Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution.
Muramidases/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...
| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2021-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0248190 |
| _version_ | 1798036336759799808 |
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| author | Olga V Moroz Elena Blagova Edward Taylor Johan P Turkenburg Lars K Skov Garry P Gippert Kirk M Schnorr Li Ming Liu Ye Mikkel Klausen Marianne T Cohn Esben G W Schmidt Søren Nymand-Grarup Gideon J Davies Keith S Wilson |
| author_facet | Olga V Moroz Elena Blagova Edward Taylor Johan P Turkenburg Lars K Skov Garry P Gippert Kirk M Schnorr Li Ming Liu Ye Mikkel Klausen Marianne T Cohn Esben G W Schmidt Søren Nymand-Grarup Gideon J Davies Keith S Wilson |
| author_sort | Olga V Moroz |
| collection | DOAJ |
| description | Muramidases/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 β-1,4-N-acetyl- and β-1,4-N,6-O-diacetylmuramidase activities, cleaving the β-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 Å resolution, together with that of its homologue from Trichobolus zukalii at 1.4 Å, 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. |
| first_indexed | 2024-04-11T21:11:27Z |
| format | Article |
| id | doaj.art-d3c1f6391cf842f98c1cc16537ed4d9e |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-11T21:11:27Z |
| publishDate | 2021-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-d3c1f6391cf842f98c1cc16537ed4d9e2022-12-22T04:03:01ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01163e024819010.1371/journal.pone.0248190Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution.Olga V MorozElena BlagovaEdward TaylorJohan P TurkenburgLars K SkovGarry P GippertKirk M SchnorrLi MingLiu YeMikkel KlausenMarianne T CohnEsben G W SchmidtSøren Nymand-GrarupGideon J DaviesKeith S WilsonMuramidases/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 β-1,4-N-acetyl- and β-1,4-N,6-O-diacetylmuramidase activities, cleaving the β-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 Å resolution, together with that of its homologue from Trichobolus zukalii at 1.4 Å, 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.https://doi.org/10.1371/journal.pone.0248190 |
| spellingShingle | Olga V Moroz Elena Blagova Edward Taylor Johan P Turkenburg Lars K Skov Garry P Gippert Kirk M Schnorr Li Ming Liu Ye Mikkel Klausen Marianne T Cohn Esben G W Schmidt Søren Nymand-Grarup Gideon J Davies Keith S Wilson Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. PLoS ONE |
| title | Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. |
| title_full | Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. |
| title_fullStr | Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. |
| title_full_unstemmed | Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. |
| title_short | Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution. |
| title_sort | fungal gh25 muramidases new family members with applications in animal nutrition and a crystal structure at 0 78a resolution |
| url | https://doi.org/10.1371/journal.pone.0248190 |
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