| RRC ID |
71376
|
| Author |
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.
|
| Title |
Fungal GH25 muramidases: New family members with applications in animal nutrition and a crystal structure at 0.78Å resolution.
|
| Journal |
PLoS One
|
| Abstract |
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.
|
| Volume |
16(3)
|
| Pages |
e0248190
|
| Published |
2021-1-1
|
| DOI |
10.1371/journal.pone.0248190
|
| PII |
PONE-D-20-36895
|
| PMID |
33711051
|
| PMC |
PMC7954357
|
| MeSH |
Animals
Cell Wall / metabolism
Crystallography, X-Ray
Fungi / metabolism*
Models, Molecular
Muramidase / metabolism*
Protein Conformation*
|
| Resource |
| General Microbes |
JCM7366 |
