Acetol monooxygenase from Mycobacterium Py1 cleaves acetol into acetate and formaldehyde

Hartmans, S

doi:10.1016/0378-1097(86)90303-4

Cited by 12 publications

(15 citation statements)

References 6 publications

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“…On the basis of the biochemical properties of acetol monooxygenase from Mycobacterium sp. strain Py1, this enzyme appears to be a BVMO (20). Therefore, it may be noteworthy to point out that two BVMOs are involved in two distinct catabolic pathways for acetone.…”

Section: Discussionmentioning

confidence: 91%

Novel Acetone Metabolism in a Propane-Utilizing Bacterium,Gordoniasp. Strain TY-5

et al. 2007

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In the propane-utilizing bacterium Gordonia sp. strain TY-5, propane was shown to be oxidized to 2-propanol and then further oxidized to acetone. In this study, the subsequent metabolism of acetone was studied. Acetone-induced proteins were found in extracts of cells induced by acetone, and a gene cluster designated acmAB was cloned on the basis of the N-terminal amino acid sequences of acetone-induced proteins. The acmA and acmB genes encode a Baeyer-Villiger monooxygenase (BVMO) and esterase, respectively. The BVMO encoded by acmA was purified from acetone-induced cells of Gordonia sp. strain TY-5 and characterized. The BVMO exhibited NADPH-dependent oxidation activity for linear ketones (C 3 to C 10 ) and cyclic ketones (C 4 to C 8 ). Escherichia coli expressing the acmA gene oxidized acetone to methyl acetate, and E. coli expressing the acmB gene hydrolyzed methyl acetate. Northern blot analyses revealed that polycistronic transcription of the acmAB gene cluster was induced by propane, 2-propanol, and acetone. These results indicate that the acmAB gene products play an important role in the metabolism of acetone derived from propane oxidation and clarify the propane metabolism pathway of strain TY-5 (propane 3 2-propanol 3 acetone 3 methyl acetate 3 acetic acid ؉ methanol). This paper provides the first evidence for BVMO-dependent acetone metabolism.Gordonia sp. strain TY-5 is an actinomycete that is capable of aerobic growth on gaseous propane as a carbon and energy source. Our previous study showed that propane is oxidized to 2-propanol by monooxygenase-mediated subterminal oxidation and then 2-propanol is further metabolized to acetone by three distinct NAD ϩ -dependent secondary alcohol dehydrogenases (27). Although n-alkanes can be metabolized to the corresponding ketones through subterminal oxidation in some bacteria, microbial metabolism of the downstream ketone is poorly understood (1,2,22,36,46,47). A variety of bacteria, including Gordonia sp. strain TY-5, are able to utilize acetone as a source of carbon and energy. Previous studies on bacterial acetone metabolism both in vivo and in vitro suggested that acetone can be metabolized in two ways. In most aerobic bacteria, acetone was hydroxylated by an O 2 -dependent reaction producing acetol (hydroxyacetone), although the corresponding enzyme system is not known (13,29,42,45). For most anaerobes (and some aerobes), acetone undergoes CO 2 -dependent carboxylation, yielding acetoacetate. Recently, the enzyme responsible for the latter reaction, acetone carboxylase (EC 6.4.1.6), has been purified and characterized (3,12,15,(39)(40)(41).This study was conducted to characterize acetone metabolism in propane-utilizing Gordonia sp. strain TY-5 at the enzymatic and gene levels. We first identified two acetone-induced proteins and cloned their corresponding genes, acmA and acmB. Subsequently, we showed that acetone is oxidized to methyl acetate by a novel Baeyer-Villiger monooxygenase (BVMO) (acmA gene product) and that the methyl acetate produced was hydrol...

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Section: Discussionmentioning

confidence: 91%

Novel Acetone Metabolism in a Propane-Utilizing Bacterium,Gordoniasp. Strain TY-5

et al. 2007

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“…2H20. Maintenance of strains, culture harvesting and storage of harvested cells were as previously described (Hartmans & de Bont, 1986). …”

Section: Methodsmentioning

confidence: 99%

“…Crude cell extracts were prepared as described previously (Hartmans & de Bont, 1986) except that 10% (v/v) glycerol (87 %) was added before sonication. All chromatographic steps were done at 4 "C. Dialysis of crude extracts was done overnight at 4 "C against 200 vols 50 mM-potassium phosphate buffer, pH 7.3, with 8.7% glycerol (buffer A).…”

Section: Preparation Of Cell Extractsmentioning

confidence: 99%

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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“…When CAA was used as a carbon source it was sterilized separately by filtration and added at a concentration of 5 mM. Culture conditions, maintenance of strains, culture harvesting and storage of harvested cells were as previously described (Hartmans & de Bont, 1986). …”

Section: Introductionmentioning

confidence: 99%

“…Crude cell extracts and dialysed extracts were prepared as described previously (Hartmans & de Bont, 1986). …”

Section: Introductionmentioning

confidence: 99%

Bacterial metabolism of 3-chloroacrylic acid

Hartmans

Jansen

Werf

et al. 1991

Journal of General Microbiology

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Two bacterial strains were isolated with 3-chloroacrylic acid (CAA) as sole source of carbon and energy. Strain CAA1, a Pseudomonas cepaciu sp., was capable of growth with only the cis-isomer of CAA. Strain CAA2, a coryneform bacterium, utilized both isomers of CAA as sole source of carbon and energy. Strain CAAl contained cis-CAA hydratase and strain CAA2 contained two hydratases, one with cis-CAA hydratase activity and one with ?vans-CAA hydratase activity. The product of the hydratase activities with CAA was malonate semialdehyde. In both strains malonate semialdehyde was subsequently decarboxylated by a cofactor-independent decarboxylase yielding acetaldehyde and C02.

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Acetol monooxygenase from Mycobacterium Py1 cleaves acetol into acetate and formaldehyde

Cited by 12 publications

References 6 publications

Novel Acetone Metabolism in a Propane-Utilizing Bacterium,Gordoniasp. Strain TY-5

Novel Acetone Metabolism in a Propane-Utilizing Bacterium,Gordoniasp. Strain TY-5

Alkene monooxygenase from Mycobacterium: a multicomponent enzyme

Bacterial metabolism of 3-chloroacrylic acid

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