Dehalogenases for pollutant degradation in brief: A mini review

sefatullah Zakary, Habeebat Adekilekun Oyewusi, Fahrul Huyop

Abstract


Dehalogenases are microbial enzyme catalysed the cleavage of carbon-halogen bond of halogenated organic compounds. It has potential use in the area of biotechnology such as bioremediation and chemical industry. Halogenated organic compounds can be found in a considerable amount in the environment due to utilization in agriculture and industry, such as pesticides and herbicides. The presence of halogenated compound in the environment have been implicated on the health and natural ecosystem. Microbial dehalogenation is a significant method to tackle this problem. This review intends to briefly describe the microbial dehalogenases in relation to the environment where they are isolated. The basic information about dehalogenases in relation to dehalogenation mechanisms, classification, sources and the transportation of these pollutants into bacterial cytoplasm will be described. We also summarised readily available synthetic halogenated organic compound in the environment.


Keywords


Halogenated compounds, Haloacid dehalogenases, L-2-haloacid dehalogenase, Dehalogenation, haloacid dehalogenase type II

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References


Adamu A, Wahab RA, Aminu AH (2020) Haloacid

dehalogenases of Rhizobium sp. and related enzymes:

catalytic properties and mechanistic analysis. Process

Biochemistry 92: 437 – 446. doi:

1016/j.procbio.2020.02.002.

Häggblom MM, Bossert ID (2004) Halogenated organic

compounds-a global perspective, in Dehalogenation.

Springer. p. 3-29. doi: 10.1007/0-306-48011-5_1.

Gribble GW (2003) The diversity of naturally produced

organohalogens. Chemosphere 52 (2): 289-297. doi:

1016/s0045-6535(03)00207-8.

Edbeib MF, Wahab RA, Huyop FZ et al. (2020) Further

Analysis of Burkholderia pseudomallei MF2 and

Identification of Putative Dehalogenase Gene by PCR.

Indonesian Journal of Chemistry 20 (2): 86 – 394. doi:

S Zakary, HA Oyewusi, F Huyop, 2020 / Dehalogenases for pollutant degradation: A mini review

JTLS | Journal of Tropical Life Science 23 Volume 11 | Number 1 | January | 2021

22146/ijc.43262.

Kemf E (2013) GCO--Global Chemicals Outlook:

Towards Sound Management of Chemicals. United

Nations Environment Programme (UNEP): Nairobi,

Kenya: GPS Publishing.

Prüss-Ustün A, Vickers C, Haefliger P, Bertollini R

(2011) Knowns and unknowns on burden of disease due

to chemicals: a systematic review. Environmental

Health 10 (1): p. 9. doi: 10.1186/1476-069x-10-9

Haritash A, Kaushik C (2009) Biodegradation aspects of

polycyclic aromatic hydrocarbons (PAHs): a review.

Journal of Hazardous Materials 169 (1-3): 1-15. doi:

1016/j.jhazmat.2009.03.137.

Zhang X, Liu Y (2019) Halogenated organics generated

during online chemical cleaning of MBR: An emerging

threat to water supply and public health. Science of The

Total Environment 656: 547 – 549. doi:

1016/j.scitotenv.2018.11.410

Jensen H (1957) Decomposition of chloro-substituted

aliphatic acids by soil bacteria. Canadian Journal of

Microbiology 3 (2): 151-164. doi: 10.1139/m57-019.

Oyewusi HA, Wahab RA, Kaya Y et al. (2020)

Alternative Bioremediation Agents against Haloacids,

Haloacetates and Chlorpyrifos Using Novel HalogenDegrading Bacterial Isolates from the Hypersaline Lake

Tuz. Catalysts 10 (6): 651. doi: 10.3390/catal10060651.

Heidarrezaei M, Shokravi H, Huyop F et al. (2020)

Isolation and Characterization of a Novel Bacterium

from the Marine Environment for Trichloroacetic Acid

Bioremediation. Applied Sciences, 10(13): p. 4593. doi:

3390/app10134593

Muslem WH, Edbeib MF, Aksoy HM et al. (2020)

Biodegradation of 3-chloropropionic acid (3-CP) by

Bacillus cereus WH2 and its in silico enzyme-substrate

docking analysis. Journal of Biomolecular Structure and

Dynamics 38 (11): 3432 – 3441. doi:

1080/07391102.2019.1655482

Wahhab BHA, Anuar NFSK, Wahab RA, et al. (2020)

Identification and characterization of a 2, 2-

dichloropropionic acid (2, 2-DCP) degrading

alkalotorelant bacterium strain BHS1 isolated from Blue

Lake, Turkey. Journal of Tropical Life Science 10 (3):

p. 245-252. doi: 10.11594/jtls.10.03.08

Parvizpour S, Hamid T, Huyop F (2013) Molecular

identification and biodegradation of 3-chloropropionic

acid (3CP) by filamentous fungi-Mucor and

Trichoderma species isolated from UTM agricultural

land. Malaysian Journal of Microbiology 9 (1): 120-124.

doi: 10.21161/mjm.40412.

Selvamani S, Wahab RA, Huyop F (2015) A novel

putative non-ligninolytic dehalogenase activity for 3-

chloropropionic acid (3CP) utilization by Trichoderma

asperellum strain SD1. Malaysian Journal of

Microbiology 11 (3): 265 – 272. doi:

21161/mjm.70315.

Muslem WH, ADBEI MF, Wahab RA et al. (2017) The

potential of a novel β-specific dehalogenase from

Bacillus cereus WH2 as a bioremediation agent for the

removal of β-haloalkanoic acids. Malaysian Journal of

Microbiology 13 (4): p. 298 – 307. doi:

21161/mjm.98816.

Cairns SS, Cornish A, Cooper RA (1996) Cloning,

sequencing and expression in Escherichia coli of two

Rhizobium sp. genes encoding haloalkanoate

dehalogenases of opposite stereospecificity. European

Journal of Biochemistry 235 (3): 744 – 749. doi:

1111/j.1432-1033.1996.t01-1-00744.x.

Tsang JS, Sallis PJ, Bull AT, Hardman DJ (1988) A

monobromoacetate dehalogenase from Pseudomonas

cepacia MBA4. Archives of Microbiology 150 (5): 441

– 446. doi: 10.1007/bf00422284.

Liu JQ, Kurihara T, Hasan AK et al. (1994) Purification

and characterization of thermostable and

nonthermostable 2-haloacid dehalogenases with

different stereospecificities from Pseudomonas sp. strain

YL. Applied and Environmental Microbiology 60 (7):

- 2393. doi: 10.1128/aem.60.7.2389-2393.1994.

Schneider B, Muller R, Frank R, Lingens F (1991)

Complete nucleotide sequences and comparison of the

structural genes of two 2-haloalkanoic acid

dehalogenases from Pseudomonas sp. strain CBS3.

Journal of Bacteriology 173 (4): 1530 – 1535. doi:

1128/jb.173.4.1530-1535.1991.

Van Der Ploeg J, Van Hall G, Janssen DB (1991)

Characterization of the haloacid dehalogenase from

Xanthobacter autotrophicus GJ10 and sequencing of the

dhlB gene. Journal of Bacteriology 173 (24): 7925 –

doi: 10.1128/jb.173.24.7925-7933.1991

Motosugi K, Esaki N, Soda K (1982) Purification and

properties of 2-halo acid dehalogenase from

Pseudomonas putida. Agricultural and Biological

Chemistry 46 (3): 837 – 838. doi:

1271/bbb1961.46.837

Kumar A, Pillay B, Olaniran AO (2016) L-2-haloacid

dehalogenase from ancylobacter aquaticus UV5:

Sequence determination and structure prediction.

International Journal of Biological Macromolecules, 83:

p. 216-225.

Anggoro RR, Ratnaningsih E (2017) Subcloning of

Haloacid Dehalogenase Gene from Klebsiella

pneumoniae Strain ITB1 into pET-30a Expression

Vector. Proceedings Book: p. 99.

Ang TF, Maiangwa J, Salleh AB et al. (2018)

Dehalogenases: from improved performance to potential

microbial dehalogenation applications. Molecules 23

(5): p. 1100. doi: 10.3390/molecules23051100.

Bidmanova S, Chaloupkova R, Damborsky J, Prokop Z

(2010) Development of an enzymatic fiber-optic

biosensor for detection of halogenated hydrocarbons.

Analytical and Bioanalytical Chemistry 398 (5): 1891-

doi: 10.1007/s00216-010-4083-z.

Los GV et al. (2008) HaloTag: a novel protein labeling

technology for cell imaging and protein analysis. ACS

Chemical Biology 3 (6): 373 – 382.

Mazumdar PA, Hulecki JC, Chernet MM et al. (2008)

X-ray crystal structure of Mycobacterium tuberculosis

haloalkane dehalogenase Rv2579. Biochimica et

Biophysica Acta (BBA)-Proteins and Proteomics, 1784

(2): 351 – 362. doi: 10.1016/j.bbapap.2007.10.014.

Chovancová E, Kosinski J, Bujnicki JM, Damborsky J

(2007) Phylogenetic analysis of haloalkane

dehalogenases. PROTEINS: Structure, Function, and

Bioinformatics 67 (2): 305 - 316. doi:

1002/prot.21313

Damborský J, Rorije E, Jesenska A et al. (2001)

Structure–specificity relationships for haloalkane

dehalogenases. Environmental Toxicology and

Chemistry: An International Journal 20 (12): 2681-

S Zakary, HA Oyewusi, F Huyop, 2020 / Dehalogenases for pollutant degradation: A mini review

JTLS | Journal of Tropical Life Science 24 Volume 11 | Number 1 | January | 2021

doi: 10.1002/etc.5620201205.

Fetzner S, Lingens F (1994) Bacterial dehalogenases:

biochemistry, genetics, and biotechnological

applications. Microbiological Reviews 58 (4): 641 -

Slater JH, Bull AT, Hardman DJ (1995) Microbial

dehalogenation. Biodegradation 6 (3): 181 – 189.

Sudi IY et al. (2012) Structure prediction, molecular

dynamics simulation and docking studies of D-specific

dehalogenase from Rhizobium sp. RC1. International

Journal of Molecular Sciences 13 (12): 15724-15754.

Abidin MHZ et al (2019) The mechanistic role of active

site residues in non-stereo haloacid dehalogenase E

(DehE). Journal of Molecular Graphics and Modelling

: 219-225.

Ismail SNF, Huyop F (2017) Microbial isolation and

degradation of selected haloalkanoic aliphatic acids by

locally isolated bacteria: A review. Malaysian Journal of

Microbiology 13 (3): 261 – 272.

Muslem WH et al. (2019) Biodegradation of 3-

chloropropionic acid (3-CP) by Bacillus cereus WH2

and its in silico enzyme-substrate docking analysis.

Journal of Biomolecular Structure and Dynamics: 1 -

Hamid TA et al. (2011) Purification and properties of a

new dehalogenase enzyme from Pseudomonas sp. B6P

grow in 3-chloropropionate (3CP). African Journal of

Biotechnology, 10(4): p. 610-614.

Hamid AAA et al. (2013) Molecular modelling and

functional studies of the non-stereospecific αhaloalkanoic acid dehalogenase (DehE) from Rhizobium

sp. RC1 and its association with 3-chloropropionic acid

(β-chlorinated aliphatic acid). Biotechnology &

Biotechnological Equipment 27 (2): 3725-3736.

Hill KE, Marchesi JR, Weightman AJ (1999)

Investigation of two evolutionarily unrelated

halocarboxylic acid dehalogenase gene families. Journal

of Bacteriology 181 (8): 2535 – 2547.

Kurihara T, Esaki N, Soda K (2000) Bacterial 2-

haloacid dehalogenases: structures and reaction

mechanisms. Journal of Molecular Catalysis B:

Enzymatic 10 (1-3): 57-65.

Gribble GW (1998) Naturally occurring organohalogen

compounds. Accounts of Chemical Research 31 (3): 141

– 152. doi: 10.1021/ar9701777

Gribble GW (2000) The natural production of

organobromine compounds. Environmental Science and

Pollution Research 7 (1): 37 – 49. doi:

1065/espr199910.002.

Schultz A et al. (2001) Dehalogenation of chlorinated

hydroxybiphenyls by fungal laccase. Applied and

Environmental Microbiology 67 (9): 4377-4381.

Dietrich D, Hickey WJ, Lamar R (1995) Degradation of

, 4'-dichlorobiphenyl, 3, 3', 4, 4'-tetrachlorobiphenyl,

and 2, 2', 4, 4', 5, 5'-hexachlorobiphenyl by the white rot

fungus Phanerochaete chrysosporium. Applied and

Environmental Microbiology 61 (11): 3904-3909.

Zeddel A, Majcherczyk A, Hüttermann A (1993)

Degradation of polychlorinated biphenyls by white‐rot

fungi pleurotus ostreatus and trametes versicolor in a

solid state system. Toxicological & Environmental

Chemistry 40 (1-4): 255-266.

Grifoll M, Hammel K (1997) Initial Steps in the

Degradation of Methoxychlor by the White Rot Fungus

Phanerochaete chrysosporium. Applied and

Environmental Microbiology 63 (3): 1175-1177.

Polnisch E et al. (1991) Degradation and dehalogenation

of monochlorophenols by the phenol-assimilating yeast

Candida maltosa. Biodegradation 2 (3): 193 – 199.

Muzikář M et al. (2011) Biodegradation of

chlorobenzoic acids by ligninolytic fungi. Journal of

Hazardous Materials 196: 386-394.

Wang C et al. (2008) Biodegradation of gaseous

chlorobenzene by white-rot fungus Phanerochaete

chrysosporium. Biomedical and Environmental

Sciences: BES 21 (6): 474-478.

Grotowska AK, Wawrzeńczyk C (2002) Lactones 13:

Biotransformation of iodolactones. Journal of Molecular

Catalysis B: Enzymatic 19: 203 – 208.

Grabarczyk M (2012) Fungal strains as catalysts for the

biotransformation of halolactones by hydrolytic

dehalogenation with the dimethylcyclohexane system.

Molecules 17 (8): 9741 – 9753.

Bustillo AJ et al. (2003) Biotransformation of the

fungistatic compound (R)-(+)-1-(4′-chlorophenyl)

propan-1-ol by Botrytis cinerea. Journal of Molecular

Catalysis B: Enzymatic 21 (4-6): 267 – 271.

Li J, Cai W, Zhu L (2011) The characteristics and

enzyme activities of 4-chlorophenol biodegradation by

Fusarium sp. Bioresource Technology 102 (3): 2985 –

Su X, Kong KF, Tsang JS (2012) Transports of acetate

and haloacetate in Burkholderiaspecies MBA4 are

operated by distinct systems. BMC Microbiology 12 (1):

Musa MA, Wahab RA, Huyop F (2018) Homology

modelling and in silico substrate-binding analysis of a

Rhizobium sp. RC1 haloalkanoic acid permease.

Biotechnology & Biotechnological Equipment 32 (2):

– 349.

Adamu Musa M, Huyop F (2018) In silico analysis of a

Rhizobium sp. RC1 putative haloalkanoic permease

sequence motif and classification. Malaysian Journal of

Microbiology 14: 680 – 690.




DOI: http://dx.doi.org/10.11594/jtls.11.01.03

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