| Phage lysozyme | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| lysozyme from bacteriophage lambda | |||||||||
| Identifiers | |||||||||
| Symbol | Phage_lysozyme | ||||||||
| Pfam | PF00959 | ||||||||
| Pfam clan | CL0037 | ||||||||
| InterPro | IPR002196 | ||||||||
| SCOP | 119l | ||||||||
| CAZy | GH24 | ||||||||
|
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In molecular biology, glycoside hydrolase family 24 is a family of glycoside hydrolases.
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.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. [5]
Glycoside hydrolase family 24 CAZY GH_24 comprises enzymes with only one known activity; lysozyme (EC 3.2.1.17). This family includes lambda phage lysozyme and Escherichia coli endolysin.[6] 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.[6][7] This mobility is thought to be important in allowing access of substrates to the enzyme active site.