• BMB Reports
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• v.37 no.5
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• pp.515-521
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• 2004

The tricarboxylate (or citrate) carrier was purified from eel liver mitochondria and functionally reconstituted into liposomes. Incubation of the proteoliposomes with various sulfhydryl reagents led to inhibition of the reconstituted citrate transport activity. Preincubation of the proteoliposomes with reversible SH reagents, such as mercurials and methanethiosulfonates, protected the eel liver tricarboxylate carrier against inactivation by the irreversible reagent N-(1-pyrenyl)maleimide (PM). Citrate and L-malate, two substrates of the tricarboxylate carrier, protected the protein against inactivation by sulfhydryl reagents and decreased the fluorescent PM bound to the purified protein. These results suggest that the eel liver tricarboxylate carrier requires a single population of free cysteine(s) in order to manifest catalytic activity. The reactive cysteine(s) is most probably located at or near the substrate binding site of the carrier protein.

• Journal of the Korean Chemical Society
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• v.57 no.4
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• pp.455-460
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• 2013

A novel and simple method for the synthesis of 2-amino-4H-pyran-3,4,5-tricarboxylate derivative and the evaluation of their antibacterial activity against Pseudomonas syringae, Xanthomonas citi and Pectobacterium carotovorum are reported. The structure of the isolated compounds has been determined by means of $^1H/^{13}C$ NMR and FT-IR Spectroscopy. The reaction of alkyl isocyanides with acetylenic esters in the presence of dimethyl acetone-1,3-dicarboxylate in the present of $BF_3.SiO_2$ at ambient temperature. Some of the compound showed significant inhibition to growth of bacteria.

• Bulletin of the Korean Chemical Society
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• v.32 no.4
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• pp.1349-1352
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• 2011