Acidostable and acidophilic proteins: The example of the α-amylase from Alicyclobacillus acidocaldarius

Comparative Biochemistry and Physiology - A Physiology

Volumn 118, Issue 3, 1997, Pages 475-479

  Matzke, Jutta ^a   Schwermann, Birgit ^a   Bakker, Evert P ^a  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

Author keywords

( )8 barrel domain; Acidostability; Expression in Escherichia coli; Surface charge density; Amylase

Indexed keywords

AMYLASE;

CELL PH; ESCHERICHIA COLI; GRAM POSITIVE BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN STABILITY; REVIEW;

EID: 0031279756     PISSN: 03009629     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9629(97)00008-X     Document Type: Article

References (21)

1. 1. Brock, T.D. Thermophilic microorganisms and life at high temperatures. New York, Heidelberg, Berlin: Springer Verlag; 1978.
2. 2. Cobley, J.G.; Cox, J.C. Energy conservation in acidophilic bacteria. Microbiol. Rev. 47:579-595;1983.
3. 3. Krulwich, T.A.; Guffanti, A.A. Physiology of acidophilic and alkaliphilic bacteria. Adv. Microbiol. Physiol. 24:173-214; 1983.
4. 4. Booth, I.R. Regulation of cytoplasmic pH in bacteria. Microbiol. Rev. 49:359-378;1985.
5. 5. Bakker, E.P. The role of alkali-cation transport in energy coupling of neutrophilic and acidophilic bacteria: An assessment of methods and concepts. FEMS Microbiol. Rev. 75:319-334; 1990.
6. 6. Ingledew, W.J. Acidophiles. In: Edwards, C. (ed). Microbiology of Extreme Environments. Stony Stratford Milton Keynes, UK: Open University Press; 1990:33-54.
7. 7. Schwermann, B.; Pfau, K.; Liliensiek, B.; Schleyer, M.; Fischer, T.; Bakker, E.P. Purification, properties and structural aspects of a thermoacidophilic α-amylase from Alicyclobacillus acidocaldarius ATCC 27009. Insights into acidostability of proteins. Eur. J. Biochem. 226:981-991;1994.
8. 8. Koivola, T.T.; Hemilä, H.; Pakkanen, R.; Sibakov, M.; Palva, I. Cloning and sequencing of a gene encoding acidophilic amylase from Bacillus acidocaldarius. J. Gen. Microbiol. 139: 2399-2407;1993.
9. 9. Michel, H.; Neugebauer, D.-Ch.; Oesterhelt, D. The crystalline cell wall of Sulfolobus acidocaldarius: Structure, solubilization and reassembly. In: Baumeister, W.; Vogell, W., (eds). Electron Microscopy at Molecular Dimensions. New York: Springer Verlag; 1980:27-35.
10. 10. Lin, X.-L.; Tang, J. Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius. J. Biol. Chem. 265:1490-1495;1990.
11. 11. Sepulveda, P.; Marciniszyn, J.; Liu, D.; Tang, J. Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin. J. Biol. Chem. 250:5082-5088;1975.
12. 12. Kusano, T.; Takeshima, T.; Inoue, C.; Shiratori, T.; Yano, T.; Fukumori, Y.; Yamanaka, T. Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II) oxidase. J. Biol. Chem. 267:11242-11247;1992.
13. 13. Nunzi, F.; Woudstra, M.; Campese, D.; Bonicel, J.; Morin, D.; Bruschi, M. Amino acid sequence of rustocyanin from Thiobacillus ferrooxidans and its comparison with other blue proteins. Biochim. Biophys. Acta 1162:28-34;1993.
14. 1H Resonance assignments and global fold of rusticyanin. Insights into the ligation and acid stability of the blue copper site. J. Mol. Biol. 244:379-384;1994.
15. 15. Fusek, M.; Lin, X.-L.; Tang, J. Enzymic properties of thermopsin. J. Biol. Chem. 265:1496-1501;1990.
16. 16. Prescott, M.; Peek, K.; Daniel, R.M. Characterization of a thermostable pepstatin-insensitive acid proteinase from Bacillus species. Int. J. Biochem. Cell Biol. 27:729-739;1995.
17. 17. Svensson, B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25:141-157;1994.
18. 18. Janknecht, R.; de Martynoff, G.; Lou, J.; Hipskind, R.A.; Nordheim, A.; Stunnenberg, H.G. Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc. Natl. Acad. Sci. USA 88:8972-8976; 1991.
19. 19. Boel, E.; Brady, L.; Brzozowski, A.M.; Drewenda, Z.; Dodson, G.G.; Jensen, V.J.; Petersen, S.B.; Swift, H.; Thim, L.; Woldlike, H.F. Calcium binding in α-amylases: An X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus. Biochemistry 29:6244-6249;1990.
20. 20. Jones, T.A. Interactive computer graphics: FRODO. Meth. Enzymol. 115:157-171;1985.
21. 21. Nakajima, R.; Imanaka, T.; Aiba, S. Comparison of amino acid sequences of eleven α-amylases. Appl. Microbiol. Biotechnol. 23:355-360;1986.