Influence of Lytic Polysaccharide Monooxygenase Active Site Segments on Activity and Affinity.

ABSTRACT: In past years, new lytic polysaccharide monooxygenases (LPMOs) have been discovered as distinct in their substrate specificity. Their unconventional, surface-exposed catalytic sites determine their enzymatic activities, while binding sites govern substrate recognition and regioselectivity. An additional factor influencing activity is the presence or absence of a family 1 carbohydrate binding module (CBM1) connected via a linker to the C-terminus of the LPMO. This study investigates the changes in activity induced by shortening the second active site segment (Seg2) or removing the CBM1 from Neurospora crassa LPMO9C. NcLPMO9C and generated variants have been tested on regenerated amorphous cellulose (RAC), carboxymethyl cellulose (CMC) and xyloglucan (XG) using activity assays,

SUBMITTER: Laurent CVFP 

PROVIDER: S-EPMC6940765 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature