Glycoside hydrolase family 24 explained
Symbol: | Phage_lysozyme |
Phage lysozyme |
Pfam: | PF00959 |
Pfam Clan: | CL0037 |
Interpro: | IPR002196 |
Scop: | 119l |
Cazy: | GH24 |
Cdd: | cd00442 |
In molecular biology, glycoside hydrolase family 24 is a family of glycoside hydrolases.
Glycoside hydrolases 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.[1] [2] [3] This classification is available on the CAZy web site,[4] [5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6] [7]
Glycoside hydrolase family 24 CAZY GH_24 comprises enzymes with only one known activity; lysozyme . This family includes lambda phage lysozyme and Escherichia coli T4 phage endolysin.[8] 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.[9] This mobility is thought to be important in allowing access of substrates to the enzyme active site.
Notes and References
- 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 . Proceedings of the National Academy of Sciences of the United States of America . 92 . 15 . 7090–4 . July 1995 . 7624375 . 41477 . 10.1073/pnas.92.15.7090 . 1995PNAS...92.7090H . free .
- Davies G, Henrissat B . Structures and mechanisms of glycosyl hydrolases . Structure . 3 . 9 . 853–9 . September 1995 . 8535779 . 10.1016/S0969-2126(01)00220-9 . free .
- Henrissat B, Bairoch A . Updating the sequence-based classification of glycosyl hydrolases . The Biochemical Journal . 316 . Pt 2 . 695–6 . June 1996 . 8687420 . 1217404 . 10.1042/bj3160695.
- Web site: Home. CAZy.org. en. 2018-03-06.
- Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B . The carbohydrate-active enzymes database (CAZy) in 2013 . Nucleic Acids Research . 42 . Database issue . D490-5 . January 2014 . 24270786 . 3965031 . 10.1093/nar/gkt1178 .
- Web site: Glycoside Hydrolase Family 24. CAZypedia.org. en. 2018-03-06.
- Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes . Glycobiology . 28 . 1 . 3–8 . December 2018 . 29040563 . 10.1093/glycob/cwx089 . CAZypedia Consortium . free .
- Weaver LH, Matthews BW . Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution . Journal of Molecular Biology . 193 . 1 . 189–99 . January 1987 . 3586019 . 10.1016/0022-2836(87)90636-X .
- Faber HR, Matthews BW . A mutant T4 lysozyme displays five different crystal conformations . Nature . 348 . 6298 . 263–6 . November 1990 . 2234094 . 10.1038/348263a0 . 1990Natur.348..263F . 4266149 .