GECCO-enzymes are offered in a stable form (lyophilized). If requested by the costumer, enzymes can also be prepared as immobilized material (entrapped in hydrogels or covalently attached to polymeric resin).

Showing 1–10 of 14 results

Alcohol dehydrogenases

Alcohol dehydrogenases currently offered are listed below. For efficient cascade reactions we are offering fusions of ADHA, TbADH and ADHMi with BVMOs. Please contact us for more details.

 

  1. ADHA Pyrococcus furiosus
  2. TbADH Thermoanaerobacter brockii
  3. ADHMi Mesotoga infera
  4. LbADH Lactobacillus brevis
  5. EhADH Entamoeba histolytica
  6. GtADH Geobacillus thermodenitrificans
  7. PpADH Pseudonomas putida
  8. RjADH Rhodococcus jostii

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.

  1. ACMO [Gordonia sp. TY-5]
  2. Afl838 [Aspergillus flavus NRRL3357]
  3. AlmA [Acinetobacter radioresistens]
  4. BVMO 4 [Dietzia sp. D5]
  5. BVMO 1 [Rhodococcus jostii RHA1]
  6. BVMO 2 [Rhodococcus jostii RHA1]
  7. BVMO 3 [Rhodococcus jostii RHA1]
  8. BVMO 4 [Rhodococcus jostii RHA1]
  9. BVMO 5 [Rhodococcus jostii RHA1]
  10. BVMO 6 [Rhodococcus jostii RHA1]
  11. BVMO 7 [Rhodococcus jostii RHA1]
  12. BVMO 8 [Rhodococcus jostii RHA1]
  13. BVMO 9 [Rhodococcus jostii RHA1]
  14. BVMO 10 [Rhodococcus jostii RHA1]
  15. BVMO 11 [Rhodococcus jostii RHA1]
  16. BVMO 12 [Rhodococcus jostii RHA1]
  17. BVMO 13 [Rhodococcus jostii RHA1]
  18. BVMO 14 [Rhodococcus jostii RHA1]
  19. BVMO 15 [Rhodococcus jostii RHA1]
  20. BVMO 16 [Rhodococcus jostii RHA1]
  21. BVMO 17 [Rhodococcus jostii RHA1]
  22. BVMO 18 [Rhodococcus jostii RHA1]
  23. BVMO 19 [Rhodococcus jostii RHA1]
  24. BVMO 20 [Rhodococcus jostii RHA1]
  25. BVMO 21 [Rhodococcus jostii RHA1]
  26. BVMO 23 [Rhodococcus jostii RHA1]
  27. BVMO 24 [Rhodococcus jostii RHA1]
  28. BVMO [Streptomyces aculeolatus]
  29. BVMO Af1 [Aspergillus fumigatus Af293]
  30. BVMO ETaA [Mycobacterium tuberculosis H37Rv]
  31. CAMO [Ilyonectria radicicola]
  32. CDMO [Rhodococcus ruber]
  33. CHMO [Acinetobacter sp. NCIMB9871]
  34. CHMO A255C-A293C (R2)
  35. CHMO A325C-L483C (R3)
  36. CHMO L323C-A325C (RV6)
  37. CHMO [Brachymonas petroleovorans]
  38. CHMO [Rhodococcus sp. HI-31]
  39. TmCHMO [Thermocrispum municipale]
  40. TmCHMO LGY3-4-D11
  41. TmCHMO LGY3-4-E5
  42. TmCHMO LGY3-D-A9
  43. TmCHMO LGY3-D-E1
  44. TmCHMO LGY2-B6
  45. TmCHMO LGY1-492-A7
  46. TmCHMO LGY1-248-D3
  47. TmCHMO LGY1-437-E12
  48. CHMO [Xanthobacter flavus]
  49. CmBVMO [Cyanidioschyzon merolae]
  50. CPDMO [Pseudomonas sp. HI-70]
  51. CPMO [Comamonas sp. NCIMB 9872]
  52. CPMO F156L
  53. HAPMO [Pseudomonas fluorescens ACB]
  54. HtCHMO [Haloterrigena turkmenica]
  55. LbBVMO [Leptospira biflexa]
  56. ObBVMO [Pseudooceanicola batsensis] / BVMO-Ocean
  57. OocK [Serratia plymuthica 4Rx13]
  58. OTEMO [Pseudomonas putida ATCC 17453]
  59. PAMO [Thermobifida fusca YX]
  60. PAMO M446G
  61. PAMO P440N
  62. PAMO P440L
  63. PAMO ΔS441ΔA442
  64. PAMO L443F
  65. PAMO A442G
  66. PAMO I67T
  67. PAMO-STMO chimera
  68. PAMO-CHMO chimera
  69. PAMO-STMO-PAMO chimera
  70. PAMO-Met1 chimera
  71. PlBVMO [Parvibaculum lavamentivorans]
  72. PockeMO [Thermothelomyces thermophilus]
  73. RpBVMO [Rhodococcus pyridinovorans]
  74. SAPMO [Comamonas testosteroni]
  75. SlPAMO-B [Streptomyces leeuwenhoekii]
  76. SlPAMO-E [Streptomyces leeuwenhoekii]
  77. STMO [Rhodococcus rhodochrous]
  78. TeBVMO [Trichodesmium erythraeum]

Catalase

The thermostable catalase from Thermobifida fusca (TfuCat) can be used in biotechnological processes for the removal of hydrogen peroxide.

Except for catalyzing the dismutation of hydrogen peroxide, TfuCat was also found to catalyze oxidations of phenolic compounds.

more info: doi:10.1007/s00253-014-6060-5.

Cofactor-recycling enzymes

We are offering an array of cofactor-recycling enzymes for regeneration of NADH, NAPDH and deazaflavin (F0 and F420) cofactors.

Dehalogenases

Page is under construction. We are offering various thermostable and engineered dehalogenases.

Please make an inquiry.

Drug metabolism studies

We are offering various enzymes of high importance for pharmaceutical reasearch:

  1. Human monoamine oxidase (MAO)
  2. Human flavin-containing monooxygenase (FMO5)
  3. Mammalian alkyldihydroxyacetonephosphate synthase (ADPS)

Please make an inquiry.

Dye-decolorizing peroxidases (DyPs)

As alternatives for the plant and animal peroxidases, the newly discovered DyP-type peroxidases (DyPs) may offer advantages. Except for facilitating the production of peroxidases and eliminating the existence of isoforms, the ability to produce DyPs in a recombinant form also allows engineering of these biocatalysts. The first DyPs were identified less than two decades ago. DyPs are unrelated in sequence and structure to known peroxidases belonging to the plant or animal peroxidase superfamilies. DyPs are typically identified by their activity on anthraquinone dyes. While DyPs are efficient in degrading these synthetic dyes, the physiological substrates for DyPs are unclear and therefore their role in nature is enigmatic. Interestingly, recent studies suggest that bacterial DyPs may play an important role in the degradation of lignin which suggests that DyPs represent the bacterial counterparts of the fungal lignin peroxidases. Except for establishing their activity on synthetic dyes and possible role in lignin degradation, little data is available concerning their biocatalytic potential.

  1. TfuDyP Thermobifida fusca DyP
  2. SviDyP Saccharomonospora viridis DyP
  3. YfeX Escherichia coli DyP
  4. PfDyP Pseudomonas fluorescens DyP

We are also offering purified basic and acidic isoforms of horseradish peroxidase (HRP).

Epoxide hydrolases

Page is under construction. We are offering various thermostable and engineered epoxide hydrolases.

Please make an inquiry.

Flavin-containing monooxygenases (FMOs)

Flavin-containing monooxygenases are known for their broad substrate specificity and their ability to perform oxygenations of e.g. amines and sulfides. Some bacterial FMOs were shown to perform hydroxylation of indoles (MeFMO) while the human FMO5 was recently shown to be able to perform various Baeyer-Villiger oxidations. Below some of the GECCO FMOs are highlighted, while we also can offer other microbial FMOs.

  1. MeFMO – Methylophaga aminisulfidivorans flavin-containing monooxygenase, available in two formats: (1) recombinant MeFMO and (2) recombinant MeFMO fused to a cofactor recycling dehydrogenase (Org Biomol Chem. 2011 Mar 7;9(5):1337-41. doi: 10.1039/c0ob00988a)
  2. Rhodococcus jostii RHA1 flavin-containing monooxygenases: eight different FMOs belonging to class B monooxygenases (J Mol Cat B Enz 88, 2013, 20–25)
  3. Human FMO5 (ACS Chem Biol. 2016, 11(4):1039-48)

Laccases

Bacterial laccases have proven advantages over fungal and plant counterparts regarding wider pH optimum, higher stability and broader biocatalytic scope. We are offering Bacillus licheniformis ATCC 9945a laccase which exhibits remarkable thermostability and resitance to inactivation by organic solvents (https://doi.org/10.1016/j.molcatb.2016.06.005).