Baeyer-Villiger Monooxygenases (BVMOs)

Baeyer-Villiger monooxygenases catalyze the oxidation of carbonylic substrates to ester or lactone products using NADPH as electron donor and molecular oxygen as oxidative reactant. Using protein engineering, kinetics, microspectrophotometry, crystallography, and intermediate analogs, we have captured several snapshots along the catalytic cycle which highlight key features in enzyme catalysis. After acting as electron donor, the enzyme-bound NADP(H) forms an H-bond with the flavin cofactor. This interaction is critical for stabilizing the oxygen-activating flavin-peroxide intermediate that results from the reaction of the reduced cofactor with oxygen. An essential active-site arginine acts as anchoring element for proper binding of the ketone substrate. Its positively charged guanidinium group can enhance the propensity of the substrate to undergo a nucleophilic attack by the flavin-peroxide intermediate. Furthermore, the arginine side chain, together with the NADP(+) ribose group, forms the niche that hosts the negatively charged Criegee intermediate that is generated upon reaction of the substrate with the flavin-peroxide. The fascinating ability of Baeyer-Villiger monooxygenases to catalyze a complex multistep catalytic reaction originates from concerted action of this Arg-NADP(H) pair and the flavin subsequently to promote flavin reduction, oxygen activation, tetrahedral intermediate formation, and product synthesis and release. The emerging picture is that these enzymes are mainly oxygen-activating and “Criegee-stabilizing” catalysts that act on any chemically suitable substrate that can diffuse into the active site, emphasizing their potential value as toolboxes for biocatalytic applications.

Our collection of BVMOs contains enzymes listed below. Please note that list is currently being updated as our collection has been expanded recently with new enzymes, but also with new mutants with promising characteristics. For certain enzymes we have libraries which can be screened for specific target compounds.

  1. PAMO
  2. PAMO M446G
  3. PAMO P440N
  4. PAMO P440L
  5. PAMO ΔS441ΔA442
  6. PAMO L443F
  7. PAMO A442G
  8. PAMO I67T
  9. CPDMO
  10. CRE2-PAMO-STMO chimera
  11. CRE2-PAMO-CHMO chimera
  12. CRE2-PAMO-STMO-PAMO chimera
  13. CRE2-PAMO-Met1 chimera
  14. CRE2-CPMO F156L
  15. BVMO1 Rhodococcus jostii
  16. BVMO4 Rhodococcus jostii
  17. BVMO6 Rhodococcus jostii
  18. BVMO9 Rhodococcus jostii
  19. BVMO10 Rhodococcus jostii
  20. BVMO11 Rhodococcus jostii
  21. BVMO14 Rhodococcus jostii
  22. BVMO15 Rhodococcus jostii
  23. BVMO20 Rhodococcus jostii
  24. BVMO21 Rhodococcus jostii
  25. BVMO24 Rhodococcus jostii
  26. CRE2-BVMO2 Rhodococcus jostii
  27. CRE2-BVMO3 Rhodococcus jostii
  28. CRE2-BVMO5 Rhodococcus jostii
  29. CRE2-BVMO7 Rhodococcus jostii
  30. CRE2-BVMO8 Rhodococcus jostii
  31. CRE2-BVMO12 Rhodococcus jostii
  32. CRE2-BVMO13 Rhodococcus jostii
  33. CRE2-BVMO16 Rhodococcus jostii
  34. CRE2-BVMO17 Rhodococcus jostii
  35. CRE2-BVMO18 Rhodococcus jostii
  36. CRE2-BVMO19 Rhodococcus jostii
  37. CRE2-BVMO Aspergillus fumigatus (Af2 fusion)
  38. CRE2-PAMO
  39. CRE2-CHMO Acinetobacter sp.
  40. CRE2-CPMO
  41. CRE2-HAPMO
  42. CRE2-EtaA
  43. CRE2-PAMO M446G
  44. CRE2-CPDMO
  45. CRE2-STMO
  46. CRE2-CHMO A255C-A293C (R2)
  47. CRE2-CHMO A325C-L483C (R3)
  48. CRE2-CHMO L323C-A325C (RV6)
  49. CRE2-BVMO Trichodesmium erythraeum (putative)
  50. CRE2-CHMO Rhodococcus HI-31
  51. CRE2-AcMO Gordonia sp.
  52. CRE2-AlmA Acinetobacter sp.
  53. CRE2-CHMO Brachymonas petroleovorans
  54. CRE2-MekA
  55. CRE2-CHMO Xanthobacter flavus
  56. CRE2-BVMO Haloterrigena turkmenica (putative)
  57. CRE2-TmCHMO
  58. CRE2-PockeMO
  59. CRE2-BVMO Parvi
  60. CRE2-OTEMO
  61. CRE2-BVMO Ocean
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