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Fungal lytic polysaccharide monooxygenases bind starch and β‐cyclodextrin similarly to amylolytic hydrolases
Author(s) -
Nekiunaite Laura,
Isaksen Trine,
VaajeKolstad Gustav,
Abou Hachem Maher
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12293
Subject(s) - polysaccharide , starch , monooxygenase , biochemistry , chemistry , lytic cycle , axenic , hydrolysis , carbohydrate binding module , biology , glycoside hydrolase , enzyme , bacteria , genetics , virus , cytochrome p450
Starch‐binding modules of family 20 ( CBM 20) are present in 60% of lytic polysaccharide monooxygenases ( LPMO s) catalyzing the oxidative breakdown of starch, which highlights functional importance in LPMO activity. The substrate‐binding properties of starch‐active LMPO s, however, are currently unexplored. Affinities and binding‐thermodynamics of two recombinant fungal LPMO s toward starch and β‐cyclodextrin were shown to be similar to fungal CBM 20s. Amplex Red assays showed ascorbate and Cu‐dependent activity, which was inhibited in the presence of β‐cylodextrin and amylose. Phylogenetically, the clustering of CBM 20s from starch‐targeting LPMO s and hydrolases was in accord with taxonomy and did not correlate to appended catalytic activity. Altogether, these results demonstrate that the CBM 20‐binding scaffold is retained in the evolution of hydrolytic and oxidative starch‐degrading activities.