Identification of a Baeyer–Villiger monooxygenase sequence motif

FEBS Letters - Tập 518 - Trang 43-47 - 2002
Marco W. Fraaije1, Nanne M. Kamerbeek1, Willem J.H. van Berkel2, Dick B. Janssen1
1Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
2Laboratory of Biochemistry, Department of Agrotechnology and Food Sciences, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands

Tóm tắt

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.

Tài liệu tham khảo

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FEBS Letters

Tập 518

43-47

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