title: Identification of a Baeyer-Villiger monooxygenase sequence motif.
abstract: Baeyer-Villiger monooxygenases (BVMOs) form a distinct class of flavoproteins that catalyze the insertion of an oxygen atom in a C-C bond using dioxygen and NAD(P)H. Using newly characterized BVMO sequences, we have uncovered a BVMO-identifying sequence motif: FXGXXXHXXXW(P/D). Studies with site-directed mutants of 4-hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB suggest that this fingerprint sequence is critically involved in catalysis. Further sequence analysis showed that the BVMOs belong to a novel superfamily that comprises three known classes of FAD-dependent monooxygenases: the so-called flavin-containing monooxygenases (FMOs), the N-hydroxylating monooxygenases (NMOs), and the BVMOs. Interestingly, FMOs contain an almost identical sequence motif when compared to the BVMO sequences: FXGXXXHXXX(Y/F). Using these novel amino acid sequence fingerprints, BVMOs and FMOs can be readily identified in the protein sequence databank.
authors: Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands. m.w.fraaije@chem.rug.nl
authors: Marco W
authors: MW
authors: Fraaije
authors: Nanne M
authors: NM
authors: Kamerbeek
authors: Willem J H
authors: WJ
authors: van Berkel
authors: Dick B
authors: DB
authors: Janssen
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017124:Conserved Sequence; D005420:Flavoproteins / Q000737:chemistry / Q000235:genetics; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009154:Mutation; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid
chemical_list: D005420:Flavoproteins; D010105:Oxygenases; C427385:4-hydroxyacetophenone monooxygenase; C020066:dimethylaniline monooxygenase (N-oxide forming)