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PMID: 6686034 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A fungal cellulase shows sequence homology with the active site of hen egg-white lysozyme.

Biochemical and biophysical research communications ·Vol. 116 ·No. 2 ·1983-10-31 ·Pages 408-11

Yaguchi M, Roy C, Rollin CF, Paice MG, Jurasek L

Abstract

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.

MeSH Terms
Agaricales/enzymology Animals Binding Sites Cellulase/analysis Cellulose/metabolism Chickens Egg White/analysis Muramidase/analysis Schizophyllum/enzymology
Chemicals
Cellulose Muramidase Cellulase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Yaguchi M
Roy C
Rollin C F
Paice M G
Jurasek L
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1983-10-31
Pages
408-11
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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