A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments

BMC Biotechnology

Volumn 15, Issue 1, 2015, Pages

  Lee, Dae Hee ^a,b   Choi, Su Lim ^a,c   Rha, Eugene ^a   Kim, Soo Jin ^a   Yeom, Soo Jin ^a   Moon, Jae Hee ^a   Lee, Seung Goo ^a,b  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b University of Science and Technology (UST)   (South Korea)

^c Department of Biotech R and D   (South Korea)

Author keywords

Alkaline phosphatase; Escherichia coli; Metagenome; PhoX

Indexed keywords

ALKALINITY; CATALYST ACTIVITY; CLONING; ECOLOGY; ENCODING (SYMBOLS); ENZYME ACTIVITY; ESCHERICHIA COLI; GENE ENCODING; LINEARIZATION; MOLECULAR BIOLOGY; MOLECULAR MASS; PURIFICATION; SIGNAL ENCODING; SUBSTRATES; TEMPERATURE; THERMODYNAMIC STABILITY; TIDES; WETLANDS;

ALKALINE PHOSPHATASE; BIOCHEMICAL CHARACTERIZATION; METAGENOMES; METAGENOMIC LIBRARIES; PHOSPHORYLATED SUBSTRATES; PHOX; RECOMBINANT ESCHERICHIA COLI; SUBSTRATE SPECIFICITY;

PHOSPHATASES;

ALKALINE PHOSPHATASE; CALCIUM;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE; GENE EXPRESSION; GENE SEQUENCE; IN VIVO STUDY; LOW TEMPERATURE; MAP GENE; METAGENOME; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PERIPLASM; PHYLOGENY; SEDIMENT; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVATION; ENZYME STABILITY; GENE LIBRARY; GENETICS; METABOLISM; MICROBIOLOGY; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; SOUTH KOREA;

ALKALINE PHOSPHATASE; AMINO ACID SEQUENCE; CALCIUM; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; GENE LIBRARY; GEOLOGIC SEDIMENTS; METAGENOME; MOLECULAR SEQUENCE DATA; PHYLOGENY; REPUBLIC OF KOREA; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 84928658510     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/s12896-015-0115-2     Document Type: Article

References (38)

1. Sebastian M, Ammerman JW. The alkaline phosphatase PhoX is more widely distributed in marine bacteria than the classical PhoA. ISME J. 2009;3:563-72
2. Torriani A. From cell membrane to nucleotides: the phosphate regulon in Escherichia coli. BioEssays. 1990;12:371-6
3. Hulett FM. The signal-transduction network for Pho regulation in Bacillus subtilis. Mol Microbiol. 1996;19:933-9
4. Kadurugamuwa JL, Beveridge TJ. Natural release of virulence factors in membrane vesicles by Pseudomonas aeruginosa and the effect of aminoglycoside antibiotics on their release. J Antimicrob Chemother. 1997;40:615-21
5. Kim EE, Wyckoff HW. Reaction mechanism of alkaline phosphatase based on crystal structures: two-metal ion catalysis. J Mol Biol. 1991;218:449-64
6. Coleman JE. Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct. 1992;21:441-83
7. Majumdar A, Ghatak A, Ghosh RK. Identification of the gene for the monomeric alkaline phosphatase of Vibrio cholerae serogroup O1 strain. Gene. 2005;344:251-8
8. Nilgiriwala KS, Alahari A, Rao AS, Apte SK. Cloning and overexpression of alkaline phosphatase PhoK from Sphingomonas sp. strain BSAR-1 for bioprecipitation of uranium from alkaline solutions. Appl Environ Microbiol. 2008;74:5516-23
9. Suzuki C, Ueda H, Tsumoto K, Mahoney WC, Kumagai I, Nagamune T. Open sandwich ELISA with VH-/VL-alkaline phosphatase fusion proteins. J Immunol Methods. 1999;224:171-84
10. Tomazic-Allen SJ. Recombinant bacterial alkaline phosphatase as an immunodiagnostic enzyme. Ann Biol Clin (Paris). 1991;49:287-90
11. Kobori H, Sullivan CW, Shizuya H. Heat-labile alkaline phosphatase from Antarctic bacteria: rapid 5' end-labeling of nucleic acids. Proc Natl Acad Sci U S A. 1984;81:6691-5
12. Rina M, Pozidis C, Mavromatis K, Tzanodaskalaki M, Kokkinidis M, Bouriotis V. Alkaline phosphatase from the Antarctic strain TAB5. Eur J Biochem. 2000;267:1230-8
13. Hauksson JB, Andrésson ÓS, Ásgeirsson B. Heat-labile bacterial alkaline phosphatase from a marine Vibrio sp. Enz Microb Technol. 2000;27:66-73
14. Suzuki Y, Mizutani Y, Tsuji T, Ohtani N, Takano K, Haruki M, et al. Gene cloning, overproduction, and characterization of thermolabile alkaline phosphatase from a psychrotrophic bacterium. Biosci Biotechnol Biochem. 2005;69:364-73
15. Schmeisser C, Steele H, Streit W. Metagenomics, biotechnology with non-culturable microbes. Appl Microbiol Biotechnol. 2007;75:955-62
16. Iqbal HA, Feng Z, Brady SF. Biocatalysts and small molecule products from metagenomic studies. Curr Opin Chem Biol. 2012;16:109-16
17. Taupp M, Mewis K, Hallam SJ. The art and design of functional metagenomic screens. Curr Opin Biotechnol. 2011;22:465-72
18. Rabausch U, Juergensen J, Ilmberger N, Böhnke S, Fischer S, Schubach B, et al. Functional screening of metagenome and genome libraries for detection of novel flavonoid-modifying enzymes. Appl Environ Microbiol. 2013;79:4551-63
19. Choi S-L, Rha E, Lee SJ, Kim H, Kwon K, Jeong Y-S, et al. Toward a generalized and high-throughput enzyme screening system based on artificial genetic circuits. ACS Syn Biol. 2014;3:163-71
20. Shingler V, Bartilson M, Moore T. Cloning and nucleotide sequence of the gene encoding the positive regulator (DmpR) of the phenol catabolic pathway encoded by pVI150 and identification of DmpR as a member of the NtrC family of transcriptional activators. J Bacteriol. 1993;175:1596-604
21. Bihani SC, Das A, Nilgiriwala KS, Prashar V, Pirocchi M, Apte SK, et al. X-ray structure reveals a new class and provides insight into evolution of alkaline phosphatases. PLoS One. 2011;6:e22767
22. Zaheer R, Morton R, Proudfoot M, Yakunin A, Finan TM. Genetic and biochemical properties of an alkaline phosphatase PhoX family protein found in many bacteria. Environ Microbiol. 2009;11:1572-87
23. Petersen TN, Brunak S, von Heijne G, Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods. 2011;8:785-6
24. Bendtsen J, Nielsen H, Widdick D, Palmer T, Brunak S. Prediction of twin-arginine signal peptides. BMC Bioinformatics. 2005;6:167
25. Berks BC, Palmer T, Sargent F. The Tat protein translocation pathway and its role in microbial physiology. Adv Microb Physiol. 2003;47:187-254. Academic Press
26. Plocke DJ, Levinthal C, Vallee BL. Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme. Biochemistry. 1962;1:373-8
27. Koutsioulis D, Wang E, Tzanodaskalaki M, Nikiforaki D, Deli A, Feller G, et al. Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase. Protein Eng Des Sel. 2008;21:319-27
28. Post MA. Alkaline phosphatase from psychrophile TAB5 and cold-adapted, northern shrimp (Pandalus borealis) are structurally similar yet functionally distinct. FASEB J. 2006;20:A479
29. Chaudhuri G, Fau CS, Venu-Babu P, Fau V-BP, Ramasamy K, Fau RK, et al. Kinetic behaviour of calf intestinal alkaline phosphatase with pNPP. Indian J Biochem Biophys. 2013;50:64-71
30. Zappa S, Rolland J-L, Flament D, Gueguen Y, Boudrant J, Dietrich J. Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi. Appl Environ Microbiol. 2001;67:4504-11
31. Lohan MC, Statham PJ, Crawford DW. Total dissolved zinc in the upper water column of the subarctic North East Pacific. Deep Sea Res Part II Top Stud Oceanogr. 2002;49:5793-808
32. Monds RD, Newell PD, Schwartzman JA, O'Toole GA. Conservation of the Pho regulon in Pseudomonas fluorescens p f0-1. Appl Environ Microbiol. 2006;72:1910-24
33. Berks BC. A common export pathway for proteins binding complex redox cofactors? Mol Microbiol. 1996;22:393-404
34. van Mourik A, Bleumink-Pluym NMC, van Dijk L, van Putten JPM, Wösten MMSM. Functional analysis of a Campylobacter jejuni alkaline phosphatase secreted via the Tat export machinery. Microbiology. 2008;154:584-92
35. Wu J-R, Shien J-H, Shieh HK, Hu C-C, Gong S-R, Chen L-Y, et al. Cloning of the gene and characterization of the enzymatic properties of the monomeric alkaline phosphatase (PhoX) from Pasteurella multocida strain X-73. FEMS Microbiol Lett. 2007;267:113-20
36. Feller G, Gerday C. Psychrophilic enzymes: molecular basis of cold adaptation. Cell Mol Life Sci. 1997;53:830-41
37. Gerday C, Aittaleb M, Arpigny JL, Baise E, Chessa J-P, Garsoux G, et al. Psychrophilic enzymes: a thermodynamic challenge. Biochim Biophys Acta. 1997;1342:119-31
38. Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol. 2011;28:2731-9