1.1.1.331: secoisolariciresinol dehydrogenase
This is an abbreviated version!
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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Crystallization
Crystallization on EC 1.1.1.331 - secoisolariciresinol dehydrogenase
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crystal structures of the apo-form and binary/ternary complexes at 1.6, 2.8, and 2.0 A resolution, respectively. The enzyme is a homotetramer, consisting of an alpha/beta single domain monomer containing seven parallel beta-strands flanked by eight alpha-helices on both sides. Its overall monomeric structure shows a conserved Asp47 residue forming a hydrogen bond with both hydroxyl groups of the adenine ribose of NAD(H), and thus specificity toward NAD(H) instead of NADP(H). The highly conserved catalytic triad Ser153, Tyr167, and Lys171 is adjacent to both NAD(H) and substrate molecules, where Tyr167 functions as a general base