Effect of polar side chains at position 172 on thermal stability of 3- isopropylmalate dehydrogenase from Thermus thermophilus

FEBS Letters

Volumn 410, Issue 2-3, 1997, Pages 141-144

  Akanuma, Satoshi ^a,b   Qu, Chunxu ^a   Yamagishi, Akihiko ^b   Tanaka, Nobuo ^a   Oshima, Tairo ^b  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

3 Isopropylmalate dehydrogenase; Electrostatic interaction; Hydrophobic packing; Site directed mutagenesis; Thermal stability

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; BACTERIAL ENZYME;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ANALYSIS; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; THERMOSTABILITY; THERMUS THERMOPHILUS;

3-ISOPROPYLMALATE DEHYDROGENASE; ALANINE; ALCOHOL OXIDOREDUCTASES; ASPARAGINE; ENZYME STABILITY; GLUTAMIC ACID; GLUTAMINE; HEATING; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 0030785695     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)00540-1     Document Type: Article

References (21)

1. Kuroki R., Taniyama Y., Seko C., Nakamura H., Kikuchi M., Ikehara M. Proc. Natl. Acad. Sci. USA. 86:1989;6903-6907.
2. Matsumura M., Becktel W.J., Levitt M., Matthews B.W. Proc. Natl. Acad. Sci. USA. 86:1989;6562-6566.
3. Pantoliano M.W., Whitlow M., Wood J.F., Rollence M.L., Finzel B.C., Gilliland G.L., Poulos T.L., Bryan P.N. Biochemistry. 27:1988;8311-8317.
4. Matthews B.W., Nicholson H., Becktel W.J. Proc. Natl. Acad. Sci. USA. 84:1987;6663-6667.
5. Nicholson H., Becktel W.J., Matthews B.W. Nature. 336:1988;651-656.
6. Yutani K., Ogasahara K., Tsujita T., Sugino Y. Proc. Natl. Acad. Sci. USA. 84:1987;4441-4444.
7. Wigley D.B., Clarke A.R., Dunn C.R., Barstow D.A., Atkinson T., Chia W.N., Muirhead H., Holbrook J.J. Biochim. Biophys. Acta. 916:1987;145-148.
8. Tanaka T., Kawano N., Oshima T. J. Biochem. (Tokyo). 89:1981;677-682.
9. Yamada T., Akutsu N., Miyazaki K., Kakinuma K., Yoshida M., Oshima T. J. Biochem. (Tokyo). 108:1990;449-456.
10. Imada K., Sato M., Tanaka N., Katsube Y., Matsuura Y., Oshima T. J. Mol. Biol. 222:1991;725-738.
11. Kotsuka T., Akanuma S., Tomuro M., Yamagishi A., Oshima T. J. Bacteriol. 178:1996;723-727.
12. Akanuma, S., Yamagishi, A. and Oshima, T. (1995) Prot. Eng. 8 Suppl. 4.
13. Qu C., Akanuma S., Moriyama H., Tanaka N., Oshima T. Prot. Eng. 10:1997;45-52.
14. Kunkel T.A., Roberts J.D., Zakour R.A. Methods Enzymol. 154:1987;367-382.
15. Sanger F., Nicklen S., Coulson A.R. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
16. Brooks B.R., Bruccoleri R.E., Olafson B.D., States D.J., Swaminathan S., Karplus M. J. Comput. Chem. 4:1983;187-217.
17. Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H. J. Mol. Biol. 240:1994;421-433.
18. Terwilliger T.C., Zabin H.B., Horvath M.P., Sandberg W.S., Schlunk P.M. J. Mol. Biol. 236:1994;556-571.
19. Rennell D., Bouvier S.E., Hardy L.W., Poteete A.R. J. Mol. Biol. 222:1991;67-88.
20. Bowie J.U., Reidhaar-Olson J.F., Lim W.A., Sauer R.T. Science. 247:1990;1306-1310.
21. Huang W., Petrosino J., Hirsch M., Shenkin P.S., Palzkill T. J. Mol. Biol. 258:1996;688-703.