Title | Identification of a Novel Dihydrodaidzein Racemase Essential for Biosynthesis of Equol from Daidzein in Lactococcus sp. Strain 20-92 |
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Author | Yoshikazu Shimada, Masayuki Takahashi, Norihiro Miyazawa, Yasuhiro Abiru, Shigeto Uchiyama, Haretsugu Hishigaki |
DOI | 10.1128/AEM.00410-12 |
Abstract | Equol is metabolized from daidzein, a soyisoflavone, by the gut microflora. In this study, we identified a novel dihydrodaidzein racemase (l-DDRC) that is involved in equol biosynthesis in a lactic acid bacterium, Lactococcus sp. strain 20-92, and confirmed that histidine-tagged recombinant l-DDRC (l-DDRC-His) was able to convert both the (R)- and (S)-enantiomers of dihydrodaidzein to the racemate. Moreover, we showed that recombinant l-DDRC-His was essential for in vitro equol production from daidzein by a recombinant enzyme mixture and that efficient in vitro equol production from daidzein was possible using at least four enzymes, including l-DDRC. We also proposed a model of the metabolic pathway from daidzein to equol in Lactococcus strain 20-92. |
Uniprot ID: I7H868
Protein: Dihydrodaizein racemase
Organism: Lactococcus garvieae
Length: 158 AA
Taxonomic identifier: 1363 [NCBI]
Source | Domain | Start | End | E-value (Domain) | Coverage |
---|---|---|---|---|---|
Pfam-A | Glyoxalase_4 | 10 | 104 | 6.5e-11 | 0.844 |
Program: hmmscan
Version: 3.1b2 (February 2015)
Method: hmmscan --domtblout hmmscan.tbl --noali -E 1e-5 pfam query.fa
Date: Mon Jul 20 14:32:16 2020
Description:
Glyoxalase_4
No Pfam abstract.
No InterPro results.
Information is taken from Pfam and InterPro web site.
(R)-dihydrodaidzein ⇒ (S)-dihydrodaidzein