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J-GLOBAL ID：200902216933707665   Reference number：05A0577825

Effects of Mutation at Methionine-42 of Escherichia coli Dihydrofolate Reductase on Stability and Function: Implication of Hydrophobic Interactions

大腸菌ジヒドロ葉酸レダクターゼの安定性及び機能に及ぼすMet42での変異の影響:疎水性相互作用の関与

Author (4)： OHMAE Eiji (Hiroshima Univ., Higashi-Hiroshima) ,  FUKUMIZU Yukari (Hiroshima Univ., Higashi-Hiroshima) ,  IWAKURA Masahiro (National Inst. of Advanced Industrial Sci. and Technol. (AIST), Tsukuba) ,  GEKKO Kunihiko (Hiroshima Univ., Higashi-Hiroshima)
Material： Journal of Biochemistry  (J Biochem)
Volume： 137  Issue： 5  Page： 643-652  Publication year： May. 01, 2005 
JST Material Number： F0286A  ISSN： 0021-924X  CODEN： JOBIAO  Document type： Article
Article type： 原著論文  Country of issue： Japan (JPN)  Language： ENGLISH (EN)

Thesaurus term： *dihydrofolate reductase ,...

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JST classification (2)： Enzyme in general  (EB09010D) ,  Microorganism biochemistry  (EG03020N)

Reference (35)：

• SAWAYA, M. R. Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase : crystallographic evidence. Biochemistry. 1997, 36, 586-603
• KITAHARA, R. High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry. 2000, 39, 12789-12795
• GEKKO, K. Effects of point mutation in a flexible loop on the stability and enzymatic function of Escherichia coli dihydrofolate reductase. J. Biochem. 1993, 113, 74-80
• GEKKO, K. Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase : important roles of a flexible loop in the stability and function. J. Biochem. 1994, 116, 34-41
• CAMERON, C. E. Evidence for a functional role of the dynamics of glycine-121 of Escherichia coli dihydrofolate reductase obtained from kinetic analysis of a site-directed mutant. Biochemistry. 1997, 36, 15792-15800

Terms in the title (5)： 大腸菌 ,  ジヒドロ葉酸レダクターゼ ,  安定性 ,  変異 ,  疎水性相互作用