Epoxidation of short chain alkenes in Mycobacterium E20: The involvement of a specific mono-oxygenase

Bont, J De

doi:10.1016/0378-1097(79)90013-2

Cited by 38 publications

(27 citation statements)

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“…There are, however, no reports on the involvement of a particulate form of the alkene monooxygenase (AMO) in alkene-utilizers. Instability, together with a low monooxygenase activity has precluded purification to date (de Bont et al, 1979;Habets-Criitzen etal., 1984). Recently, partial purification of the components of AMO from Mycobacterium E3 was attempted.…”

Section: Discussionmentioning

confidence: 99%

“…Formation of epoxyethane by the soluble fraction was dependent on the presence of molecular oxygen and NADH. This is indicative of a typical monooxygenase reaction (Colby et al, 1977;de Bont et al, 1979). No activity was observed in the absence of molecular oxygen, NADH or with heat-killed extracts.…”

Section: The Involvem Ent Of a Specific M Onooxygenasementioning

confidence: 99%

“…The first intermediate in the metabolism of gaseous 1-alkenes is the corresponding 1,2-epoxyalkane formed by a NADH-dependent monooxygenase (de Bont et al, 1979Bont et al, & 1983. The further metabolism of epoxyethane may proceed via acetyl-CoA (de Bont & Harder, 1978;Wiegant & de Bont, 1980) and the metabolism of 1,2-epoxypropane via a Cj+Cj cleavage (Cerniglia et al, 1976).…”

Section: Alkene-utilizersmentioning

confidence: 99%

“…Mycobacterium E20 contains two monooxygenases (de Bont et al, 1979): an alkene monooxygenase induced by growth of the organism on ethene, produces optically active R-1,2-epoxypropane (ee=76%) and/?-1,2-epoxybutane (ee=62%), while the other enzyme is an alkane monooxygenase induced by growth on ethane, and produces racemic epoxyalkanes (Habets-Criitzen et al, 1985). In contrast, Nocardia corallina B276 forms chiral R-1,2-epoxypropane (ee=74%), R-1,2-epoxybutane (ee=68%) and R -1,2-epoxytetradecane (ee=86%) when alkane-grown.…”

Section: Alkene-utilizersmentioning

confidence: 99%

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Biocatalysts for production of chiral epoxides

Mahmoudian

Michael

1992

Appl Microbiol Biotechnol

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An extensive screen for microorganisms capable of growth on olefins was carried out. Over 100 bacterial strains (mesophilic, thermophilic) were isolated in pure culture with gaseous or liquid (internal & terminal) olefins as the sole source of carbon and energy. The organisms included Aero coccus, Aeromonas,Alcaligenes, Flavobacterium, Micrococcus, Moraxella, Nocardia, Pseudomonas, Staphylococcus, Streptomyces and Vibrio spp. and a variety of Gram-negative, Gram-positive and Gram-variable rods/coccobacilli not yet identified. Given the success of isolating many different genera of alkene-utilizing bacteria, it would suggest that the ability to utilize olefin hydrocarbons is more widespread in nature than previously recognized.Initial studies involved testing a collection of strains for i) growth rate on the substrate of isolation and ii) evidence of epoxide accumulation from lower gaseous olefins. All of the 18 ethene-and propene-utilizing bacteria tested, stereospecifically formed R-1,2-epoxypropane (ee=90-96%), R -l,2-epoxybutane (ee=90-98%) and trans-(2/?,37?)-epoxybutane (ee=64-88%), as analyzed by chiral complexation glc. A particularly promising strain of Micrococcus sp. M90C was selected to demonstrate: a) Induction of epoxidation activity in carbohydrate-grown cells. b) Optimization of a biotransformation process for production of epoxyethane. c) Involvement of a specific monooxygenase in the formation of chiral epoxides. d) Stereoselectivity of epoxyalkane degradation. e) Substrate specificity toward a range of olefins.Micrococcus sp. M90C stereospecifically formed S-(+)-phenyl glycidyl ether (ee=93%) and /?-(+)-phenyl methyl sulphoxide (ee>98%), as analyzed by chiral-shift NMR and HPLC. The ability to catalyze heteroatom oxygenation as well as epoxidation of a wide range of olefins in high optical and chemical yields, demonstrates its potential as a 'general-purpose' biocatalyst for the production of optically pure oxygenated compounds.Two other promising ethene-utilizing bacteria (M26, M93 A) each catalyzed the stereospecific formation of S-(+)-phenyl glycidyl ether (ee=93%). This has attracted considerable industrial interest and is currently under investigation at ICI for commercial production of optically active./1-blockers. In addition to Micrococcus sp. M90C, the substrate specificities of 6 other organisms were studied in order to probe the active site of the enzymes involved. The pattern of reactivity for the group of 4 ethene-(M26, M90C, M93A, M186) and 2 propene-(M142, M l 56) utilizers differed from that expected with peracids, suggesting a considerable degree of enzymatic control.The nature of the substrate, however, modulated enzymatic epoxidations in Staphylcoccus sp. M97B. CONTENTS

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Section: Discussionmentioning

confidence: 99%

Section: The Involvem Ent Of a Specific M Onooxygenasementioning

confidence: 99%

Section: Alkene-utilizersmentioning

confidence: 99%

Section: Alkene-utilizersmentioning

confidence: 99%

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Biocatalysts for production of chiral epoxides

Mahmoudian

Michael

1992

Appl Microbiol Biotechnol

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“…De Bont & Harder (1978) demonstrated that the initial step in ethene metabolism in Mycobacterium E20 was the oxidation of ethene to epoxyethane by alkene monooxygenase (AMO). Low activities of AM0 were also detected in crude extracts of Mycobacterium E20 (de Bont et al, 1979).…”

Section: Introductionmentioning

confidence: 96%

Alkene monooxygenase from Mycobacterium: a multicomponent enzyme

Hartmans

Weber²,

Somhorst³

et al. 1991

Journal of General Microbiology

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A NADH-or NADPH-dependent alkene monooxygenase (AMO) activity has been detected in cell-free extracts of the ethene-utilizing Mycobacterium E3 and Mycobacterium uurum L1. The activity was not linear with protein concentration in the assay suggesting AM0 is a multicomponent enzyme. The inhibition pattern of AM0 activity was very similar to the inhibition patterns published for the three-component soluble methane monooxygenases. Fractionation of crude extracts revealed that combination of two fractions was required to restore alkene monooxygenase activity. The first fraction was inhibited by acetylene, indicating it contained an oxygenase component. The second fraction contained reductase activity which was absent from non-induced cells. This reductase activity is probably the NADH-acceptor reductase of AMO.

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Oxygenation of CH and CC Bonds

Flitsch¹,

Grogan²,

Ashcroft³

2002

Enzyme Catalysis in Organic Synthesis

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Reactions catalyzed by oxygenase enzymes (mono or dioxygenases) are interesting for applications in organic synthesis. There are numerous examples of such reactions in biological systems, yet there are few chemical reagents or catalysts that can compete with biocatalysts. Examples of monoxygenases catalyzed biotransformations are shown in Figure 16.1-1. These include heteroatom oxygenation, aromatic hydroxylation, Bayer-Villiger oxidation, double-bond epoxidation and hydroxylation of nonactivated hydrocarbon atoms. The latter can occur with regio-, stereo-,

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Epoxidation of short chain alkenes in Mycobacterium E20: The involvement of a specific mono-oxygenase

Cited by 38 publications

References 10 publications

Biocatalysts for production of chiral epoxides

Biocatalysts for production of chiral epoxides

Alkene monooxygenase from Mycobacterium: a multicomponent enzyme

Oxygenation of CH and CC Bonds

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