A fungal cellulase shows sequence homology with the active site of hen egg-white lysozyme.
The N-terminal amino acid sequence of an endo-beta-1,4-glucanase from the cellulase complex of the white-rot fungus Schizophyllum commune has been determined. The sequence from Glu-33 to Tyr-51 was homologous with the active site sequences of various hen egg-white type lysozymes, including lysozyme catalytic residues (Glu-35, Asp-52) and substrate binding residue Asn-44. The homology offers evidence for a lysozyme-type mechanism in enzymic hydrolysis of cellulose.
D000363:Agaricales / Q000201:enzymology*; D000818:Animals; D001665:Binding Sites; D002480:Cellulase / Q000032:analysis*; D002482:Cellulose / Q000378:metabolism; D002645:Chickens; D004529:Egg White / Q000032:analysis*; D009113:Muramidase / Q000032:analysis*; D012567:Schizophyllum / Q000201:enzymology*
D002482:Cellulose; D009113:Muramidase; D002480:Cellulase