Characterization of thermostable native alkaline phosphatase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1

Applied Microbiology and Biotechnology

Volumn 74, Issue 1, 2007, Pages 107-112

  Helianti, Is ^a,b   Okubo, Takako ^a   Morita, Yasutaka ^a,c   Tamiya, Eiichi ^a  

^a JAPAN ADVANCED INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b AGENCY FOR THE ASSESSMENT AND APPLICATION OF TECHNOLOGY BPPT   (Indonesia)

^c KINKI UNIVERSITY   (Japan)

Author keywords

Aeropyrum pernix; Alkaline phosphatase; Hyperthermophilic; Thermostable

Indexed keywords

MAGNESIUM COMPOUNDS; MOLECULAR BIOLOGY; MONOMERS; PLANTS (BOTANY); THERMODYNAMIC STABILITY;

AEROPYRUM PERNIX; ALKALINE PHOSPHATASE; HYPERTHERMOPHILIC;

ENZYMES;

ALKALINE PHOSPHATASE; CALCIUM; COBALT; HOMODIMER; MAGNESIUM; MAGNESIUM ION; MONOMER;

ENZYME ACTIVITY; HOMOGENEITY; MAGNESIUM; PHOSPHATASE; PROKARYOTE;

AEROPYRUM; AEROPYRUM PERNIX K1; ARTICLE; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STABILITY; HYPERTHERMOPHILIC ARCHAEON; INCUBATION TEMPERATURE; MOLECULAR WEIGHT; NONHUMAN; PH; TEMPERATURE;

AEROBIOSIS; AEROPYRUM; ALKALINE PHOSPHATASE; ENZYME STABILITY; HEAT; HYDROGEN-ION CONCENTRATION; SUBSTRATE SPECIFICITY;

AEROPYRUM PERNIX; ARCHAEA;

EID: 33846640474     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0640-y     Document Type: Article

References (26)

1. Anba J, Bidaud M, Vasil ML, Lazdunski A (1990) Nucleotide sequence of the Pseudomonas aeruginosa phoB gene, the regulatory gene for the phosphate regulon. J Bacteriol 172:4685-4689
2. Besman M, Coleman JE (1985) Isozymes of bovine intestinal alkaline phosphatase. J Biol Chem 260:11190-11193
3. Bortolato M, Besson F, Roux B (1999) Role of metal ions on the secondary and quaternary structure of alkaline phosphatase from bovine intestinal mucosa. Proteins 37:310-318
4. Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
5. Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA (1981) Amino acid sequence of Escherichia coli alkaline phosphatase. Proc Natl Acad Sci USA 78:3473-3477
6. Croocker PC, Sako Y, Uchida A (1999) Purification and characterization of intracellular heat-stable proteinase (pernilase) from the marine hyperthermophilic archaeon Aeropyrum pernix K1. Extremophiles 3:3-9
7. Dong G, Zeikus JG (1997) Purification and characterization of alkaline phosphatase from Thermotoga neapolitana. Enzyme Microb Technol 21:335-340
8. 2+-dependent inducible alkaline phosphatase from the extremely halophilic archaebacterium Haloarcula marismortui. J Bacteriol 172:7065-7070
9. Helianti I, Morita Y, Yamamura A, Murakami Y, Yokoyama K, Tamiya (2001) Characterization of native glutamate dehydrogenase from an aerobic hyperthermophilic archaeon Aeropyrum pernix K1. Appl Microbiol Biotechnol 56:388-394
10. Helianti I, Morita Y, Murakami Y, Yokoyama K, Tamiya (2002) Expression of two kinds of recombinant glutamate dehydrogenase from Aeropyrum pernix with different N-terminal sequence length in Escherichia coli. Appl Microbiol Biotechnol 59:462-466
11. Hodson AW, Skillen AW (1988) Comparison of diazo-coupling, formazan, and silver staining techniques for visualizing alkaline phosphatase isoenzymes after electrophoresis in homogeneous-pore and gradient-pore polyacrylamide gels. Anal Biochem 169:253-261
12. Karamyshev AL, Karamysheva ZN, Kajava AV, Ksenzenko VN, Nesmeyanova MA (1998) Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. J Mol Biol 277:859-870
13. Kawarabayasi Y, Hino Y, Horikawa H, Yamazaki S, Haikawa Y, Jin-no K, Takahashi M, Sekine M, Baba S, Ankai A, Kosugi H, Hosoyama A, Fukui S, Nagai Y, Nishijima K, Nakazawa H, Takamiya M, Masuda S, Funahashi T, Tanaka T, Kudoh Y, Yamazaki J, Kushida N, Oguchi A, Kikuchi H et al (1999) Complete genome sequence of an aerobic hyperthermophilic crenarcheon, Aeropyrum pernix K1. DNA Res 6:83-101
14. Kim EE, Wyckoff HW (1991) Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J Mol Bio 218:449-464
15. Mori S, Okamoto M, Nishibori M, Ichimura M, Sakayama J, Endo H (1999) Purification and characterization of alkaline phosphatase from Bacillus stearothermophilus. Biotechnol Appl Biochem 29:235-239
16. Moura RS, Martín JF, Martín A, Liras P (2001) Substrate analysis and molecular cloning of the extracellular alkaline phosphatase of Streptomyces griseus. Microbiol 147:1525-1533
17. Niehaus F, Bertoldo C, Kahler M, Antranikian G (1999) Extremophiles as a source of novel enzymes for industrial application. Appl Microbiol Biotechnol 51:711-729
18. Pantazaki AA, Karagiorgas AA, Liakopoulou-Kyriakides M, Kyriakidis HA (1998) Hyperalkaline and thermostable phosphatase in Thermus thermophilus. Appl Biochem Biotechnol 75:249-259
19. Rina M, Pozidis C, Mavromatis K, Tzanodaskalaki M, Kokkinidis M, Bouriotis V (2000) Alkaline phosphatase from the Antarctic strain TAB5: properties and psychrophilic adaptations. Eur J Biochem 267 1230-1238 (FEBS 2000)
20. Robyl JF, White BJ (eds) (1987) Biochemical techniques: theory and practices. Brooks-cde, Monterey CA, page 247
21. Sako Y, Nomura N, Uchida A, Ishida Y, Morii H, Koga Y, Hoaki T, and Maruyama T (1996) Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100°C. Int J Syst Bacteriol 46:1010-1077
22. Sako Y, Croocker PC, Ishida Y (1997) An extremely heat-stable extracellular proteinase (aeropyrolysin) from the hyperthermophilic archaeon Aeropyrum pernix K1. FEBS Lett 415: 329-334
23. Trowsdale J, Martin D, Bicknell D, and Campbell I (1990) Alkaline phosphatases. Biochem Soc Trans 18:178-180
24. Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43
25. Zappa S, Rolland JL, Flament D, Gueguen Y, Boudrant J, and Dietrich (2001) Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi. Appl Environ Microbiol 67:4504-4511
26. Zueva NN, Dalev PG, Lazarova DL (1993) Properties, production, and practical uses of alkaline phosphatase. Biokhimiia 58: 1009-1023