Thermostable alkaline phosphatase in bacteria and archaea at a glance

Authors

  • Haider Mousa Hamzah Department of Biology, College of Science, University of Sulaimani, Kurdistan Region, Iraq. Author

DOI:

https://doi.org/10.17656/jzs.10757

Keywords:

Alkaline phosphatase, Archaea, Hyperthermophile, Thermophiles

Abstract

Alkaline Phosphatase (AP) is one of the most ubiquitous enzymes for the dephosphorylation of nucleic acids in molecular biology; as reporter enzymes for secreted proteins; for
colorimetric immunoassays; and as an indicator of activity in research and diagnostic kits. Today, there are continuing efforts suggesting the possibility of producing unique AP from
thermophilic bacteria and archaeal cells. As AP is found in a few members of thermophiles, it is also anticipated that it will be detected in their siblings, yet the reason behind the
variation in their AP activities is ambiguous. This mini review provides a comprehensive survey of the bacterial and archaeal alkaline phosphatases with particular emphasis on the
thermostable APs from the members of thermophiles and their activity variation.

References

Sharma, U, Pal, D, and Prasad, R. "Alkaline phosphatase: An overview". Indian J. Clin. Biochem., Vol. 29, No. 3, pp. 269–278. (2014). DOI: https://doi.org/10.1007/s12291-013-0408-y

Lin, X, Wang, L, Shi, X, and Lin, S. "Rapidly diverging evolution of an atypical alkaline phosphatase (PhoAaty) in marine phytoplankton: Insights from dinoflagellate alkaline phosphatases". Front. Microbiol., Vol. 6, p. 868. (2015). DOI: https://doi.org/10.3389/fmicb.2015.00868

Millán, JL. "Alkaline Phosphatases Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes". Purinergic Signal., Vol. 2, pp. 335–341. (2006). DOI: https://doi.org/10.1007/s11302-005-5435-6

Kathuria, S, and Martiny, AC. "Prevalence of a calcium-based alkaline phosphatase associated with the marine cyanobacterium Prochlorococcus and other ocean bacteria". Environ. Microbiol., Vol. 13, No. 1, pp. 74–83. (2011). DOI: https://doi.org/10.1111/j.1462-2920.2010.02310.x

Simão, AMS, Bolean, M, Hoylaerts, MF, Millán, JL, and Ciancaglini, P. "Effects of pH on the Production of Phosphate and Pyrophosphate by Matrix Vesicles’ Biomimetics". Calcif. Tissue Int., Vol. 93, No. 3, pp. 222–232. (2013). DOI: https://doi.org/10.1007/s00223-013-9745-3

Luo, H, Benner, R, Long, RL, and Hu, J. "Subcellular localization of marine bacterial alkaline phosphatases". Proc. Natl. Acad. Sci., Vol. 106, No. 50, pp. 21219–21223. (2009). DOI: https://doi.org/10.1073/pnas.0907586106

Albillos, SM, Reddy, R, and Salter, R. "Evaluation of Alkaline Phosphatase Detection in Dairy Products Using a Modified Rapid Chemiluminescent Method and Official Methods". J. Food Prot., Vol. 74, No. 7, pp. 1144–1154. (2011). DOI: https://doi.org/10.4315/0362-028X.JFP-10-422

Zappa, S, Rolland, JL, Flament, D, Gueguen, Y, Boudrant, J, and Dietrich, J. "Characterization of a Highly Thermostable Alkaline Phosphatase from the Euryarchaeon Pyrococcus abyssi". Appl. Environ. Microbiol., Vol. 67, No. 10, pp. 4504–4511. (2001). DOI: https://doi.org/10.1128/AEM.67.10.4504-4511.2001

Ausubel, FM, et al. "Current protocols in molecular biology". Vol. 1, Brooklyn, New York: John Wiley & Sons. Inc. (2003).

Rader, PA. "Alkaline phosphatase, an unconventional immune protein". Front. Immunol., Vol. 8, p. 897. (2017). DOI: https://doi.org/10.3389/fimmu.2017.00897

Kumar, M, Pawan PK, and Deepak G. "Isolation of periplasmic alkaline phosphatase from Rhizobium bacteria." Res. J. Microbiol. 3. 157-162. (2008). DOI: https://doi.org/10.3923/jm.2008.157.162

Derman, AI, and Beckwith, J. "Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: A caution for gene fusion studies". J. Bacteriol., Vol. 177, No. 13, pp. 3764–3770. (1995). DOI: https://doi.org/10.1128/jb.177.13.3764-3770.1995

Karamyshev, AL, Karamysheva, ZN, Kajava, AV, Ksenzenko, VN, and Nesmeyanova, MA. "Processing of Escherichia coli alkaline phosphatase: Role of the primary structure of the signal peptide cleavage region". J. Mol. Biol., Vol. 277, No. 4, pp. 859–870. (1998). DOI: https://doi.org/10.1006/jmbi.1997.1617

Wojciechowski, CL, and Kantrowitz, ER. "Altering of the metal specificity of Escherichia coli alkaline phosphatase". J. Biol. Chem., Vol. 277, No. 52, pp. 50476–50481. (2002). DOI: https://doi.org/10.1074/jbc.M209326200

Coleman, JE. "Structure and mechanism of alkaline phosphatase". Annu. Rev. Biophys. Biomol. Struct., Vol. 21, pp. 441–483. (1992). DOI: https://doi.org/10.1146/annurev.bb.21.060192.002301

Boulanger, RR, and Kantrowitz, ER. "Characterization of a monomeric Escherichia coli alkaline phosphatase formed upon a single amino acid substitution". J. Biol. Chem., Vol. 278, No. 26, pp. 23497–23501. (2003). DOI: https://doi.org/10.1074/jbc.M301105200

Llinas,P, Masella, M, Stigbrand, T, Ménez, A, Stura, EA, and Le Du, MHL. "Structural studies of human alkaline phosphatase in complex with strontium: Implication for its secondary effect in bones". Protein Sci., Vol. 15, No. 7, pp. 1691–1700. (2006). DOI: https://doi.org/10.1110/ps.062123806

Turner, PM. "The use of alkaline-phosphatase-conjugated second antibody for the visualization of electrophoretically separated proteins recognized by monoclonal antibodies". J. Immunol. Methods, Vol. 63, No. 1, pp. 1–6. (1983). DOI: https://doi.org/10.1016/0022-1759(83)90204-1

Wang, J, et al. "One-step immunoassay for tetrabromobisphenol a using a camelid single domain antibody-alkaline phosphatase fusion protein". Anal. Chem., Vol. 87, No. 9, pp. 4741–4748. (2015). DOI: https://doi.org/10.1021/ac504735p

Alvarado-Gámez, AL, Alonso-Lomillo, MA, Domínguez-Renedo, O, and Arcos-Martínez, MJ. "A disposable alkaline phosphatase-based biosensor for vanadium chronoamperometric determination". Sensors (Switzerland), Vol. 14, No. 2, pp. 3756–3767. (2014). DOI: https://doi.org/10.3390/s140203756

Singh, BK, and Walker, A. "Microbial degradation of organophosphorus compounds". FEMS Microbiol. Rev., Vol. 30, No. 3, pp. 428–471. (2006). DOI: https://doi.org/10.1111/j.1574-6976.2006.00018.x

Chaudhuri, G, Dey, P, Dalal, D, Venu-Babu, P, and Thilagaraj, WR. "A novel approach to precipitation of heavy metals from industrial effluents and single-ion solutions using bacterial alkaline phosphatase". Water. Air. Soil Pollut., Vol. 224, No. 7, p. 1625. (2013). DOI: https://doi.org/10.1007/s11270-013-1625-y

Yamane, K, and Maruo, B. "Alkaline phosphatase possessing alkaline phosphodiesterase activity and other phosphodiesterases in Bacillus subtilis". J. Bacteriol., Vol. 134, No. 1, pp. 108e-114 (1978). DOI: https://doi.org/10.1128/jb.134.1.108-114.1978

Hamzah, HM, and Hassan, HG. "Local Isolate of Bacillus stearothermophilus Producing Alkaline Phosphatase Activity by two Fermentation Systems". Iraqi National J. Chemistry. (17):143-50. (2005).

Zaheer, R, Morton, R, Proudfoot, M, Yakunin, A, and Finan, TM. "Genetic and biochemical properties of an alkaline phosphatase PhoX family protein found in many bacteria". Environ. Microbiol., Vol. 11, No. 6, pp. 1572–1587. (2009). DOI: https://doi.org/10.1111/j.1462-2920.2009.01885.x

Sebastian, M, and Ammerman, JW. "Role of the phosphatase PhoX in the phosphorus metabolism of the marine bacterium Ruegeria pomeroyi DSS-3". Environ. Microbiol. Rep., Vol. 3, No. 5, pp. 535–542. (2011). DOI: https://doi.org/10.1111/j.1758-2229.2011.00253.x

White, AE. "New insights into bacterial acquisition of phosphorus in the surface ocean". Proc. Natl. Acad. Sci., Vol. 106, No. 50, pp. 21013–21014. (2009). DOI: https://doi.org/10.1073/pnas.0912475107

Zalatan, JG, Fenn, TD, Brunger, AT, and Herschlag, D. "Structural and Functional Comparisons of Nucleotide Pyrophosphatase/ Phosphodiesterase and Alkaline Phosphatase: Implications for Mechanism and Evolution". Biochemistry, Vol. 45, pp. 9788–9803. (2006). DOI: https://doi.org/10.1021/bi060847t

Zhang, Y, et al. "A moderately thermostable alkaline phosphatase from Geobacillus thermodenitrificans T2: Cloning, expression and biochemical characterization". Appl. Biochem. Biotechnol., Vol. 151, No. 1, pp. 81–92. (2008). DOI: https://doi.org/10.1007/s12010-008-8166-7

Yurchenko, JV, Budilov, AV, Deyev, SM, Khromov, IS, and Sobolev, AY. "Cloning of an alkaline phosphatase gene from the moderately thermophilic bacterium Meiothermus ruber and characterization of the recombinant enzyme". Mol. Genet. Genomics, Vol. 270, No. 1, pp. 87–93. (2003). DOI: https://doi.org/10.1007/s00438-003-0899-y

Divya, A, Santhiagu, A, and Prakash, SJ. "Cloning, expression and characterization of a highly active thermostable alkaline phosphatase from Bacillus licheniformis MTCC 1483 in Escherichia coli BL21 (DE3)". Appl. Biochem. Microbiol., Vol. 52, No. 4, pp. 358–365. (2016). DOI: https://doi.org/10.1134/S0003683816040037

Lee, DH, et al. "A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments". BMC Biotechnol., Vol. 15, No. 1, pp. 1–13. (2015). DOI: https://doi.org/10.1186/s12896-015-0115-2

Gong, N, Chen, C, Xie, L, Chen, H, Lin, X, and Zhang, R. "Characterization of a thermostable alkaline phosphatase from a novel species Thermus yunnanensis sp. nov. and investigation of its cobalt activation at high temperature". Biochim. Biophys. Acta (BBA)-Proteins Proteomics, Vol. 1750, No. 2, pp. 103–111. (2005). DOI: https://doi.org/10.1016/j.bbapap.2005.05.007

Vieille, C, and Zeikus, GJ. "Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability". Microbiol. Mol. Biol. Rev., Vol. 65, No. 1, pp. 1–43. (2001). DOI: https://doi.org/10.1128/MMBR.65.1.1-43.2001

de Miguel Bouzas, T, Barros-Velazquez, J, and Gonzalez Villa, T. "Industrial Applications of Hyperthermophilic Enzymes: A Review". Protein Pept. Lett., Vol. 13, No. 7, pp. 645–651. (2006). DOI: https://doi.org/10.2174/092986606777790548

Turner, P, Mamo, G, and Karlsson, EN. "Potential and utilization of thermophiles and thermostable enzymes in biorefining". Microb. Cell Fact., Vol. 6, No. 1, p. 9. (2007). DOI: https://doi.org/10.1186/1475-2859-6-9

Kumar, L, Awasthi, G, and Singh, B. "Extremophiles: A novel source of industrially important enzymes". Biotechnology, Vol. 10, No. 2, pp. 121–135. (2011). DOI: https://doi.org/10.3923/biotech.2011.121.135

Mehta, R, Singhal, P, Singh, H, Damle, D, and Sharma, AK. "Insight into thermophiles and their wide-spectrum applications". Biotech, Vol. 6, No. 1, p. 81. (2016). DOI: https://doi.org/10.1007/s13205-016-0368-z

Sunden, F, Peck, A, Salzman, J, Ressl, S, and Herschlag, D. "Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site". Elife, Vol. 4, p. e06181. (2015). DOI: https://doi.org/10.7554/eLife.06181

Sunden, F, et al. "Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase Superfamily". J. Am. Chem. Soc., Vol. 138, No. 43, pp. 14273–14287. (2016). DOI: https://doi.org/10.1021/jacs.6b06186

Wojciechowski, CL, Cardia, JP, and Kantrowitz, ER. "Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity". Protein Sci., Vol. 11, No. 4, pp. 903–911. (2002). DOI: https://doi.org/10.1110/ps.4260102

Nelson, KE, et al. "Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima". Nature, Vol. 399, pp. 323–329. (1999). DOI: https://doi.org/10.1038/20601

Nesbø, CL, L’Haridon, S, Stetter, KW, and Ford Doolittle, W. "Phylogenetic analyses of two ‘archaeal’ genes in Thermotoga maritima reveal multiple transfers between Archaea and Bacteria". Mol. Biol. EVol., Vol. 18, No. 3, pp. 362–375. (2 DOI: https://doi.org/10.1093/oxfordjournals.molbev.a003812

Published

2019-12-20

How to Cite

Thermostable alkaline phosphatase in bacteria and archaea at a glance. (2019). Journal of Zankoy Sulaimani - Part A, 21(2), 57-64. https://doi.org/10.17656/jzs.10757