Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity.

ABSTRACT: The recently discovered lytic polysaccharide monooxygenases (LPMOs) carry out oxidative cleavage of polysaccharides and are of major importance for efficient processing of biomass. NcLPMO9C from Neurospora crassa acts both on cellulose and on non-cellulose β-glucans, including cellodextrins and xyloglucan. The crystal structure of the catalytic domain of NcLPMO9C revealed an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. The ability of NcLPMO9C to act on soluble substrates was exploited to study enzyme-substrate interactions. EPR studies demonstrated that the Cu(2+) center environment is altered upon substrate binding, whereas isothermal titration calorimetry studies revealed binding affinities in the low micromolar range for po

SUBMITTER: Borisova AS 

PROVIDER: S-EPMC4645601 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature