Enantioselective oxidation by a cyclohexanone monooxygenase from the xenobiotic-degrading Polaromonas sp. strain JS666

Alexander, Anne K.; Biedermann, David; Fink, Michael; Mihovilovic, Marko D.; Mattes, Timothy E.

doi:10.1016/j.molcatb.2012.03.002

Cited by 12 publications

(6 citation statements)

References 34 publications

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“…Transcriptomics and proteomics indicate that cDCE causes upregulation of several genes that are candidates for encoding the competing initial reactions (13). Transcriptomics previously indicated that cyclohexanone monooxygenase is upregulated in JS666 grown on cDCE (13), and there is modest consumption of cyclohexanone by cDCE-grown cells (Table 1); however, the enzyme does not appear to be directly involved in cDCE degradation (65). Three lines of evidence support this conclusion.…”

Section: Discussionmentioning

confidence: 98%

Cytochrome P450 Initiates Degradation ofcis-Dichloroethene by Polaromonas sp. Strain JS666

Nishino

Shin

Gossett

et al. 2013

Appl Environ Microbiol

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bPolaromonas sp. strain JS666 grows on cis-1,2-dichoroethene (cDCE) as the sole carbon and energy source under aerobic conditions, but the degradation mechanism and the enzymes involved are unknown. In this study, we established the complete pathway for cDCE degradation through heterologous gene expression, inhibition studies, enzyme assays, and analysis of intermediates. Several lines of evidence indicate that a cytochrome P450 monooxygenase catalyzes the initial step of cDCE degradation. Both the transient accumulation of dichloroacetaldehyde in cDCE-degrading cultures and dichloroacetaldehyde dehydrogenase activities in cell extracts of JS666 support a pathway for degradation of cDCE through dichloroacetaldehyde. The mechanism minimizes the formation of cDCE epoxide. The molecular phylogeny of the cytochrome P450 gene and the organization of neighboring genes suggest that the cDCE degradation pathway recently evolved in a progenitor capable of degrading 1,2-dichloroethane either by the recruitment of the cytochrome P450 monooxygenase gene from an alkane catabolic pathway or by selection for variants of the P450 in a preexisting 1,2-dichloroethane catabolic pathway. The results presented here add yet another role to the broad array of productive reactions catalyzed by cytochrome P450 enzymes.

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Section: Discussionmentioning

confidence: 98%

Cytochrome P450 Initiates Degradation ofcis-Dichloroethene by Polaromonas sp. Strain JS666

Nishino

Shin

Gossett

et al. 2013

Appl Environ Microbiol

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“…strain HI-70 (Fink et al 2011 ; Iwaki et al 2006 ), and CHMO from Polaromonas sp. strain JS666 (Alexander et al 2012 ). Therefore, the strict selection against substituents in position 3 and 4 of the ring seems to be a unique behavior of BVMO Lepto since to the best of our knowledge, such clear selectivity has never been reported for another BVMO before.…”

Section: Discussionmentioning

confidence: 99%

“…The HAPMO from P. fluorescens ACB is the phylogenetically closest BVMO that has been evaluated on ketones 31 and 32 ; this enzyme showed modest yield and ee for the desymmetrization of 31 and 32 (Mihovilovic et al 2005a ). However, the CHMO-type enzymes, which belong to the phylogenetic group III, readily catalyze the desymmetrization of prochiral ketones 31 – 33 to the corresponding lactones with high ee (Alexander et al 2012 ; Alphand et al 1998 ; Rial et al 2008a ; Rudroff et al 2007 ). The racemic cis -bicyclo[3.2.0]hept-2-en-6-one ( 34 ) is a well-known substrate for CHMO from Acinetobacter sp.…”

Section: Discussionmentioning

confidence: 99%

“…The racemic cis -bicyclo[3.2.0]hept-2-en-6-one ( 34 ) is a well-known substrate for CHMO from Acinetobacter sp. NCIMB 9871 and for many other BVMOs (Alexander et al 2012 ; Alphand and Furstoss 1992 ; Ferroni et al 2014 ; Fink et al 2011 ; Mihovilovic et al 2005b , 2008 ; Rial et al 2008b ). After 24 h, the BVMO Lepto oxidized this racemic substrate almost completely to equal amounts of normal and abnormal lactones (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa

et al. 2017

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Baeyer–Villiger monooxygenases are recognized by their ability and high selectivity as oxidative biocatalysts for the generation of esters or lactones using ketones as starting materials. These enzymes represent valuable tools for biooxidative syntheses since they can catalyze reactions that otherwise involve strong oxidative reagents. In this work, we present a novel enzyme, the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa. This protein is phylogenetically distant from other well-characterized BVMOs. In order to study this new enzyme, we cloned its gene, expressed it in Escherichia coli and characterized the substrate scope of the Baeyer–Villiger monooxygenase from L. biflexa as a whole-cell biocatalyst. For this purpose, we performed the screening of a collection of ketones with variable structures and sizes, namely acyclic ketones, aromatic ketones, cyclic ketones, and fused ketones. As a result, we observed that this biocatalyst readily oxidized linear- and branched- medium-chain ketones, alkyl levulinates and linear ketones with aromatic substituents with excellent regioselectivity. In addition, this enzyme catalyzed the oxidation of 2-substituted cycloketone derivatives but showed an unusual selection against substituents in positions 3 or 4 of the ring.Electronic supplementary materialThe online version of this article (doi:10.1186/s13568-017-0390-5) contains supplementary material, which is available to authorized users.

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“…ZL5 (CHMO Xantho ) have a very broad substrate acceptance profile and the ability to convert some bulky ketones not accepted by other BVMOs (Rial et al, 2008a , b ). More recently, Alexander et al ( 2012 ) reported the cloning and evaluation of a CHMO from the xenobiotic-degrading Polaromonas sp. JS666.…”

Section: Baeyer-villiger Oxidationsmentioning

confidence: 99%

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications

2014

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External flavoprotein monooxygenases comprise a group of flavin-dependent oxidoreductases that catalyze the insertion of one atom of molecular oxygen into an organic substrate and the second atom is reduced to water. These enzymes are involved in a great number of metabolic pathways both in prokaryotes and eukaryotes. Flavoprotein monooxygenases have attracted the attention of researchers for several decades and the advent of recombinant DNA technology caused a great progress in the field. These enzymes are subjected to detailed biochemical and structural characterization and some of them are also regarded as appealing oxidative biocatalysts for the production of fine chemicals and valuable intermediates toward active pharmaceutical ingredients due to their high chemo-, stereo-, and regioselectivity. Here, we review the most representative reactions catalyzed both in vivo and in vitro by prototype flavoprotein monooxygenases, highlighting the strategies employed to produce them recombinantly, to enhance the yield of soluble proteins, and to improve cofactor regeneration in order to obtain versatile biocatalysts. Although we describe the most outstanding features of flavoprotein monooxygenases, we mainly focus on enzymes that were cloned, expressed and used for biocatalysis during the last years.

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Enantioselective oxidation by a cyclohexanone monooxygenase from the xenobiotic-degrading Polaromonas sp. strain JS666

Cited by 12 publications

References 34 publications

Cytochrome P450 Initiates Degradation ofcis-Dichloroethene by Polaromonas sp. Strain JS666

Cytochrome P450 Initiates Degradation ofcis-Dichloroethene by Polaromonas sp. Strain JS666

Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications

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