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Stimulated interaction between and subunits of tryptophan synthase from hyperthermophile enhances its thermal stability.
J Biol Chem. 2003 Mar 14; 278(11):8922-8.JB

Abstract

Tryptophan synthase from hyperthermophile, Pyrococcus furiosus, was found to be a tetrameric form (22) composed of and 2 subunits. To elucidate the relationship between the features of the subunit association and the thermal stability of the tryptophan synthase, the subunit association and thermal stability were examined by isothermal titration calorimetry and differential scanning calorimetry, respectively, in comparison with those of the counterpart from Escherichia coli. The association constants between the and subunits in the hyperthermophile protein were of the order of 108 M1, which were higher by two orders of magnitude than those in the mesophile one. The negative values of the heat capacity change and enthalpy change upon the subunit association were much lower in the hyperthermophile protein than in the mesophile one, indicating that the conformational change of the hyperthermophile protein coupled to the subunit association is slight. The denaturation temperature of the subunit from the hyperthermophile was enhanced by 17 degrees C due to the formation of the 22 complex. This increment in denaturation temperature due to complex formation could be quantitatively estimated by the increase in the association constant compared with that of the counterpart from E. coli.

Authors+Show Affiliations

Institute for Protein Research, Osaka University, Suita City, Osaka 565-0871, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12643278

Citation

Ogasahara, Kyoko, et al. "Stimulated Interaction Between and Subunits of Tryptophan Synthase From Hyperthermophile Enhances Its Thermal Stability." The Journal of Biological Chemistry, vol. 278, no. 11, 2003, pp. 8922-8.
Ogasahara K, Ishida M, Yutani K. Stimulated interaction between and subunits of tryptophan synthase from hyperthermophile enhances its thermal stability. J Biol Chem. 2003;278(11):8922-8.
Ogasahara, K., Ishida, M., & Yutani, K. (2003). Stimulated interaction between and subunits of tryptophan synthase from hyperthermophile enhances its thermal stability. The Journal of Biological Chemistry, 278(11), 8922-8.
Ogasahara K, Ishida M, Yutani K. Stimulated Interaction Between and Subunits of Tryptophan Synthase From Hyperthermophile Enhances Its Thermal Stability. J Biol Chem. 2003 Mar 14;278(11):8922-8. PubMed PMID: 12643278.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stimulated interaction between and subunits of tryptophan synthase from hyperthermophile enhances its thermal stability. AU - Ogasahara,Kyoko, AU - Ishida,Masami, AU - Yutani,Katsuhide, PY - 2003/3/20/pubmed PY - 2003/5/15/medline PY - 2003/3/20/entrez SP - 8922 EP - 8 JF - The Journal of biological chemistry JO - J Biol Chem VL - 278 IS - 11 N2 - Tryptophan synthase from hyperthermophile, Pyrococcus furiosus, was found to be a tetrameric form (22) composed of and 2 subunits. To elucidate the relationship between the features of the subunit association and the thermal stability of the tryptophan synthase, the subunit association and thermal stability were examined by isothermal titration calorimetry and differential scanning calorimetry, respectively, in comparison with those of the counterpart from Escherichia coli. The association constants between the and subunits in the hyperthermophile protein were of the order of 108 M1, which were higher by two orders of magnitude than those in the mesophile one. The negative values of the heat capacity change and enthalpy change upon the subunit association were much lower in the hyperthermophile protein than in the mesophile one, indicating that the conformational change of the hyperthermophile protein coupled to the subunit association is slight. The denaturation temperature of the subunit from the hyperthermophile was enhanced by 17 degrees C due to the formation of the 22 complex. This increment in denaturation temperature due to complex formation could be quantitatively estimated by the increase in the association constant compared with that of the counterpart from E. coli. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/12643278/Stimulated_interaction_between_and_subunits_of_tryptophan_synthase_from_hyperthermophile_enhances_its_thermal_stability_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(19)71257-5 DB - PRIME DP - Unbound Medicine ER -