Cloning and biochemical characterization of Co2+-activated bromoperoxidase-esterase (perhydrolase) from Pseudomonas putida IF-3 strain

Kawanami, Takafumi; Liu, Jiquan; Dairi, Tohru; Miyakoshi, Masao; Nitta, C.; Kimoto, Yoshio

doi:10.1016/s0167-4838(00)00261-2

Cited by 16 publications

(19 citation statements)

References 37 publications

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“…In addition, MHlip displays significant identity (~30%) to various haloperoxidases and proteases. Although similarity between some esterases, oxidases and proteases was reported [29,35,36], MHlip does not show any detectable activity when tested for the conversion of the substrate phenol red to bromophenol blue [37] or azo-casein hydrolysis [38] (data not shown).…”

Section: Discussionmentioning

confidence: 94%

Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome

Berlemont

Jacquin

Delsaute

et al. 2013

Biology

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An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the α/β hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others. MHlip was produced, purified and its activity was determined. The substrate profile of MHlip reveals a high specificity for short p-nitrophenyl-esters. The apparent optimal activity of MHlip was measured for p-nitrophenyl-acetate, at 33 °C, in the pH range of 6–9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 °C. The biochemical characterization of this enzyme showed its adaptation to cold temperatures, even when it did not present evident signatures associated with cold-adapted proteins. Thus, MHlip adaptation to cold probably results from many discrete structural modifications, allowing the protein to remain active at low temperatures. Functional metagenomics is a powerful approach to isolate new enzymes with tailored biophysical properties (e.g., cold adaptation). In addition, beside the ever growing amount of sequenced DNA, the functional characterization of new catalysts derived from environment is still required, especially for poorly characterized protein families like α/β hydrolases.

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Section: Discussionmentioning

confidence: 94%

Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome

Berlemont

Jacquin

Delsaute

et al. 2013

Biology

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“…2b) and a variety of cellular roles. They exhibit signiWcant sequence similarities to bacterial chloride/bromide peroxidases (An09g00820) (Itoh et al 2001), plastic degradation enzymes (An09g00840), the multidrug transporter atrA of A. nidulans (An09g00850) (Del Sorbo et al 1997), the aXatoxin eZux pump aXT of A. parasiticus (An09g00870), an aminopeptidase (An09g00950) (Asano et al 1989), and the alpha-1 chain of Na + /K + -exchanging ATPases (An09g00930) (Yagawa et al 1990). Other ORFs putatively encode a putative tannase precursor (An09g00890) (Hatamoto et al 1996), an alpha-L-arbinofuranosidase (An09g00880) (Flipphi et al 1994), or a cutinase-domain containing enzyme (An09g00790).…”

Section: Resultsmentioning

confidence: 99%

Strain-specific retrotransposon-mediated recombination in commercially used Aspergillus niger strain

2008

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Transposons are usually present in multiple copies in their hosts' genomes. Recombination between two transposon copies can result in chromosomal rearrangements. Here, we describe a recombination event between two copies of the retrotransposon ANiTa1 within the genome of the fungus Aspergillus niger (strain CBS513.88). The observed chromosomal rearrangement appears to be strain-specific, as the corresponding genomic region in another strain, ATCC1015, shows a different organization. Strain ATCC1015 actually seems to lack full-length ANiTa1 copies and possesses only solo LTR sequences. Presumably strain ATCC1015 was once colonized by ANiTa1, but then the genome subsequently lost the ANiTa1 copies. The striking genomic differences in ANiTa1 copy distribution leading to differences in the chromosomal structure between the two strains, ATTC1015 and CBS513.88, suggest that the activity of transposons may profoundly affect the evolution of different fungal strains.

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“…Although the products of the enzyme reaction were not determined in this study, DCH was thought to convert peracetic acid to acetic acid and hydrogen peroxide because of the existing evidence that DCH and other perhydrolases are able to catalyse the reverse reaction, i.e. the formation of a peracetic acid from acetic acid and hydrogen peroxide [1,12,16,28] and because DCH could catalyse the halogenation reaction in the presence of not only acetic acid but also other organic acids, such as formic acid, propionic acid, and n ‐butyric acid [1]: peroxoacids corresponding to these organic acids might also serve as substrates of the enzyme.…”

Section: Discussionmentioning

confidence: 99%

Role of Acinetobacter calcoaceticus 3,4‐dihydrocoumarin hydrolase in oxidative stress defence against peroxoacids

Honda¹,

Kataoka²,

Sakuradani³

et al. 2003

European Journal of Biochemistry

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The physiological role of a bifunctional enzyme, 3,4-dihydrocoumarin hydrolase (DCH), which is capable of both hydrolysis of ester bonds and organic acid-assisted bromination of organic compounds, was investigated. Purified DCH from Acinetobacter calcoaceticus F46 catalysed dose-and time-dependent degradation of peracetic acid. The gene (dch) was cloned from the chromosomal DNA of the bacterium. The dch ORF was 831 bp long, corresponding to a protein of 272 amino acid residues, and the deduced amino acid sequence showed high similarity to those of bacterial serine esterases and perhydrolases. The dch gene was disrupted by homologous recombination on the A. calcoaceticus genome. The dch disruptant strain was more sensitive to growth inhibition by peracetic acid than the parent strain. On the other hand, the recombinant Escherichia coli cells expressing dch were more resistant to peracetic acid. A putative catalase gene was found immediately downstream of dch, and Northern blot hybridization analysis revealed that they are transcribed as part of a polycistronic mRNA. These results suggested that in vivo DCH detoxifies peroxoacids in conjunction with the catalase, i.e. peroxoacids are first hydrolysed to the corresponding acids and hydrogen peroxide by DCH, and then the resulting hydrogen peroxide is degraded by the catalase.Keywords: Acinetobacter calcoaceticus; catalase; 3,4-dihydrocoumarin hydrolase; perhydrolase; peroxoacid.In a previous study, we found and isolated a novel lactonohydrolase, 3,4-dihydrocoumarin hydrolase (DCH), from Acinetobacter calcoaceticus F46 [1]. The amino acid sequences of the N-terminal and internal peptide of DCH exhibited high similarity to those of several serine-hydrolases and perhydrolases (nonhaem haloperoxidases). Furthermore, the enzyme also showed both hydrolysis activity toward aromatic lactones, such as 3,4-dihydrocoumarin (Scheme 1), and organic acid-assisted bromination activity toward monochlorodimedon (2-chloro-5,5-dimethyl-1,3-cyclohexanedione).Perhydrolases were originally identified as the enzymes catalysing halogenation reactions of various organic compounds, because these enzymes catalyse the halogenation of various organic compounds in the presence of hydrogen peroxide, halide ions, and organic acids. Various perhydrolases have been isolated, mainly from Pseudomonas and Streptomyces species [2][3][4][5][6][7][8]. Several of these species are known to produce halogenated metabolites. Perhydrolases had been, as a result of this, thought to be involved in the synthesis of halogenated metabolites in vivo, and had been called Ônonhaem haloperoxidasesÕ, to distinguish them from the ÔtrueÕ haloperoxidases, which are haem-or vanadiumdependent enzymes [9]. However, there is now evidence that perhydrolases do not participate in the biosynthesis of halogenated compounds. A perhydrolase-deficient mutant of Pseudomonas fluorsecens yielded a chlorinated metabolite, pyrrolnitrin, like the parent strain [4], and the Streptomyces enzyme, which chlorinates tetracycline, is not relate...

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Cloning and biochemical characterization of Co2+-activated bromoperoxidase-esterase (perhydrolase) from Pseudomonas putida IF-3 strain

Cited by 16 publications

References 37 publications

Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome

Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome

Strain-specific retrotransposon-mediated recombination in commercially used Aspergillus niger strain

Role of Acinetobacter calcoaceticus 3,4‐dihydrocoumarin hydrolase in oxidative stress defence against peroxoacids

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