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
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General Information on EC 1.1.1.331 - secoisolariciresinol dehydrogenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
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molecular phylogenetic analysis of specialized metabolic enzyme genes from lignan-producing plants, two common gene clusters include genes from various plants and plant lineage-specific gene clusters. The specialized metabolic enzyme genes from lignan-producing plants include enzymes involved in the early common lignan biosynthesis upstream of matairesinol such as PLR and SIRD, suggesting that they have occurred in their ancestral plants and conserved their biological functions
metabolism
physiological function
additional information
metabolism
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the enzyme is involved in the lignan biosynthesis pathway, overview
metabolism
the enzyme is involved in the lignan biosynthetic pathways in Forsythia, overview
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
metabolism
Phialocephala podophylli
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway, overview. Podophyllotoxin is an important aryltetralin lignan, that possesses antitumor and antihyperlipidemic activities
metabolism
the enzyme catalyzes a step in the podophyllotoxin biosynthesis pathway
metabolism
the enzyme is involved in the enzymatic cascade for (-)-podophyllotoxin biosynthesis
metabolism
Phialocephala podophylli PPE7
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the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
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physiological function
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matairesinol biosynthesis is prominently enhanced and matairesinol is highly accumulated in callus
physiological function
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
physiological function
Phialocephala podophylli
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
physiological function
the enzyme SIRD is involved in the biosynthesis of lignan matairesinol in Forsythia. The leaves show seasonal alteration in amounts of major lignans, such as pinoresinol, matairesinol, and arctigenin, gene expression profile of secoisolariciresinol dehydrogenase (SIRD) and other related enzymes in the leaves of Forsythia suspense from April to November: all of the lignans in the leaf continuously increase from April to June, reach the maximal level in June, and then decrease
physiological function
Phialocephala podophylli PPE7
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the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
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additional information
the enzyme forms a homotetramer composed of an alpha/beta single domain structure with a dinucleotide-binding Rossmann fold for the binding of NAD+ and an active site with a highly conserved catalytic triad of amino acids, Ser153, Tyr167 and Lys171
additional information
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the enzyme forms a homotetramer composed of an alpha/beta single domain structure with a dinucleotide-binding Rossmann fold for the binding of NAD+ and an active site with a highly conserved catalytic triad of amino acids, Ser153, Tyr167 and Lys171
