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Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
( Chan Yong Lee ),( Boris Illarionov ),( Young Eun Woo ),( Kristina Kemter ),( Ryu Ryun Kim ),( Sabine Eberhardt ),( Mark Cushman ),( Wolfgang Eisenreich ),( Markus Fischer ),( Adelbert Bacher ) 생화학분자생물학회 2007 BMB Reports Vol.40 No.2
Ligand Binding Properties of the N-Terminal Domain of Riboflavin Synthase from Escherichia coli
Lee, Chan-Yong,Illarionov, Boris,Woo, Young-Eun,Kemter, Kristina,Kim, Ryu-Ryun,Eberhardt, Sabine,Cushman, Mark,Eisenreich, Wolfgang,Fischer, Markus,Bacher, Adelbert Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.2
Riboflavin synthase from Escherichia coli is a homotrimer of 23.4 kDa subunits and catalyzes the formation of one molecule each of riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione by the transfer of a 4-carbon moiety between two molecules of the substrate, 6,7- dimethyl-8-ribityllumazine. Each subunit comprises two closely similar folding domains. Recombinant expression of the N-terminal domain is known to provide a $C_2$-symmetric homodimer. In this study, the binding properties of wild type as well as two mutated proteins of N-terminal domain of riboflavin synthase with various ligands were tested. The replacement of the amino acid residue A43, located in the second shell of riboflavin synthase active center, in the recombinant N-terminal domain dimer reduces the affinity for 6,7-dimethyl-8-ribityllumazine. The mutation of the amino acid residue C48 forming part of activity cavity of the enzyme causes significant $^{19}F$ NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein, while substitution of A43 results in smaller chemical shift changes.