메뉴 건너뛰기




Volumn 29, Issue 2, 1999, Pages 113-120

Molecular basis for thermoprotection in Bemisia: Structural differences between whitefly ketose reductase and other medium-chain dehydrogenases/reductases

Author keywords

Heat stress; Insect carbohydrates; Polyols; Sorbitol dehydrogenase

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; COMPLEMENTARY DNA; IDITOL DEHYDROGENASE; INSECT PROTEIN; ISOMERASE; KETOSE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SORBITOL; UNCLASSIFIED DRUG;

EID: 0033082418     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(98)00114-3     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0018789680 scopus 로고
    • Increased thermostability of proteins in the presence of sugars and polyols
    • Black J.F., Oakenfull D., Smith M.B. Increased thermostability of proteins in the presence of sugars and polyols. Biochemistry. 18:1979;5191-5196.
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Black, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 2
    • 0027480616 scopus 로고
    • Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
    • Bocanegra J.A., Scrutton N.S., Perham R.N. Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering. Biochemistry. 32:1993;2737-2740.
    • (1993) Biochemistry , vol.32 , pp. 2737-2740
    • Bocanegra, J.A.1    Scrutton, N.S.2    Perham, R.N.3
  • 3
    • 0024356865 scopus 로고
    • Eye lens ζ-crystallin relationships to the family of "long-chain" alcohol dehydrogenases. Protein trimming and conservation of stable parts
    • Borras T., Persson B., Jörnvall H. Eye lens ζ-crystallin relationships to the family of "long-chain" alcohol dehydrogenases. Protein trimming and conservation of stable parts. Biochemistry. 28:1989;6133-6139.
    • (1989) Biochemistry , vol.28 , pp. 6133-6139
    • Borras, T.1    Persson, B.2    Jörnvall, H.3
  • 4
    • 0025989616 scopus 로고
    • Role of aspartic acid 38 in the cofactor specificity of Drosphila alcohol dehydrogenase
    • Chen Z., Lee W.R., Chang S.H. Role of aspartic acid 38 in the cofactor specificity of Drosphila alcohol dehydrogenase. European Journal of Biochemistry. 202:1991;263-267.
    • (1991) European Journal of Biochemistry , vol.202 , pp. 263-267
    • Chen, Z.1    Lee, W.R.2    Chang, S.H.3
  • 5
    • 0022332394 scopus 로고
    • Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases
    • Eklund H., Horjales E., Jörnvall H., Brändén C.-I., Jeffery J. Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry. 24:1985;8005-8012.
    • (1985) Biochemistry , vol.24 , pp. 8005-8012
    • Eklund, H.1    Horjales, E.2    Jörnvall, H.3    Brändén, C.-I.4    Jeffery, J.5
  • 8
    • 0029134288 scopus 로고
    • The effect of polyol compounds on the thermostability of penicillin G acylase from a mutant of Escherichia coli ATCC 11105
    • Erarslan A. The effect of polyol compounds on the thermostability of penicillin G acylase from a mutant of Escherichia coli ATCC 11105. Process Biochemistry. 30:1995;133-139.
    • (1995) Process Biochemistry , vol.30 , pp. 133-139
    • Erarslan, A.1
  • 9
    • 0031657942 scopus 로고    scopus 로고
    • Polyol metabolism in homopterans at high temperatures: Accumulation of mannitol in aphids (Aphididae: Homoptera) and sorbitol in whiteflies (Aleyrodidae: Homoptera)
    • Hendrix D.L., Salvucci M.E. Polyol metabolism in homopterans at high temperatures: accumulation of mannitol in aphids (Aphididae: Homoptera) and sorbitol in whiteflies (Aleyrodidae: Homoptera). Comparative Biochemistry and Physiology. A120:1998;487-494.
    • (1998) Comparative Biochemistry and Physiology , vol.120 , pp. 487-494
    • Hendrix, D.L.1    Salvucci, M.E.2
  • 10
    • 0020073382 scopus 로고
    • Heat protection by glycerol in vitro
    • Henle J., Warters R.L. Heat protection by glycerol in vitro. Cancer Research. 42:1982;2171-2176.
    • (1982) Cancer Research , vol.42 , pp. 2171-2176
    • Henle, J.1    Warters, R.L.2
  • 14
    • 0014853306 scopus 로고
    • Horse liver alcohol dehydrogenase. On the primary structure of the isoenzymes
    • Jörnvall H. Horse liver alcohol dehydrogenase. On the primary structure of the isoenzymes. European Journal of Biochemistry. 16:1970;41-49.
    • (1970) European Journal of Biochemistry , vol.16 , pp. 41-49
    • Jörnvall, H.1
  • 15
    • 0023411028 scopus 로고
    • Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases
    • Jörnvall H., Persson B., Jeffery J. Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases. European Journal of Biochemistry. 167:1987;195-201.
    • (1987) European Journal of Biochemistry , vol.167 , pp. 195-201
    • Jörnvall, H.1    Persson, B.2    Jeffery, J.3
  • 16
    • 0021753525 scopus 로고
    • Extensive variations and basic features in the alcohol dehydrogenase - Sorbitol dehydrogenase family
    • Jörnvall H., von Bahr-Lindström H., Jeffery J. Extensive variations and basic features in the alcohol dehydrogenase - sorbitol dehydrogenase family. European Journal of Biochemistry. 140:1984;17-23.
    • (1984) European Journal of Biochemistry , vol.140 , pp. 17-23
    • Jörnvall, H.1    Von Bahr-Lindström, H.2    Jeffery, J.3
  • 17
    • 0027320944 scopus 로고
    • Zinc coordination in mammalian sorbitol dehydrogenase. Replacement of putative zinc ligands by site-directed mutagenesis
    • Karlsson C., Höög J.-O. Zinc coordination in mammalian sorbitol dehydrogenase. Replacement of putative zinc ligands by site-directed mutagenesis. European Journal Biochemistry. 216:1993;103-107.
    • (1993) European Journal Biochemistry , vol.216 , pp. 103-107
    • Karlsson, C.1    Höög, J.-O.2
  • 19
    • 29044440152 scopus 로고
    • Effect of glycerol on protein aggregation: Quantitation of thermal aggregation of proteins from CHO cells and analysis of aggregated proteins
    • Kim D., Lee Y.J. Effect of glycerol on protein aggregation: quantitation of thermal aggregation of proteins from CHO cells and analysis of aggregated proteins. Journal of Thermal Biology. 18:1993;41-48.
    • (1993) Journal of Thermal Biology , vol.18 , pp. 41-48
    • Kim, D.1    Lee, Y.J.2
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. Journal of Applied Chrystallography. 24:1991;946-950.
    • (1991) Journal of Applied Chrystallography , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0023490966 scopus 로고
    • A rapid cold-hardening process in insects
    • Lee R.E., Chen C.-P. Jr., Denlinger D.L. A rapid cold-hardening process in insects. Science. 238:1987;1415-1417.
    • (1987) Science , vol.238 , pp. 1415-1417
    • Lee, R.E.1    Chen C.-P., Jr.2    Denlinger, D.L.3
  • 24
    • 0027162878 scopus 로고
    • A cold-inducible Bombyx gene encoding a protein similar to mammalian sorbitol dehydrogenase
    • Niimi T., Yamashita O., Yaginuma T. A cold-inducible Bombyx gene encoding a protein similar to mammalian sorbitol dehydrogenase. European Journal Biochemistry. 213:1993;1125-1131.
    • (1993) European Journal Biochemistry , vol.213 , pp. 1125-1131
    • Niimi, T.1    Yamashita, O.2    Yaginuma, T.3
  • 25
    • 0030293131 scopus 로고    scopus 로고
    • Structure of the Bombyx sorbitol dehydrogenase gene: A possible alternative use of the promoter
    • Niimi T., Yamashita O., Yaginuma T. Structure of the Bombyx sorbitol dehydrogenase gene: a possible alternative use of the promoter. Insect Molecular Biology. 5:1996;269-280.
    • (1996) Insect Molecular Biology , vol.5 , pp. 269-280
    • Niimi, T.1    Yamashita, O.2    Yaginuma, T.3
  • 27
    • 0028212644 scopus 로고
    • Molecular characterization of microbial alcohol dehydrogenases
    • Reid M.F., Fewson C.A. Molecular characterization of microbial alcohol dehydrogenases. Critical Reviews in Microbiology. 20:1994;13-56.
    • (1994) Critical Reviews in Microbiology , vol.20 , pp. 13-56
    • Reid, M.F.1    Fewson, C.A.2
  • 28
    • 0027267295 scopus 로고
    • Photoaffinity labeling of ribulose-1,5-bisphosphate carboxylase/oxygenase activase with ATP γ-benzophenone
    • Salvucci M.E., Rajagopalan K., Sievert G., Haley B.E., Watt D.S. Photoaffinity labeling of ribulose-1,5-bisphosphate carboxylase/oxygenase activase with ATP γ-benzophenone. Journal of Biological Chemistry. 268:1993;14239-14244.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 14239-14244
    • Salvucci, M.E.1    Rajagopalan, K.2    Sievert, G.3    Haley, B.E.4    Watt, D.S.5
  • 29
    • 0030737718 scopus 로고    scopus 로고
    • Effect of sucrose concentration on carbohydrate metabolism in Bemisia argentifolii: Biochemical mechanism and physiological role for trehalulose synthesis in the silverleaf whitefly
    • Salvucci M.E., Wolfe G.R., Hendrix D.L. Effect of sucrose concentration on carbohydrate metabolism in Bemisia argentifolii: Biochemical mechanism and physiological role for trehalulose synthesis in the silverleaf whitefly. Journal of Insect Physiology. 43:1997;457-464.
    • (1997) Journal of Insect Physiology , vol.43 , pp. 457-464
    • Salvucci, M.E.1    Wolfe, G.R.2    Hendrix, D.L.3
  • 30
    • 0032078489 scopus 로고    scopus 로고
    • Purification and properties of an unusual NADPH-dependent ketose reductase from the silverleaf whitefly
    • Salvucci M.E., Wolfe G.R., Hendrix D.L. Purification and properties of an unusual NADPH-dependent ketose reductase from the silverleaf whitefly. Insect Biochemistry and Molecular Biology. 28:1998;357-363.
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , pp. 357-363
    • Salvucci, M.E.1    Wolfe, G.R.2    Hendrix, D.L.3
  • 31
    • 0011140369 scopus 로고
    • Molecular Cloning, A laboratory manual
    • New York: Cold Spring Harbor Laboratory
    • Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning, A laboratory manual. 2nd ed. 1989;Cold Spring Harbor Laboratory, New York.
    • (1989) 2nd Ed.
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 32
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton N.S., Berry A., Perham R.N. Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature. 343:1990;38-43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 35
    • 0032127601 scopus 로고    scopus 로고
    • A thermoprotective role for sorbitol in the silverleaf whitefly Bemisia argentifolii
    • Wolfe G.R., Hendrix D.L., Salvucci M.E. A thermoprotective role for sorbitol in the silverleaf whitefly Bemisia argentifolii. Journal of Insect Physiology. 44:1998;597-603.
    • (1998) Journal of Insect Physiology , vol.44 , pp. 597-603
    • Wolfe, G.R.1    Hendrix, D.L.2    Salvucci, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.