Phylogenetic diversity and characterization of 2-haloacid degrading bacteria from the marine sponge Hymeniacidon perlevis

Huang, Jing; Xin, Yanjuan; Cao, Xupeng; Zhang, Wei

doi:10.1007/s11274-010-0636-8

Cited by 15 publications

(7 citation statements)

References 39 publications

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“…The abundance of organohalogens in the marine environment makes algae and marine microbes a potential source of novel halogenase and dehalogenase enzymes. A recent study describes a number of species from the Rhodobacteraceae family that tested positive for haloacid dehalogenase activity . However, none of these l ‐HADs were structurally characterized.…”

Section: Introductionmentioning

confidence: 99%

Marine Rhodobacteraceae l‐haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water

et al. 2013

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The putative L-haloacid dehalogenase gene (DehRhb) from a marine Rhodobacteraceae family was cloned and overexpressed in Escherichia coli. The DehRhb protein was shown to be an L-haloacid dehalogenase with highest activity towards brominated substrates with short carbon chains ( C3). The optimal temperature for enzyme activity was 55°C, and the V max and K m were 1.75 lMÁmin À1 Ámg À1 of protein and 6.72 mM, respectively, when using monobromoacetic acid as a substrate. DehRhb showed moderate thermal stability, with a melting temperature of 67°C. The enzyme demonstrated high tolerance to solvents, as shown by thermal shift experiments and solvent incubation assays. The DehRhb protein was crystallized and structures of the native, reaction intermediate and substrate-bound forms were determined. The active site of DehRhb had significant differences from previously studied L-haloacid dehalogenases. The asparagine and arginine residues shown to be essential for catalytic activity in other L-haloacid dehalogenases are not present in DehRhb. The histidine residue which replaces the asparagine residue in DehRhb was coordinated by a conformationally strained glutamate residue that replaces a conserved glycine. The His/Glu dyad is positioned for deprotonation of the catalytic water which attacks the ester bond in the reaction intermediate. The catalytic water in DehRhb is shifted by~1.5 A from its position in other L-haloacid dehalogenases. A similar His/Glu or Asp dyad is known to activate the catalytic water in haloalkane dehalogenases. The DehRhb enzyme represents a novel member within the L-haloacid dehalogenase family and it has potential to be used as a commercial biocatalyst. DatabaseThe coordinates and structure factors of the crystal structures have been deposited in the Protein Data Bank with the codes 2yml, 2ymm, 2ymp, 2ymq and 2yn4. Nucleotide sequence data has been deposited in the GenBank database under the accession number JX868516.

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Section: Introductionmentioning

confidence: 99%

Marine Rhodobacteraceae l‐haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water

et al. 2013

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“…Eleven bacterial strains isolated from the marine sponge Hymeniacidon perlevis degraded 2-chloropropionic acid (2-CPA; Huang et al, 2011 ). Based on the 16S rRNA gene sequence analysis, they were clustered into the Rhodobacteraceae family of α-Proteobacteria and the Pseudomonadaceae family of γ-Proteobacteria.…”

Section: Marine Biocatalysts For Degrading Pahs and Halogenated Compomentioning

confidence: 99%

Marine-Derived Biocatalysts: Importance, Accessing, and Application in Aromatic Pollutant Bioremediation

et al. 2017

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The aim of the present review is to highlight the potential use of marine biocatalysts (whole cells or enzymes) as an alternative bioprocess for the degradation of aromatic pollutants. Firstly, information about the characteristics of the still underexplored marine environment and the available scientific tools used to access novel marinederived biocatalysts is provided. Marine-derived enzymes, such as dioxygenases and dehalogenases, and the involved catalytic mechanisms for the degradation of aromatic and halogenated compounds, are presented, with the purpose of underpinning their potential use in bioremediation. Emphasis is given on persistent organic pollutants (POPs) that are organic compounds with significant impact on health and environment due to their resistance in degradation. POPs bioaccumulate mainly in the fatty tissue of living organisms, therefore current efforts are mostly focused on the restriction of their use and production, since their removal is still unclear. A brief description of the guidelines and criteria that render a pollutant POP is given, as well as their potential biodegradation by marine microorganisms by surveying recent developments in this rather unexplored field.

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“…Pseudomonas stutzeri DEH138 which was isolated by Huang et al (2011) was cultured aerobically in the same minimal medium (MM) to Zhang et al (2013a), and 10 mM 2-CPA was supplemented as the sole carbon source for 47 h, which was used as the inoculum. All of the cultures were incubated in 100 ml medium in a 500-ml flask with the inoculation ratios of 1:20 at 30°C with shaking at 220 rev/min, unless stated otherwise.…”

Section: Microorganisms and Culture Conditionsmentioning

confidence: 99%

“…Pseudomonas stutzeri DEH138, isolated from the intertidal marine sponge Hymeniacidon perlevis (Huang et al 2011), is capable of using 2-chloropropionate (2-CPA) as sole carbon source which induces the expression of L-DEX. L-DEX with production and productivity 2.46 U and 0.05 U/h, respectively, was obtained when DEH138 was cultured for 48 h with 10 mM 2-CPA as sole carbon source.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of L-2-haloacid dehalogenase expression in Pseudomonas stutzeri DEH138 based on the different substrate specificity between dehalogenase-producing bacteria and their dehalogenases

Wang

Xin

Cao

et al. 2015

World J Microbiol Biotechnol

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There was no direct correlation in substrate specificity between the metabolism of Pseudomonas stutzeri DEH138 and its corresponding dehalogenase. Dehalogenase substrates that could be dehalogenated might not be degraded by DEH138 or vice versa. Basing on this, different approaches to enhance L-2-haloacid dehalogenase (L-DEX) production in DEH138 via the combination of non-halogenated compounds with different inducers were applied. The optimum approach to obtain more L-DEX from DEH138 was the combination of DL-lactate and DL-2-chlorobutyrate, with 5.7-fold greater production and 11.7-fold greater productivity of the enzyme after optimization.

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Phylogenetic diversity and characterization of 2-haloacid degrading bacteria from the marine sponge Hymeniacidon perlevis

Cited by 15 publications

References 39 publications

Marine Rhodobacteraceae l‐haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water

Marine Rhodobacteraceae l‐haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water

Marine-Derived Biocatalysts: Importance, Accessing, and Application in Aromatic Pollutant Bioremediation

Enhancement of L-2-haloacid dehalogenase expression in Pseudomonas stutzeri DEH138 based on the different substrate specificity between dehalogenase-producing bacteria and their dehalogenases

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