Old Yellow Enzyme from<i>Candida macedoniensis</i>Catalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone

Kataoka, Michihiko; Kotaka, Atsushi; Hasegawa, Akiko; Wada, Masaaki; Yoshizumi, Ayumi; Nakamori, Shigeru; Shimizu, Sakayu

doi:10.1271/bbb.66.2651

Cited by 70 publications

(34 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A solution of the purified recombinant L-DZNR-His from E. coli was light yellow in color (data not shown). Kataoka et al (16) reported that the OYE from Candida macedoniensis could catalyze the enantioselective hydrogenation of the carbon double bond of ketoisophorone (KIP; 2,6,6-trimethyl-2-cyclohexen-1,4-dione). We examined whether L-DZNR catalyzes a reduction of daidzein with enantioselectivity or not and showed that recombinant L-DZNR-His participated in the enantioselective hydrogenation of daidzein, with the dihydrodaidzein produced almost always being (S)-dihydrodaidzein.…”

Section: Discussionmentioning

confidence: 99%

Cloning and Expression of a Novel NADP(H)-Dependent Daidzein Reductase, an Enzyme Involved in the Metabolism of Daidzein, from Equol-Producing Lactococcus Strain 20-92

Shimada

Yasuda

Takahashi

et al. 2010

Appl Environ Microbiol

View full text Add to dashboard Cite

Equol is a metabolite produced from daidzein by enteric microflora, and it has attracted a great deal of attention because of its protective or ameliorative ability against several sex hormone-dependent diseases (e.g., menopausal disorder and lower bone density), which is more potent than that of other isoflavonoids. We It was further suggested that L-DZNR was an NAD(H)/NADP(H):flavin oxidoreductase belonging to the old yellow enzyme (OYE) family. Recombinant histidine-tagged L-DZNR was expressed in Escherichia coli.The recombinant protein converted daidzein to (S)-dihydrodaidzein with enantioselectivity. This is the first report of the isolation of an enzyme related to daidzein metabolism and equol production in enteric bacteria.Isoflavones are flavonoids present in various plants and are known to be abundant in soybeans and legumes. These compounds have been called phytoestrogens because their chemical structure is similar to that of the female sex hormone, estrogen. Isoflavones have an ability to bind to estrogen receptors and show protection against or improvement in several sex hormone-dependent diseases, such as breast cancer, prostate cancer, menopausal disorder, lower bone density, and hypertension, due to their weak agonistic or antagonistic effects (1,19,27).Daidzein is one of the main soy isoflavonoids produced from daidzin by the glucosidase of intestinal bacteria (17). Equol is a metabolite produced from daidzein by the enterobacterial microflora (5). Recently, equol has attracted a great deal of attention because its estrogenic activity is more potent than that of other isoflavonoids, including daidzein (27). It is well known that individual variation exists in the ability of these enteric microflora to produce equol and that less than half the human population is capable of producing equol after ingesting soy isoflavones (3). Therefore, to increase the production of equol in the enteric environment of each individual, the development of probiotics using safe bacteria which have the ability to produce equol from daidzein is ongoing.Lactococcus strain 20-92 (Lactococcus 20-92; 30a) is an equol-producing lactic acid bacterium isolated from the feces of healthy humans by Uchiyama et al. (30). This bacterium is spherical and Gram positive and is a strain of L. garvieae. The application of Lactococcus 20-92 in probiotics is advantageous because L. garvieae is not pathogenic or toxic to humans.To date, other bacterial strains that are capable of transforming daidzein to dihydrodaidzein or equol have been isolated (9,21,22,23,29,32,36,37). Daidzein is thought to be metabolized by human intestinal bacteria to equol or to Odesmethylangolensin via dihydrodaidzein and tetrahydrodaidzein (14,15,22,32); however, neither the enzymes involved in the metabolism of daidzein to equol nor even the metabolic pathway has been clarified fully for equol-producing bacteria.In this study, we purified an enzyme from Lactococcus 20-92 that assisted in the conversion of daidzein to dihydrodaidzein. Furthermore, we cloned the...

show abstract

Section: Discussionmentioning

confidence: 99%

Cloning and Expression of a Novel NADP(H)-Dependent Daidzein Reductase, an Enzyme Involved in the Metabolism of Daidzein, from Equol-Producing Lactococcus Strain 20-92

Shimada

Yasuda

Takahashi

et al. 2010

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…The properties of RIR were compared with the following NADPH-dependent reductases: Pip2CR from Pseudomonas putida, 16,17) which catalyzes the enantioselective reduction of the C=N bond of Pyr2C and Pip2C to L-proline and L-pipecolic acid, and old yellow enzyme (OYE) from Candida macedoniensis, 18) which catalyzes the stereospecific reduction of the C=C bond of KIP to form (6R)-levodione. RIR is similar to these reductases as for coenzyme, inhibitor sensitivity and A B The following buffers were used at a concentration of 100 mM: sodium citrate buffer (diamond), sodium acetate buffer (square), potassium phosphate buffer (triangle), Tris/HCl buffer (circle), and glycine/NaOH buffer (x-mark).…”

Section: Comparison Of Rir With Other Nad(p)h-dependent Oxidoreductasesmentioning

confidence: 99%

Purification and Characterization of a Novel (R)-Imine Reductase fromStreptomycessp. GF3587

Mitsukura

Suzuki

Shinoda

et al. 2011

Bioscience, Biotechnology, and Biochemistry

127

104

View full text Add to dashboard Cite

“…2,[4][5][6][7][8] Hence, OYEs represent a group of enzymes with industrial interests. Although many OYE family members have been identified from yeast, bacteria, and plants recently [9][10][11][12][13][14][15][16][17][18] ) and their potential metabolic functions have been suggested, the exact physiological functions of OYEs are largely unknown. 11,[19][20][21] Gluconobacter oxydans is regarded as one of the most important industrial bacteria due to its unique ability to incompletely oxidize a wide range of carbohydrates and alcohols with excellent efficiency and regio-, stereo-, and enantio-selectivity under natural conditions.…”

mentioning

confidence: 99%

Structural insights into stereospecific reduction of α, β-unsaturated carbonyl substrates by old yellow enzyme from Gluconobacter oxydans

Yin

Deng

Lim

et al. 2015

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

show abstract

Old Yellow Enzyme fromCandida macedoniensisCatalyzes the Stereospecific Reduction of the C=C Bond of Ketoisophorone

Cited by 70 publications

References 18 publications

Cloning and Expression of a Novel NADP(H)-Dependent Daidzein Reductase, an Enzyme Involved in the Metabolism of Daidzein, from Equol-Producing Lactococcus Strain 20-92

Cloning and Expression of a Novel NADP(H)-Dependent Daidzein Reductase, an Enzyme Involved in the Metabolism of Daidzein, from Equol-Producing Lactococcus Strain 20-92

Purification and Characterization of a Novel (R)-Imine Reductase fromStreptomycessp. GF3587

Structural insights into stereospecific reduction of α, β-unsaturated carbonyl substrates by old yellow enzyme from Gluconobacter oxydans

Contact Info

Product

Resources

About