생명과학회지 (Journal of Life Science)

  • 제14권1호
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  • Pages.14-16
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  • 2004
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  • 1225-9918(pISSN)
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  • 2287-3406(eISSN)
한국생명과학회 (Korean Society of Life Science)
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트립토판 합성효소의 이소조절성에 미치는 리간드

Effects of Ligands on the Allosteric Property of Tryptophan Synthase

  • 김일 (부산대학교 자연과학대학 분자생물학과) ;
  • 신혜자 (동서대학교 응용공학부 환경공학전공) ;
  • 임운기 (부산대학교 자연과학대학 분자생물학과) ;
  • 김한도 (부산대학교 자연과학대학 분자생물학과)
  • Kim, Il (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Shin, Hye-Ja (Environmental Engineering Major, Division of Applied Engineering, Dongseo University) ;
  • Im, Woon-Ki (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Kim, Han-Do (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • 발행 : 2004.02.01
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초록

트립토판 합성효소의 이소조절성에 작용하는 리간드가 알려져 있다. $\beta$반응의 기질인 세린만이 있는 조건에서 일가 양이온과 glycerophosphate의 리간드효과를 잔기치환체를 사용하여 조사하였다. 이들 리간드가 이 효소의 이소조절성에 관여하고 있음을 보여주고 있다.

Various ligands function as regulators in the allosteric control of tryptophan synthase. Effects of the monovalent cations and glycerophosphate on the mutant tryptophan synthases were examined in the presence of L-serine. The results showed that these compounds might play roles in the allosteric control of the proteins.

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참고문헌

  1. Biochemistry v.39 Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligane. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects Fan,Y.Y.;P.McPhie;E.W.Milles https://doi.org/10.1021/bi9921586
  2. Arch. Biochem. Biophys. v.284 Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfoldings of the tryptophan synthase alpha subunit from Salmonella typhimurium Kanzaki,H.;P.McPhie;E.W.Miles https://doi.org/10.1016/0003-9861(91)90280-V
  3. Methods Enzymol. v.142 Tryptophan synthase from Escherichia coli and Salmonella typhimurium Miles,E.W.;R.Bauerle;S.A.Ahmed https://doi.org/10.1016/S0076-6879(87)42051-X
  4. J. Biol. Chem. v.264 The β subunit of tryptophan synthase; Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230 Miles,E.W.;H.Kawasaki;S.A.Ahmed;H.Morita;S.Nagata
  5. Trends Biochem. Sci. v.22 Protein atchitecture, dynamics and allostery in tryptophan synthase channeling Pan,P.;E.Woehl;M.F.Dunn https://doi.org/10.1016/S0968-0004(96)10066-9
  6. J. Biol. Chem. v.273 Cryocrystallograpy of a true substrate, indole-3-glycerol phosphate, bound to a mutant (αD60N) tryptophan synthase α₂β₂complex reveals the correct orientation of active site αGlu49 Rhee,S.E.;W.Miles;D.R.Davies https://doi.org/10.1074/jbc.273.15.8553
  7. Biochemistry v.36 Crystal stryctyres of a mutant (βK87T) tryptophan synthase α₂β₂ complex with ligands bound to the active sites of the α- and β-subunits reveal ligand-induced comformational changes Rhee,S.K.;D.Parris;C.C.Hyde;S.A.Ahmed;E.W.Miles;D.R.Davies https://doi.org/10.1021/bi9700429
  8. Biochemistry v.37 Mutations in the contact region between the α and β subunits of tryptophan synthase alter subunit interaction and intersubunit communication Rowlett,R.;L.H.Yang;S.A.Ahmed;P.McPhie;K.H.Jhee;E.W.Miles https://doi.org/10.1021/bi972286z
  9. J. Biol. Chem. v.270 Monovalent cations partially repair a conformational defect in a mutant tryptophan synthase α₂β₂ complex(βE109A) Ruvinov,S.B.;S.A.Ahmed;P.McPhie;E.W.Miles https://doi.org/10.1074/jbc.270.29.17333
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