Structural highlights
Function
LP11B_ASPFU Lytic polysaccharide monooxygenase (LPMO)-like protein that acts as a strict peroxygenase and does not catalyze a monooxygenase reaction (PubMed:34567832). It is indeed hardly active on chitin, while being very active on soluble oligomers of N-acetylglucosamine (PubMed:34567832). Cleaves the glycosidic bonds byoxidizing the C1 position (PubMed:34567832). Also unable to oxidize cellopentaose (PubMed:34738811). Probably breaks glycosidic bonds in non-polymeric substrates possibly carbohydrates in the cell wall of the fungus or its competitors (PubMed:34567832). In the presence of chitotetraose, the enzyme can withstand considerable amounts of H(2)O(2), which it uses to efficiently and stoichiometrically convert this substrate (PubMed:34567832).[1] [2]
References
- ↑ Rieder L, Petrović D, Väljamäe P, Eijsink VGH, Sørlie M. Kinetic Characterization of a Putatively Chitin-Active LPMO Reveals a Preference for Soluble Substrates and Absence of Monooxygenase Activity. ACS Catal. 2021 Sep 17;11(18):11685-11695. PMID:34567832 doi:10.1021/acscatal.1c03344
- ↑ Rieder L, Stepnov AA, Sørlie M, Eijsink VGH. Fast and Specific Peroxygenase Reactions Catalyzed by Fungal Mono-Copper Enzymes. Biochemistry. 2021 Nov 30;60(47):3633-3643. PMID:34738811 doi:10.1021/acs.biochem.1c00407
