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Publication Abstract from PubMed

The so-called miraculin-like proteins (MLPs) are homologous to miraculin, a homodimeric protein with taste-modifying activity that converts sourness into sweetness. The identity between MLPs and miraculin generally ranges from 30% to 55%, and both MLPs and miraculin are categorized into the Kunitz-type soybean trypsin inhibitor (STI) family. MLP from grape (Vitis vinifera; vvMLP) exhibits significant homology to miraculin (61% identity), suggesting that vvMLP possesses miraculin-like properties. The results of size-exclusion chromatography and sensory analysis illustrated that vvMLP exists as a monomer in solution with no detectable taste-modifying activity. Crystal structure determination revealed that vvMLP exists as a beta-trefoil fold, similarly as other MLPs and Kunitz-type protein inhibitors. The conformation of the loops, including the so-called reactive loop in the STI family, was substantially different between vvMLP and STI. Recombinant vvMLP had inhibitory activity against trypsin (Ki=13.7muM), indicating that the protein can act as a moderate trypsin inhibitor.

Structural and functional analysis of miraculin-like protein from Vitis vinifera.,Ohkura SI, Hori M, Saitoh K, Okuzawa T, Okamoto I, Furukawa N, Shimizu-Ibuka A Biochim Biophys Acta Proteins Proteom. 2018 Nov;1866(11):1125-1130. doi:, 10.1016/j.bbapap.2018.08.009. Epub 2018 Aug 27. PMID:30282610^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.