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Volumn 1433, Issue 1-2, 1999, Pages 132-138

Weakly bound calcium ions involved in the thermostability of aqualysin I, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1

Author keywords

Aqualysin I; Calcium binding site; Heat stable protease; Metal ion substitution; Thermostability; Titration calorimetry

Indexed keywords

CALCIUM ION; LANTHANUM; METAL ION; NEODYMIUM; PROTEINASE; STRONTIUM; TERBIUM;

EID: 0032797930     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00140-5     Document Type: Article
Times cited : (23)

References (15)
  • 1
    • 0002639249 scopus 로고
    • Production of the thermophilic extracellular proteases (aqualysins I and II) by Thermus aquaticus YT-1, an extreme thermophile
    • Matsuzawa H., Hamaoki M., Ohta T. Production of the thermophilic extracellular proteases (aqualysins I and II) by Thermus aquaticus YT-1, an extreme thermophile. Agric. Biol. Chem. 47:1983;25-28.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 25-28
    • Matsuzawa, H.1    Hamaoki, M.2    Ohta, T.3
  • 2
    • 0023958951 scopus 로고
    • Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1
    • Matsuzawa H., Tokugawa K., Hamaoki M., Mizoguchi M., Taguchi H., Terada I., Kwon S.-T., Ohta T. Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1. Eur. J. Biochem. 171:1988;441-447.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 441-447
    • Matsuzawa, H.1    Tokugawa, K.2    Hamaoki, M.3    Mizoguchi, M.4    Taguchi, H.5    Terada, I.6    Kwon, S.-T.7    Ohta, T.8
  • 3
    • 0024276069 scopus 로고
    • Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme
    • Kwon S.-T., Terada I., Matsuzawa H., Ohta T. Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme. Eur. J. Biochem. 173:1988;491-497.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 491-497
    • Kwon, S.-T.1    Terada, I.2    Matsuzawa, H.3    Ohta, T.4
  • 5
    • 0024099136 scopus 로고
    • Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1
    • Kwon S.-T., Matsuzawa H., Ohta T. Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1. J. Biochem. 104:1988;557-579.
    • (1988) J. Biochem. , vol.104 , pp. 557-579
    • Kwon, S.-T.1    Matsuzawa, H.2    Ohta, T.3
  • 6
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisin-like serine proteases
    • Siezen R.J., Leunissen J.A.M. Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6:1997;501-523.
    • (1997) Protein Sci. , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.M.2
  • 7
    • 0023678775 scopus 로고
    • The enzymatic activity of proteinase K is controlled by calcium
    • Bajorath J., Hinrichs W., Saenger W. The enzymatic activity of proteinase K is controlled by calcium. Eur. J. Biochem. 176:1988;441-447.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 441-447
    • Bajorath, J.1    Hinrichs, W.2    Saenger, W.3
  • 8
    • 0024191755 scopus 로고
    • Three-dimensional structure of proteinase K at 0.15-nm resolution
    • Betzel C., Pal G.P., Saenger W. Three-dimensional structure of proteinase K at 0.15-nm resolution. Eur. J. Biochem. 178:1988;155-171.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 155-171
    • Betzel, C.1    Pal, G.P.2    Saenger, W.3
  • 10
    • 0026846393 scopus 로고
    • 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli
    • 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli. FEMS Microbiol. Lett. 92:1992;73-78.
    • (1992) FEMS Microbiol. Lett. , vol.92 , pp. 73-78
    • Lee, Y.-C.1    Ohta, T.2    Matsuzawa, H.3
  • 11
    • 0031126863 scopus 로고    scopus 로고
    • Increase of the protease activity of aqualysin I, a thermostable serine protease, by replacing Asn219 near the catalytic residue Ser222
    • Lin S.-J., Kim D.-W., Ryugo Y., Wakagi T., Matsuzawa H. Increase of the protease activity of aqualysin I, a thermostable serine protease, by replacing Asn219 near the catalytic residue Ser222. Biosci. Biotechnol. Biochem. 61:1997;718-719.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 718-719
    • Lin, S.-J.1    Kim, D.-W.2    Ryugo, Y.3    Wakagi, T.4    Matsuzawa, H.5
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0002818018 scopus 로고
    • Calcium ion binding by thermitase
    • Briedigkeit L., Frömmel C. Calcium ion binding by thermitase. FEBS Lett. 253:1989;83-87.
    • (1989) FEBS Lett. , vol.253 , pp. 83-87
    • Briedigkeit, L.1    Frömmel, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.