Yaguchi M, Roy C, Rollin C F, Paice M G, Jurasek L
Biochem Biophys Res Commun. 1983 Oct 31;116(2):408-11. doi: 10.1016/0006-291x(83)90537-5.
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.
已确定了来自白腐真菌裂褶菌纤维素酶复合物的一种内切-β-1,4-葡聚糖酶的N端氨基酸序列。从Glu-33到Tyr-51的序列与各种鸡蛋清类型溶菌酶的活性位点序列同源,包括溶菌酶催化残基(Glu-35、Asp-52)和底物结合残基Asn-44。这种同源性为纤维素酶促水解中的溶菌酶型机制提供了证据。