23LO
crystal structure of a flavin dependent Baeyer Villiger monooxygenase from Micromonospora lupini NBC_00409 in complex with FAD
Summary for 23LO
| Entry DOI | 10.2210/pdb23lo/pdb |
| Descriptor | flavin dependent Baeyer Villiger monooxygenase, FLAVIN-ADENINE DINUCLEOTIDE (2 entities in total) |
| Functional Keywords | spirotetronates, marine actinomycete, fad-dependent monooxygenase, biosynthesis, oxidative modification, macrocyclic lactone, biosynthetic protein |
| Biological source | Micromonospora lupini |
| Total number of polymer chains | 6 |
| Total formula weight | 337282.78 |
| Authors | Lin, Z.E.,Chen, S.Q.,Zhang, L.P.,Zhang, C.S. (deposition date: 2026-02-10, release date: 2026-05-27, Last modification date: 2026-06-03) |
| Primary citation | Chen, S.,Lin, Z.,Zhang, Q.,Tan, B.,Zhang, X.,Zhang, W.,Zhang, H.,Zhu, Y.,Zhang, L.,Zhang, C. Deciphering Early Oxidative Steps in Spirotetronate Biosynthesis Reveals a Two-Enzyme Cascade for Macrocyclic Lactone Formation. Org.Lett., 28:6376-6381, 2026 Cited by PubMed Abstract: We decipher functions of three monooxygenases (PasO1, PasO3, and PasO4) in early biosynthetic steps in spirotetronate PA-46101 and demonstrate a PasO4/PasO3 cascade for forging the signature macrocyclic lactone. The P450 PasO4 oxidizes a methyl group to a carboxylate, enabling a regiospecific Baeyer-Villiger oxidation by PasO3. Structural analysis of a PasO3 homologue identifies a carboxylate-binding pocket essential for this strict substrate specificity. This two-enzyme cascade can serve as a portable biocatalytic tool for diversifying spirotetronates. PubMed: 42125861DOI: 10.1021/acs.orglett.6c01499 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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