裂解性多糖单加氧酶的生物信息学分析OA

Lytic polysaccharide monooxygenase(LPMO)can catalyze the oxidative lysis of glycosidic bonds in polysaccha-ride such as cellulose,and plays a key role in the degradation of biomass such as straw.To further explore the structure-activity relationship of LPMO,115 experimentally verified LPMO included in UniProtKB database were systematically stud-ied using bioinformatics analysis technology.According to its source statistics,101 LPMO from AA9 family accounted for as high as 87.8%.Further molecular evolutionary tree analysis based on genetic distance and cluster relationship obtained six groups,all AA9 family LPMO were distributed in Group I-Group V and the other three families were clustered in Group Ⅵ.Analysis of 34 LPMO derived from Aspergillus revealed that all of these proteins had at least two copper ion binding sites and contained five 100%highly conserved sequence sites.Further study of the motifs and domains of LPMO from Aspergil-lus showed that LPMO with highly similar motifs composition were close in evolution and development,but the different order of motifs can also affect the catalytic activity;the catalytic domain of LPMO of AA9 family mainly had cellulolytic enzyme activity,while the catalytic domain of AA13 family mainly had starch degradation activity.This study lays a theo-retical foundation for further investigation of LPMO structure-activity relationship.