1.1.1.331: secoisolariciresinol dehydrogenase
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For detailed information about secoisolariciresinol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.331
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1.1.1.331
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lignans
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podophyllotoxin
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forsythia
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podophyllum
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intermedia
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enterolactone
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plr
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hexandrum
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etoposide
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teniposide
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single-shot
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peltatum
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enantiospecific
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phase-shifting
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holography
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hologram
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pinoresinol-lariciresinol
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enterodiol
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koreana
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semi-synthetic
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pixel
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linum
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phytoestrogens
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+-pinoresinol
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versipellis
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cancer-preventative
- 1.1.1.331
-
lignans
- podophyllotoxin
- forsythia
- podophyllum
- intermedia
- enterolactone
- plr
- hexandrum
- etoposide
- teniposide
-
single-shot
- peltatum
-
enantiospecific
-
phase-shifting
-
holography
-
hologram
-
pinoresinol-lariciresinol
- enterodiol
- koreana
-
semi-synthetic
-
pixel
- linum
-
phytoestrogens
-
+-pinoresinol
- versipellis
-
cancer-preventative
Reaction
Synonyms
FkSIRD, matairesinol biosynthetic enzyme, PhSDH, PpSD, PpSDH, SDH, sdh-PpH, SDH_Pp7, secoisolariciresinol dehydrogenase, SirD, SSDH
ECTree
1.1.1.331 secoisolariciresinol dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.1.1.331 - secoisolariciresinol dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K171A
mutation in conserved catalytic triad, complete loss of activity
S153A
mutation in conserved catalytic triad, severe reduction of activity
Y167A
mutation in conserved catalytic triad, complete loss of activity
additional information
additional information
the two genes, termed plr-PpH and sdh-PpH, encoding pinoresinol-lariciresinol reductase (PLR) and secoisolariciresinol dehydrogenase (SDH), are linked to form two bifunctional fusion genes, plr-sdh and sdh-plr, which are expressed in Escherichia coli and purified. The proteins are linked via a (GGGGS)4 protein linker to maintain flexibility. Bioconversion in vitro at 22°C for 60 min shows that the conversion efficiency of fusion protein PLR-SDH is higher than that of the mixture of recombinant PLR and reacombinant SDH. The percent conversion of (+)-pinoresinol to matairesinol is 49.8% using PLR-SDH and only 17.7% using a mixture of rPLR and rSDH. Conversion of (+)-pinoresinol by fusion protein SDH-PLR stops at the intermediate product, secoisolariciresinol. In vivo, (+)-pinoresinol is completely converted to matairesinol by living recombinant Escherichia coli expressing PLR-SDH without addition of cofactors
additional information
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the two genes, termed plr-PpH and sdh-PpH, encoding pinoresinol-lariciresinol reductase (PLR) and secoisolariciresinol dehydrogenase (SDH), are linked to form two bifunctional fusion genes, plr-sdh and sdh-plr, which are expressed in Escherichia coli and purified. The proteins are linked via a (GGGGS)4 protein linker to maintain flexibility. Bioconversion in vitro at 22°C for 60 min shows that the conversion efficiency of fusion protein PLR-SDH is higher than that of the mixture of recombinant PLR and reacombinant SDH. The percent conversion of (+)-pinoresinol to matairesinol is 49.8% using PLR-SDH and only 17.7% using a mixture of rPLR and rSDH. Conversion of (+)-pinoresinol by fusion protein SDH-PLR stops at the intermediate product, secoisolariciresinol. In vivo, (+)-pinoresinol is completely converted to matairesinol by living recombinant Escherichia coli expressing PLR-SDH without addition of cofactors
additional information
assembly of plant enzymes in Escherichia coli for the production of the valuable (-)-podophyllotoxin precursor (-)-pluviatolide. (-)-Pluviatolide is considered a crossroad compound in lignan biosynthesis, because the methylenedioxy bridge in its structure, resulting from the oxidation of (-)-matairesinol, channels the biosynthetic pathway toward the microtubule depolymerizer (-)-podophyllotoxin. This oxidation reaction is catalyzed with high regio- and enantioselectivity by a cytochrome P450 monooxygenase from Sinopodophyllum hexandrum (CYP719A23), which is expressed and optimized regarding redox partners in Escherichia coli. Pinoresinol-lariciresinol reductase from Forsythia intermedia (FiPLR), secoisolariciresinol dehydrogenase from Podophyllum pleianthum (PpSDH), and CYP719A23 are coexpressed together with a suitable NADPH-dependent reductase to ensure P450 activity, allowing for four sequential biotransformations without intermediate isolation. By using an Escherichia coli strain coexpressing the enzymes originating from four plants, (+)-pinoresinol is efficiently converted, allowing the isolation of enantiopure (-)-pluviatolide at a concentration of 137 mg/l (enantiomeric excess over 99% with 76% isolated yield), reaction scheme and method, overview
additional information
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assembly of plant enzymes in Escherichia coli for the production of the valuable (-)-podophyllotoxin precursor (-)-pluviatolide. (-)-Pluviatolide is considered a crossroad compound in lignan biosynthesis, because the methylenedioxy bridge in its structure, resulting from the oxidation of (-)-matairesinol, channels the biosynthetic pathway toward the microtubule depolymerizer (-)-podophyllotoxin. This oxidation reaction is catalyzed with high regio- and enantioselectivity by a cytochrome P450 monooxygenase from Sinopodophyllum hexandrum (CYP719A23), which is expressed and optimized regarding redox partners in Escherichia coli. Pinoresinol-lariciresinol reductase from Forsythia intermedia (FiPLR), secoisolariciresinol dehydrogenase from Podophyllum pleianthum (PpSDH), and CYP719A23 are coexpressed together with a suitable NADPH-dependent reductase to ensure P450 activity, allowing for four sequential biotransformations without intermediate isolation. By using an Escherichia coli strain coexpressing the enzymes originating from four plants, (+)-pinoresinol is efficiently converted, allowing the isolation of enantiopure (-)-pluviatolide at a concentration of 137 mg/l (enantiomeric excess over 99% with 76% isolated yield), reaction scheme and method, overview
additional information
podophyllotoxin biosynthesis pathway genes expression at low temperature. The low temperature enhances the podophyllotoxin accumulation in Dysosma versipellis
