Heterologous expression of the methyl carbamate-degrading hydrolase MCD

Naqvi, Tatheer Alam; Cheesman, Matthew J.; Williams, Michelle R.; Campbell, Peter M.; Ahmed, Safia; Russell, Robyn J.; Scott, Colin; Oakeshott, John G.

doi:10.1016/j.jbiotec.2009.09.009

Cited by 23 publications

(24 citation statements)

References 50 publications

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“…2009). MCD is a Mn 2+ ‐dependent enzyme, as demonstrated by chelator and reconstitution studies (Karns and Tomasek 1991; Naqvi et al. 2009).…”

Section: Insecticidal Carbamate Metabolizing Enzymesmentioning

confidence: 97%

“…2002) are esterases capable of hydrolysing the carboxylester bond of 1‐naphthyl acetate. Indeed, MCD hydrolyses 1‐naphthyl acetate 30 times faster than it does carbaryl, with a k cat value of 52 s −1 for 1‐naphthyl actetate (Naqvi et al. 2009).…”

Section: Insecticidal Carbamate Metabolizing Enzymesmentioning

confidence: 99%

“…MCD, CehA and CahA have all been described as possessing broad (although not identical) substrate ranges (Table 1). Interestingly, MCD has been demonstrated to have low (promiscuous) levels of PTE activity, with a k cat / K m for dimethyl umbelliferyl phosphate of 3 × 10 −3 , 10 7 times lower than its k cat / K m for carbaryl (Naqvi et al. 2009).…”

Section: Insecticidal Carbamate Metabolizing Enzymesmentioning

confidence: 99%

“…Both MCD from Achromobacter WM111 (Derbyshire et al 1987) and CehA from Rhizobium sp AC100 (Hashimoto et al 2002) are esterases capable of hydrolysing the carboxylester bond of 1-naphthyl acetate. Indeed, MCD hydrolyses 1-naphthyl acetate 30 times faster than it does carbaryl, with a k cat value of 52 s )1 for 1-naphthyl actetate (Naqvi et al 2009). MCD is a Mn 2+ -dependent enzyme, as demonstrated by chelator and reconstitution studies (Karns and Tomasek 1991;Naqvi et al 2009).…”

Section: Bacterial Enzymesmentioning

confidence: 99%

“…Indeed, MCD hydrolyses 1-naphthyl acetate 30 times faster than it does carbaryl, with a k cat value of 52 s )1 for 1-naphthyl actetate (Naqvi et al 2009). MCD is a Mn 2+ -dependent enzyme, as demonstrated by chelator and reconstitution studies (Karns and Tomasek 1991;Naqvi et al 2009). The catalytic machinery of CehA remains a mystery, as it is inhibited by neither serine hydrolase inhibitors nor chelators, and contains no recognizable catalytic motif (Bornscheuer 2002).…”

Section: Bacterial Enzymesmentioning

confidence: 99%

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The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide‐resistant insects

Russell

Scott

Jackson

et al. 2011

Evolutionary Applications

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Here, we compare the evolutionary routes by which bacteria and insects have evolved enzymatic processes for the degradation of four classes of synthetic chemical insecticide. For insects, the selective advantage of such degradative activities is survival on exposure to the insecticide, whereas for the bacteria the advantage is simply a matter of access to additional sources of nutrients. Nevertheless, bacteria have evolved highly efficient enzymes from a wide variety of enzyme families, whereas insects have relied upon generalist esterase-, cytochrome P450- and glutathione-S-transferase-dependent detoxification systems. Moreover, the mutant insect enzymes are less efficient kinetically and less diverged in sequence from their putative ancestors than their bacterial counterparts. This presumably reflects several advantages that bacteria have over insects in the acquisition of new enzymatic functions, such as a broad biochemical repertoire from which new functions can be evolved, large population sizes, high effective mutation rates, very short generation times and access to genetic diversity through horizontal gene transfer. Both the insect and bacterial systems support recent theory proposing that new biochemical functions often evolve from ‘promiscuous’ activities in existing enzymes, with subsequent mutations then enhancing those activities. Study of the insect enzymes will help in resistance management, while the bacterial enzymes are potential bioremediants of insecticide residues in a range of contaminated environments.

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“…2009). MCD is a Mn 2+ ‐dependent enzyme, as demonstrated by chelator and reconstitution studies (Karns and Tomasek 1991; Naqvi et al. 2009).…”

Section: Insecticidal Carbamate Metabolizing Enzymesmentioning

confidence: 97%

Section: Insecticidal Carbamate Metabolizing Enzymesmentioning

confidence: 99%

Section: Insecticidal Carbamate Metabolizing Enzymesmentioning

confidence: 99%

Section: Bacterial Enzymesmentioning

confidence: 99%

Section: Bacterial Enzymesmentioning

confidence: 99%

See 3 more Smart Citations

The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide‐resistant insects

Russell

Scott

Jackson

et al. 2011

Evolutionary Applications

Self Cite

122

100

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Genetic and metabolic analysis of the carbofuran catabolic pathway in Novosphingobium sp. KN65.2

Nguyen

Helbling

Bers

et al. 2014

Appl Microbiol Biotechnol

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The widespread agricultural application of carbofuran and concomitant contamination of surface and ground waters has raised health concerns due to the reported toxic effects of this insecticide and its degradation products. Most bacteria that degrade carbofuran only perform partial degradation involving carbamate hydrolysis without breakdown of the resulting phenolic metabolite. The capacity to mineralize carbofuran beyond the benzofuran ring has been reported for some bacterial strains, especially sphingomonads, and some common metabolites, including carbofuran phenol, were identified. In the current study, the catabolism of carbofuran by Novosphingobium sp. KN65.2 (LMG 28221), a strain isolated from a carbofuran-exposed Vietnamese soil and utilizing the compound as a sole carbon and nitrogen source, was studied. Several KN65.2 plasposon mutants with diminished or abolished capacity to degrade and mineralize carbofuran were generated and characterized. Metabolic profiling of representative mutants revealed new metabolic intermediates, in addition to the initial hydrolysis product carbofuran phenol. The promiscuous carbofuran-hydrolyzing enzyme Mcd, which is present in several bacteria lacking carbofuran ring mineralization capacity, is not encoded by the Novosphingobium sp. KN65.2 genome. An alternative hydrolase gene required for this step was not identified, but the constitutively expressed genes of the unique cfd operon, including the oxygenase genes cfdC and cfdE, could be linked to further degradation of the phenolic metabolite. A third involved oxygenase gene, cfdI, and the transporter gene cftA, encoding a TonB-dependent outer membrane receptor with potential regulatory function, are located outside the cfd cluster. This study has revealed the first dedicated carbofuran catabolic genes and provides insight in the early steps of benzofuran ring degradation.

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Microbial elimination of carbamate pesticides: specific strains and promising enzymes

Sun

Zhang

et al. 2022

Appl Microbiol Biotechnol

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Heterologous expression of the methyl carbamate-degrading hydrolase MCD

Cited by 23 publications

References 50 publications

The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide‐resistant insects

The evolution of new enzyme function: lessons from xenobiotic metabolizing bacteria versus insecticide‐resistant insects

Genetic and metabolic analysis of the carbofuran catabolic pathway in Novosphingobium sp. KN65.2

Microbial elimination of carbamate pesticides: specific strains and promising enzymes

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