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Synthesis of a Phosphotyrosine-ontaining Peptide Fragment of the Regulatory Domain of pp60c-src
Lee, Eung-Seok,Mark, Cushman 영남대학교 약품개발연구소 1994 영남대학교 약품개발연구소 연구업적집 Vol.4 No.-
t-Boc-Tyr(PO₃Me₂)-OH (4) was ulitized in the synthesis of PheThrSerThrGluProGlnTyr(PO₃H₂)-GlnProGlyGluAsnLeu (1), a phosphotyrosine-containing peptide fragment of the regulatory domain of pp60^(c-src). The protected amino acid 4 was employed during the synthesis of PheThrSer-ThrGluProGlnTyr(PO₃Me₂)GlnProGlyGluAsnLeu (5), during which problems involving incomplete incorporation of the Tyr(PO₃Me₂) residue, as well as partial demethylation of the dimethylphosphono group and dephosphorylation during peptide synthesis, were encountered. In addition, an acid-catalyzed backbone rearrangement was encountered involving migration of the phenylalanine acyl group from the nitrogen to the hydroxyl group of the adjacent threonine residue during the deprotection of the phosphate group of 5 with a mixture of trifluoromethanesulfonic acid, trifluoroacetic acid, dimethyl sulfide, and m-cresol (10:50:30:10).
Lee, Eung-Seok,Jurayj, Jurjus,Cushman, Mark 영남대학교 약품개발연구소 1994 영남대학교 약품개발연구소 연구업적집 Vol.4 No.-
tert-Boc-L-3-Deoxymimosine (13) and tert-Boc-D-Deoxymimosine (16) were prepared in two steps from tert-Boc-L-aspatagine and tert-Boc-D-asparagine, respectively. Both 13 and 16 were determined to be optically pure by derivatization with Marphey's reagent. Activation and coupling of 16 to L-isoleucine methyl ester resulted in a diostereomeric mixture of products containing 96% of the DL diastereomer and 4% of the LL diastereomer. [L-3-Deoxymimosine⁴]-angiotensin 1 was synthsized from 13 as an approach to the disign and synthesis of selective protein-tyrosine kinase (PTK) inhibitors.
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.