lytic starch monooxygenase;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
starch, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
starch + reduced acceptor + O2 = D-glucono-1,5-lactone-terminated malto-oligosaccharides + short-chain malto-oligosaccharides + acceptor + H2O
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.
EC 184.108.40.206 created 2017
K00516 lytic starch monooxygenase
PFY: PFICI_03594 PFICI_10005
ACT: ACLA_008190 ACLA_099410
NFI: NFIA_009310 NFIA_027740
PCS: Pc13g11940 Pc20g13600
TRG: TRUGW13939_00643 TRUGW13939_07018 » show all
Vu VV, Beeson WT, Span EA, Farquhar ER, Marletta MA
A family of starch-active polysaccharide monooxygenases.
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
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.
Lo Leggio L, Simmons TJ, Poulsen JC, Frandsen KE, Hemsworth GR, Stringer MA, von Freiesleben P, Tovborg M, Johansen KS, De Maria L, Harris PV, Soong CL, Dupree P, Tryfona T, Lenfant N, Henrissat B, Davies GJ, Walton PH
Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase.