Baeyer-Villiger Monooxygenases (BVMOs)
Baeyer-Villiger monooxygenases (BVMOs) catalyze the oxidation of carbonylic substrates to ester or lactone products using NADPH as electron donor and molecular oxygen as electron acceptor. 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, which makes BVMOs versatile tools for biocatalytic applications.
Besides Baeyer-Villiger oxidations, these enzymes are used for heteroatom oxidations, with most industrial efforts focused on the oxidation of sulfides, forming chiral sulfoxides. Also oxidations of amines, boron and selenium have been demonstrated.
Our collection of BVMOs contains the enzymes listed below, of which a large proportion is in stock as purified enzyme. Our collection of BVMOs is continuously expanded with new enzymes, but also with new mutants with promising characteristics. For several enzymes we have larger libraries that can be screened to fine-tune selectivity.
- ACMO [Gordonia sp. TY-5]
- Afl838 [Aspergillus flavus NRRL3357]
- AlmA [Acinetobacter radioresistens]
- BVMO 4 [Dietzia sp. D5]
- BVMO 1 [Rhodococcus jostii RHA1]
- BVMO 2 [Rhodococcus jostii RHA1]
- BVMO 3 [Rhodococcus jostii RHA1]
- BVMO 4 [Rhodococcus jostii RHA1]
- BVMO 5 [Rhodococcus jostii RHA1]
- BVMO 6 [Rhodococcus jostii RHA1]
- BVMO 7 [Rhodococcus jostii RHA1]
- BVMO 8 [Rhodococcus jostii RHA1]
- BVMO 9 [Rhodococcus jostii RHA1]
- BVMO 10 [Rhodococcus jostii RHA1]
- BVMO 11 [Rhodococcus jostii RHA1]
- BVMO 12 [Rhodococcus jostii RHA1]
- BVMO 13 [Rhodococcus jostii RHA1]
- BVMO 14 [Rhodococcus jostii RHA1]
- BVMO 15 [Rhodococcus jostii RHA1]
- BVMO 16 [Rhodococcus jostii RHA1]
- BVMO 17 [Rhodococcus jostii RHA1]
- BVMO 18 [Rhodococcus jostii RHA1]
- BVMO 19 [Rhodococcus jostii RHA1]
- BVMO 20 [Rhodococcus jostii RHA1]
- BVMO 21 [Rhodococcus jostii RHA1]
- BVMO 23 [Rhodococcus jostii RHA1]
- BVMO 24 [Rhodococcus jostii RHA1]
- BVMO [Streptomyces aculeolatus]
- BVMO Af1 [Aspergillus fumigatus Af293]
- BVMO ETaA [Mycobacterium tuberculosis H37Rv]
- CAMO [Ilyonectria radicicola]
- CDMO [Rhodococcus ruber]
- CHMO [Acinetobacter sp. NCIMB9871]
- CHMO A255C-A293C (R2)
- CHMO A325C-L483C (R3)
- CHMO L323C-A325C (RV6)
- CHMO [Brachymonas petroleovorans]
- CHMO [Rhodococcus sp. HI-31]
- TmCHMO [Thermocrispum municipale]
- TmCHMO LGY3-4-D11
- TmCHMO LGY3-4-E5
- TmCHMO LGY3-D-A9
- TmCHMO LGY3-D-E1
- TmCHMO LGY2-B6
- TmCHMO LGY1-492-A7
- TmCHMO LGY1-248-D3
- TmCHMO LGY1-437-E12
- CHMO [Xanthobacter flavus]
- CmBVMO [Cyanidioschyzon merolae]
- CPDMO [Pseudomonas sp. HI-70]
- CPMO [Comamonas sp. NCIMB 9872]
- CPMO F156L
- HAPMO [Pseudomonas fluorescens ACB]
- HtCHMO [Haloterrigena turkmenica]
- LbBVMO [Leptospira biflexa]
- ObBVMO [Pseudooceanicola batsensis] / BVMO-Ocean
- OocK [Serratia plymuthica 4Rx13]
- OTEMO [Pseudomonas putida ATCC 17453]
- PAMO [Thermobifida fusca YX]
- PAMO M446G
- PAMO P440N
- PAMO P440L
- PAMO ΔS441ΔA442
- PAMO L443F
- PAMO A442G
- PAMO I67T
- PAMO-STMO chimera
- PAMO-CHMO chimera
- PAMO-STMO-PAMO chimera
- PAMO-Met1 chimera
- PlBVMO [Parvibaculum lavamentivorans]
- PockeMO [Thermothelomyces thermophilus]
- RpBVMO [Rhodococcus pyridinovorans]
- SAPMO [Comamonas testosteroni]
- SlPAMO-B [Streptomyces leeuwenhoekii]
- SlPAMO-E [Streptomyces leeuwenhoekii]
- STMO [Rhodococcus rhodochrous]
- TeBVMO [Trichodesmium erythraeum]
- RhCHMO (thermostable variant – M8B: S534R/E91Q/R280Y/A455V/A115V/N431Y/Q439P/D95H)