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Structure of muramidase from Trichobolus zukaliiStructure of muramidase from Trichobolus zukalii
Structural highlights
FunctionPublication Abstract from PubMedMuramidases/lysozymes hydrolyse the peptidoglycan component of the bacterial cell wall. They are found in many of the glycoside hydrolase (GH) families. Family GH25 contains muramidases/lysozymes, known as CH type lysozymes, as they were initially discovered in the Chalaropsis species of fungus. The characterized enzymes from GH25 exhibit both beta-1,4-N-acetyl- and beta-1,4-N,6-O-diacetylmuramidase activities, cleaving the beta-1,4-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) moieties in the carbohydrate backbone of bacterial peptidoglycan. Here, a set of fungal GH25 muramidases were identified from a sequence search, cloned and expressed and screened for their ability to digest bacterial peptidoglycan, to be used in a commercial application in chicken feed. The screen identified the enzyme from Acremonium alcalophilum JCM 736 as a suitable candidate for this purpose and its relevant biochemical and biophysical and properties are described. We report the crystal structure of the A. alcalophilum enzyme at atomic, 0.78 A resolution, together with that of its homologue from Trichobolus zukalii at 1.4 A, and compare these with the structures of homologues. GH25 enzymes offer a new solution in animal feed applications such as for processing bacterial debris in the animal gut. Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78A resolution.,Moroz OV, Blagova E, Taylor E, Turkenburg JP, Skov LK, Gippert GP, Schnorr KM, Ming L, Ye L, Klausen M, Cohn MT, Schmidt EGW, Nymand-Grarup S, Davies GJ, Wilson KS PLoS One. 2021 Mar 12;16(3):e0248190. doi: 10.1371/journal.pone.0248190., eCollection 2021. PMID:33711051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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