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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.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Nakamura, Kenichi Komatsu, Katsuko Hattori, Masao Iwashima, Makoto |
| Copyright Year | 2013 |
| Abstract | 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 40 kDa 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(2)O condition, which closely resembles those of glycoside hydrolase family 4 and 109. |
| Starting Page | 2155 |
| Ending Page | 2160 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://www.jstage.jst.go.jp/article/bpb/36/4/36_b12-01011/_pdf |
| PubMed reference number | 23328408v1 |
| Volume Number | 36 |
| Issue Number | 4 |
| Journal | Biological & pharmaceutical bulletin |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Amino Acid Sequence Amino Acids Deuterium Dinucleoside Phosphates Glucose Glycosides Homologous Gene Molecular Mass Niacin Nicotinamide adenine dinucleotide (NAD) daidzein newton puerarin |
| Content Type | Text |
| Resource Type | Article |
