The enzyme cleaves starch in an oxidative manner. It releases fragments of starch with a D-glucono-1,5-lactone at the reducing end. The initially formed alpha-D-glucono-1,5-lactone at the reducing end of the shortend amylose chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate has been found to be able to serve as reducing agent. The enzyme contains copper at the active site.
Gudmundsson M, Kim S, Wu M, Ishida T, Momeni MH, Vaaje-Kolstad G, Lundberg D, Royant A, Stahlberg J, Eijsink VG, Beckham GT, Sandgren M
Title
Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction.
