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首页> 外文期刊>Biological & pharmaceutical bulletin >Enzymatic cleavage of the C-glucosidic bond of puerarin by three proteins, Mn~(2+), and oxidized form of nicotinamide adenine dinucleotide
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Enzymatic cleavage of the C-glucosidic bond of puerarin by three proteins, Mn~(2+), and oxidized form of nicotinamide adenine dinucleotide

机译：葛根素的三种蛋白，Mn〜（2+）和氧化形式的幼吨酰胺腺嘌呤二核苷酸酶促切割葛根素的C-葡糖苷键

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We previously isolated the human intestinal bacterium, strain PUE, which can cleave the C-glucosidic bond of puerarin to yield its aglycone daidzein and glucose. In this study, we partially purified puerarin C-glucosidic bond cleaving enzyme from the cell-free extract of strain PUE and demonstrated that the reaction was catalyzed by at least three proteins, Mn~(2+), and oxidized form of nicotinamide adenine dinucleotide (NAD~+). We completely purified one of the proteins, called protein C, by chromatographic separation in three steps. The molecular mass of protein C was approximately 40kDa and the amino acid sequence of its N-terminal region shows high homology to those of two putative proteins which belong to Gfo/Idh/MocA family oxidoreductase. Protein C catalyzed hydrogen-deuterium exchange reaction of puerarin to 2″-deuterated puerarin in D_2O condition, which closely resembles those of glycoside hydrolase family 4 and 109.
机译：我们以前隔离了人肠道细菌，菌株型，这可以切割葛根素的C-葡糖苷键，以产生其糖苷龙氏菌和葡萄糖。 在该研究中，我们将葛根素C-葡糖苷键切割酶从菌株提取物部分纯化，并证明了反应催化了至少三种蛋白质，Mn〜（2+）和氧化胺酰胺腺嘌呤二核苷酸的氧化形式 （nad〜+）。 通过三个步骤，我们完全纯化称为蛋白C的蛋白质，称为蛋白质C. 蛋白质c的分子量约为40kDa，其N-末端区域的氨基酸序列显示出与属于GFO / IDH / MOCA家族氧化还原酶的两个推定蛋白质的高同源性。 蛋白C催化葛根素的氢 - 氘交换反应在D_2O条件下的葛根蛋白，这与糖苷水解酶4和109的糖酸酯相似。

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