Camphor-grown Pseudomonas putida, a multifunctional biocatalyst for undertaking Baeyer-Villiger monooxygenase-dependent biotransformations

Camphor Pathway Redux: Functional Recombinant Expression of 2,5- and 3,6-Diketocamphane Monooxygenases of Pseudomonas putida ATCC 17453 with Their Cognate Flavin Reductase Catalyzing Baeyer-Villiger Reactions

“…Suffice it to say that the camE and camG genes and the camE and camE 36 genes are predicted to be divergently transcribed per the position on the opposite DNA strand. Interestingly, this supports an earlier observation that the MO1 (mixtures of 2,5-and 3,6-DKCMO) and MO2 (OTEMO) activities are not "coordinately controlled" (27).…”

“…A mixture of the 2,5-DKCMO and 3,6-DKCMO enzymes has been referred to as MO1 to distinguish it from the MO2 activity of 2-oxo-⌬ 3 -4,5,5-trimethylcyclopentenylacetyl-coenzyme A (CoA) monooxygenase (OTEMO), a type 1 BVMO (15,(26)(27)(28)(29). Importantly, each DKCMO enzyme was shown to have absolute specificity for substrates of the respective enantiomeric series of camphor ketones and was also shown to have useful enantioselective properties (27,(30)(31)(32)(33). These enzymes are also active on the respective camphor enantiomers (13,14,34).…”

Cloning, Baeyer-Villiger Biooxidations, and Structures of the Camphor Pathway 2-Oxo-Δ 3 -4,5,5-Trimethylcyclopentenylacetyl-Coenzyme A Monooxygenase of Pseudomonas putida ATCC 17453

“…One of the earliest observations for biotransformations catalyzed by partially purified OTEMO (then known as MO2) was its selectivity for monocyclic substrates rather than bicyclic ketone such as bicyclo(2.2.1)heptan-2-one (25). The ability to transform some 2-alkyl cyclopentanones and 2-substituted cyclohexanones, in some cases resulting in excellent enantiomeric excesses (92 to 95%) and enantioselectivities (E values, 52 to 104), has also been reported (3,23).…”

“…1). The flavin adenine dinucleotide (FAD)-and NADPH-dependent 2-oxo-⌬ 3 -4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase (OTEMO), sometimes referred to as MO2 (25,63), was one of the first identified members of the type 1 ring-expanding Baeyer-Villiger (BV) monooxygenases (BVMOs) (EC 1.14.13.--), with the prototype and most studied BVMO being the cyclohexanone monooxygenase (CHMO) of Acinetobacter sp. strain NCIMB 9871 (55,61,63).…”

Monooxygenase-Mediated Baeyer−Villiger Oxidations

“…[110] Conversion of the racemic ketone 66a by 2,5-DKCMO gave regiodivergent oxidation to the ''normal'' lactone (1R,5S)-67a (89% ee) and the ''abnormal'' product (1S,5R)-68a (99% ee), while biotransformation with MO2 produced enantiomeric products with 35% ee and 95% ee, respectively. [143] The performance of isolated 2,5-and 3,6-DKCMO displayed similar enantiopreference for the conversion of this substrate type, with lower selectivity of the latter enzyme. [144] Whole-cell transformations furnished 86% total yield of (1R,5S)-67a (50% ee) and (1S,5R)-68a (Ͼ 95% ee).…”