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.
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The enzyme appears in viruses and cellular organisms
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.
cellobiose dehydrogenase may serve as the physiologic electron donor. In the presence of cellobiose dehydrogenase and cellobiose the enzyme activity is comparable to that with excess ascorbate.
cellobiose dehydrogenase may serve as the physiologic electron donor. In the presence of cellobiose dehydrogenase and cellobiose the enzyme activity is comparable to that with excess ascorbate.
enzyme acts in synergy with glycoside hydrolase, beta-amylase, largely enhancing maltose release from retrograded starch by beta-amylase. The largest enhancements are obtained under specific conditions using the reducing cofactor cysteine, the presence of LPMO enhances the release of maltose by beta-amylase by 100fold
structure with an ordered zinc-bound active site, at 1.65 A resolution, and three structures from crystals soaked with maltooligosaccharides in solutions devoid of zinc ions, at resolutions of up to 1.10 A
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concomitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concommitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concomitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concomitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concommitant with secretion of several redoxactive enzymes
LPMO13A and LPMO13B are among the most abundant proteins in the culture supernatants upon growth on starches, concommitant with secretion of several redoxactive enzymes