Microbial Baeyer–Villiger oxidation of terpenones by recombinant whole-cell biocatalysts—formation of enantiocomplementary regioisomeric lactones

Černuchová, Petra; Mihovilovic, Marko D.

doi:10.1039/b703175k

Cited by 58 publications

(33 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…More specifically, members of the CHMO family are known to give S-lactones in high enantiomeric excesses, while members of the CPMO family give R-lactones of moderate optical purity, as also shown in Table 2. CHMO-type enzymes also showed regiodivergent oxidations to both "normal" and "abnormal" lactones, depending on the absolute configuration of the ketone precursors, whereas CPMO-type BVMOs usually yielded abnormal lactone products (11).…”

Section: Discussionmentioning

confidence: 99%

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

Leisch

Shi

Große

et al. 2012

Appl Environ Microbiol

View full text Add to dashboard Cite

ABSTRACTA dimeric Baeyer-Villiger monooxygenase (BVMO) catalyzing the lactonization of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-coenzyme A (CoA), a key intermediate in the metabolism of camphor byPseudomonas putidaATCC 17453, had been initially characterized in 1983 by Ougham and coworkers (H. J. Ougham, D. G. Taylor, and P. W. Trudgill, J. Bacteriol. 153:140–152, 1983). Here we cloned and overexpressed the 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (OTEMO) inEscherichia coliand determined its three-dimensional structure with bound flavin adenine dinucleotide (FAD) at a 1.95-Å resolution as well as with bound FAD and NADP+at a 2.0-Å resolution. OTEMO represents the first homodimeric type 1 BVMO structure bound to FAD/NADP+. A comparison of several crystal forms of OTEMO bound to FAD and NADP+revealed a conformational plasticity of several loop regions, some of which have been implicated in contributing to the substrate specificity profile of structurally related BVMOs. Substrate specificity studies confirmed that the 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetic acid coenzyme A ester is preferred over the free acid. However, the catalytic efficiency (kcat/Km) favors 2-n-hexyl cyclopentanone (4.3 × 105M−1s−1) as a substrate, although its affinity (Km= 32 μM) was lower than that of the CoA-activated substrate (Km= 18 μM). In whole-cell biotransformation experiments, OTEMO showed a unique enantiocomplementarity to the action of the prototypical cyclohexanone monooxygenase (CHMO) and appeared to be particularly useful for the oxidation of 4-substituted cyclohexanones. Overall, this work extends our understanding of the molecular structure and mechanistic complexity of the type 1 family of BVMOs and expands the catalytic repertoire of one of its original members.

show abstract

Section: Discussionmentioning

confidence: 99%

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

Leisch

Shi

Große

et al. 2012

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…insertion of one atom of oxygen at the most‐ or least‐substituted position, respectively). BVMOs display a broad substrate scope,4, 5 which include cyclic ketones with a heteroatom,6, 7 macrocyclic ketones,8, 9, 10, 11 and substituted derivatives of various ring size (for example, terpene‐based substrates12, 13). 14, 15 BVMOs are also especially interesting in the synthesis of branched lactones, from which branched aliphatic polyesters with low glass transition temperatures can be made 16, 17, 18, 19, 20, 21, 22, 23, 24, 25…”

Section: Introductionmentioning

confidence: 99%

Application of a thermostable Baeyer–Villiger monooxygenase for the synthesis of branched polyester precursors

Delgove

Elford

Bernaerts

et al. 2018

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUNDIt is widely accepted that the poor thermostability of Baeyer–Villiger monooxygenases limits their use as biocatalysts for applied biocatalysis in industrial applications. The goal of this study was to investigate the biocatalytic oxidation of 3,3,5‐trimethylcyclohexanone using a thermostable cyclohexanone monooxygenase from Thermocrispum municipale (TmCHMO) for the synthesis of branched ϵ‐caprolactone derivatives as building blocks for tuned polymeric backbones. In this multi‐enzymatic reaction, the thermostable cyclohexanone monooxygenase was fused to a phosphite dehydrogenase (PTDH) in order to ensure co‐factor regeneration.RESULTSUsing reaction engineering, the reaction rate and product formation of the regio‐isomeric branched lactones were improved and the use of co‐solvents and the initial substrate load were investigated. Substrate inhibition and poor product solubility were overcome using continuous substrate feeding regimes, as well as a biphasic reaction system with toluene as water‐immiscible organic solvent. A maximum volumetric productivity, or space–time‐yield, of 1.20 g L‐1 h‐1 was achieved with continuous feeding of substrate using methanol as co‐solvent, while a maximum product concentration of 11.6 g L‐1 was achieved with toluene acting as a second phase and substrate reservoir.CONCLUSIONThese improvements in key process metrics therefore demonstrate progress towards the up‐scaled Baeyer–Villiger monooxygenase‐biocatalyzed synthesis of the target building blocks for polymer application. © 2018 The Authors. Journal of Chemical Technology & Biotechnology published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

show abstract

“…(À)-Menthone (39) was not converted by any of the tested BVMOs. 115 Other enantioselective regiodivergent BVMO-mediated oxidations have been reported for the oxidation of aliphatic ketones, 171 the N-protected GeismanÀWaiss lactone (138), 214 and 2-(cyanomethyl)cyclohexanone (139) 163 with recombinant whole cells expressing CHMO from either Acinetobacter NCIMB 9871 or the native strain Acinetobacter TD63.…”

Section: Bmentioning

confidence: 99%

“…The formation of enantiocomplementary regioisomeric lactones from terpenones by several recombinant whole cell expression systems of BVMOs was investigated in more detail by the group of Mihovilovic and will be discussed in section 4.5.5 of this review. 68,115 4.3. Degradation of Linear, Cyclic, and Aromatic Ketones…”

mentioning

confidence: 99%

Baeyer−Villiger Monooxygenases: More Than Just Green Chemistry

2011

View full text Add to dashboard Cite

Microbial Baeyer–Villiger oxidation of terpenones by recombinant whole-cell biocatalysts—formation of enantiocomplementary regioisomeric lactones

Abstract: Recombinant whole-cell expression systems for Baeyer-Villiger monooxygenases of various bacterial origin were utilized in the regiodivergent biooxidation of cyclic terpenones enabling access to enantio- and regioisomeric lactones on preparative scale.

Cited by 58 publications

References 43 publications

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

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

Application of a thermostable Baeyer–Villiger monooxygenase for the synthesis of branched polyester precursors

Baeyer−Villiger Monooxygenases: More Than Just Green Chemistry

Contact Info

Product

Resources

About

Microbial Baeyer–Villiger oxidation of terpenones by recombinant whole-cell biocatalysts—formation of enantiocomplementary regioisomeric lactones

Abstract: Recombinant whole-cell expression systems for Baeyer-Villiger monooxygenases of various bacterial origin were utilized in the regiodivergent biooxidation of cyclic terpenones enabling access to enantio- and regioisomeric lactones on preparative scale.

Cited by 58 publications

References 43 publications

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

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

Application of a thermostable Baeyer–Villiger monooxygenase for the synthesis of branched polyester precursors

Baeyer−Villiger Monooxygenases: More Than Just Green Chemistry

Contact Info

Product

Resources

About

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

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