
|Average length of the domain:||110.60 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||59.84 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Phage_lysozyme domain has been found. There are 658 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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