• Biomolecules & Therapeutics
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• v.6 no.4
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• pp.378-382
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• 1998

In the previous screening on antidiabetic effect of Lycii fructus by glucose transport method using $N_2$-STZ diabeted rat model, each extracts showed the potent antidiabetic activity. We obtained three compounds isolated from the water fraction, EtOAc fraction and n-BuOH fraction of Lycii fructus in the present work and their structures were identified as 1-carboxy-N,N,N-trimethylmethanaminium hydroxide inner salt, 2,4(1H,3H)-pyrimidinedione and 3,3',4',5,7-pentahydroxyflavone-3-rutinoside . Among the constituents separated from Lycii fructus, 2,4(IH,3H)-pyrimidinedione, 3,3',4',5,7-pentahydroxyflavone-3-rutinoside and ascorbic acid were shown a remarkable antidiabetic effect.

• BMB Reports
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• v.40 no.2
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• pp.239-246
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• 2007

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.