Microbial Baeyer–Villiger Oxidation of Prochiral Polysubstituted Cyclohexanones by Recombinant Whole‐Cells Expressing Two Bacterial Monooxygenases

Mihovilovic, Marko D.; Rudroff, Florian; Grötzl, Birgit; Stanetty, Peter

doi:10.1002/ejoc.200400676

Cited by 35 publications

(21 citation statements)

References 61 publications

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“…The efficient conversions and excellent enantioselectivities obtained for lactones 13b-17b are in agreement with previous observations for CHMO-type enzymes [10,17,22,23] and indicate that at least the tested substituents in the 4-positions of 3,5-dimethylcyclohexanones impose no spatial limitations on this BVMO.…”

Section: Substrate Acceptance Profile Of the Chmo From Xanthobacter Ssupporting

confidence: 89%

Stereoselective Desymmetrizations by Recombinant Whole Cells Expressing the Baeyer–Villiger Monooxygenase from Xanthobacter sp. ZL5: A New Biocatalyst Accepting Structurally Demanding Substrates

et al. 2008

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In this work the substrate profile and stereoselectivity of engineered whole cells overexpressing the Baeyer–Villiger monooxygenase from Xanthobacter sp. ZL5 with respect to biotransformations of prochiral substrates is characterized. This enzyme catalyzes the desymmetrization of cyclic ketones bearing different chemical features with stereoselectivity similar to that obtained with a related protein fromAcinetobacter as a prototype representative of the cyclohexanone monooxygenase enzyme cluster. Moreover, this biocatalyst is able to convert sterically demanding substrates previously not transformed by other enzymes with excellent enantioselectivities. These results expand the repertoire of optically pure lactones accessible by whole‐cell biotransformation processes, which are useful intermediates for the synthesis of natural and bioactive products. In addition, we observed a remarkable epoxidation reaction of a non‐activated C=C bond catalyzed by this monooxygenase.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)

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Section: Substrate Acceptance Profile Of the Chmo From Xanthobacter Ssupporting

confidence: 89%

Stereoselective Desymmetrizations by Recombinant Whole Cells Expressing the Baeyer–Villiger Monooxygenase from Xanthobacter sp. ZL5: A New Biocatalyst Accepting Structurally Demanding Substrates

et al. 2008

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“…The ring hydroxy group in 5 was found to be in an axial position on the basis of interpretation of chemical shift and coupling constant data from the H-5 carbinol proton [δ H 3.71 (br s, the width of the peak ≈ 10 Hz)]. 15 Mosher acylation of 5 with R-and S-MTPA-Cl yielded the bis-S-and R-MTPA esters (8a and 8b). Analysis of 1 H chemical shifts in the 1D 1 H NMR and gCOSY spectra of the esters allowed calculation of Δδ S-R values and established the absolute configurations of C-2 as S and C-12 as R ( Figure 6).…”

Section: Resultsmentioning

confidence: 99%

Salinipyrones and Pacificanones, Mixed-Precursor Polyketides from the Marine Actinomycete Salinispora pacifica

Gontang

Kauffman

et al. 2008

J. Nat. Prod.

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Chemical examination of a phylogenetically unique strain of the obligate marine actinomycete Salinispora pacifica led to the discovery of four new polyketides, salinipyrones A and B (1, 2) and pacificanones A and B (3, 4). These compounds appear to be derived from a mixed-precursor polyketide biosynthesis involving acetate, propionate, and butyrate building blocks. Spectral analysis, employing NMR, IR, UV, and CD methods and chemical derivatization, was used to assign the structures and absolute configurations of these new metabolites. Salinipyrones A and B displayed exactly opposite CD spectra, indicating their pseudoenantiomeric relationship. This relationship was shown to be a consequence of the geometric isomerization of one double bond. The phenomenon of polyketide module skipping is proposed to explain the unusual biosynthesis of the salinipyrones and the pacificanones.The existence of actinomycetes indigenous to the marine environment has been debated, 1 but recent research results have shown that the ocean is indeed a rich habitat for these chemically prolific microorganisms. Although their ecological roles in the marine environment remain largely unknown, some marine actinomycetes are adapted to live in seawater, some are found in association with invertebrate hosts, while others have been recovered from the deepest ocean trenches. As an example, a salt-dependent pelagic marine actinomycete belonging to the family Nocardioidaceae was recently identified in surface sea water. 2 Marine invertebrates, especially sponges, are now well-known as hosts for diverse bacterial assemblages and represent rich sources for novel actinobacteria. 3 From marine sediments, we recently reported the first obligate marine actinomycete genus, the Salinispora ,4 which has proven to be a prolific source of secondary metabolites. 5 Our continuing research on Salinispora diversity, based upon comprehensive comparisons of 16S rDNA sequence data, has resulted in the cultivation of a third Salinispora species for which the name Salinispora pacifica has been proposed. 6 An investigation of the secondary metabolites produced by S. pacifica led to the isolation of the structurally novel metabolites cyanosporasides A and B, which raised intriguing questions about the genetic capacity of Salinispora strains to produce enediyne antibiotics. 7 Further genetic analysis of other S. pacifica strains collected from Palau 8 revealed a new phylotype (strain CNS-237) that differed from the cyanosporaside-producing strains at only three nucleotide positions (16S rRNA gene). 9 Chemical screening of this strain by LC-MS analysis indicated that a secondary metabolite profile was quite different from those of the other S. pacifica phylotypes.* To whom correspondence should be addressed. Tel: (858) 534-2133. Fax: (858) 534-1318. wfenical@ucsd.edu. Supporting Information Available: 1 H, 13 C, and 2D NMR spectra of 1-5, 1 H NMR data for the MTPA esters 6a and 6b, LC/MS traces of CNS-237, and additional discussion about the relative configurati...

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“…100 n.a. 45 [9] 8 Me, Et 79 (-) 100 75 (-) 91 [8] 27 (-) 100 21 (-) 56 [9] 9 Me, OH' [b] 86 (-) 100 86 (-) 48 [10] 80 (+) 100 76(+) 54 [10] 10 Me, Phe' 42 (-) 25 n.c. [9,11] n.c. n.c. [9] 11 H (X=C) 98 (-) 100 99 (-) 65 [12] 81 (+) 100 91(+) 58 [12] 12 =CH2 (X=C) 83 (+) 100 92(+) 54 [12] 73 (-) 100 99 (-) 63 [12] 13 cyclopropyl (X=C) >99 (+) 100 99 (+) 57 [12] n.c. n.c. [12] 14 trans-OH (X=C) 97(+) 100 96 (+) 80 [12] n.c. n.c. [12] 15 X=O 99 (-) 100 99 (-) 80 [13] n.c. n.c. [13] 16 Ph 38(-) 100 43 (-) 70 [14] 11 (+) 100 37(+) 66 [15] 17 4-Cl-Ph 62(+) 100 85 (+) 88 [16] 6 (+) 53 44 (+) 78 [15] 18 Bn 72(-) 100 82 (-) 57 [17] 28(-) 100 31(-) 37 [15] 19 3,4-(OCH2O)-Bn 96 (-) 100 95 (-) 83 [14] 41 (-) 100 40(-) 56 [15] 20 Butyl 15 100 17 62 [15] 76 (-) 100 76 (-) 72 [15] 21 endo >CHCl 98 (-) 58 80 (-) 75 [18] 46 (+) 100 60(+) 79 [18] 22 n.c. n.c. [10] 97 (+) 58 95 (+) 70 [10] 23 -C3H6-n.d. 23 [c] 97 (+) [d] 80 [19] n.d. n.d.…”

Section: General Protocol For Ce Biotransformationsunclassified

Self‐Sufficient Baeyer–Villiger Monooxygenases: Effective Coenzyme Regeneration for Biooxygenation by Fusion Engineering

et al. 2008

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Two‐in‐one biocatalysts were engineered by the covalent fusion of NADPH‐dependent Baeyer–Villiger monooxygenases to a phosphite dehydrogenase for coenzyme regeneration (see scheme). Not only the purified fusion proteins, but also whole cells and crude cell extracts containing the enzyme conjugates, could be used to catalyze biotransformations with high efficiency. NADP+=nicotinamide adenine dinucleotide phosphate.

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Microbial Baeyer–Villiger Oxidation of Prochiral Polysubstituted Cyclohexanones by Recombinant Whole‐Cells Expressing Two Bacterial Monooxygenases

Cited by 35 publications

References 61 publications

Stereoselective Desymmetrizations by Recombinant Whole Cells Expressing the Baeyer–Villiger Monooxygenase from Xanthobacter sp. ZL5: A New Biocatalyst Accepting Structurally Demanding Substrates

Stereoselective Desymmetrizations by Recombinant Whole Cells Expressing the Baeyer–Villiger Monooxygenase from Xanthobacter sp. ZL5: A New Biocatalyst Accepting Structurally Demanding Substrates

Salinipyrones and Pacificanones, Mixed-Precursor Polyketides from the Marine Actinomycete Salinispora pacifica

Self‐Sufficient Baeyer–Villiger Monooxygenases: Effective Coenzyme Regeneration for Biooxygenation by Fusion Engineering

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