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Enzyme Nomenclature
Information on EC 1.1.1.331 - secoisolariciresinol dehydrogenase
Word Map on EC 1.1.1.331
- 1.1.1.331
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lignans
- matairesinol
- podophyllum
- forsythia
- podophyllotoxin
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anticancer
- intermedia
- enterolactone
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antiviral
- peltatum
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enantiospecific
- etoposide
- teniposide
- glucosides
- rhizome
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bioconversion
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short-chain
-
semi-synthetic
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cancer-preventative
-
ingestion
- enterodiol
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phytoestrogens
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.331
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RECOMMENDED NAME
GeneOntology No.
secoisolariciresinol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(-)-secoisolariciresinol + 2 NAD+ = (-)-matairesinol + 2 NADH + 2 H+
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SYSTEMATIC NAME
IUBMB Comments
(-)-secoisolariciresinol:NAD+ oxidoreductase
Isolated from the plants Forsythia intermedia [1] and Podophyllum peltatum [1-3]. An intermediate lactol is detected in vitro.
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CAS REGISTRY NUMBER
COMMENTARY
249765-11-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
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product is optically pure, more than 99% enantiomeric excess. (-)-Matairesinol is formed preferentially in the in vitro reactions with enzyme preparations. The opposite (+)-enantiomer is isolated from Daphne genkwa shoot
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?
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
Daphne odora
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product is optically pure, more than 99% enantiomeric excess. (-)-Matairesinol is formed preferentially in the in vitro reactions with enzyme preparations. The opposite (+)-enantiomer is isolated from Daphne odora callus
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?
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
conversion is enantiospecific, reaction proceeds via the corresponding lactol intermediate
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-
?
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
conversion is enantiospecific, reaction proceeds via the corresponding lactol intermediate
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-
?
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
NAD+ binds first followed by the substrate (-)-secoisolariciresinol. For hydride transfer, the incoming hydride abstracted from the substrate takes up the pro-S position in the NADH formed
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-
?
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
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nicotinamide and the substrate are in the proper orientation for the well established B-face-specific hydride transfer to C-4 from the corresponding substrate reaction center, crystallization data. The Lys171 residue lowers the pKa of the phenolic hydroxyl group of the Tyr167 in the catalytic triad together with the positively charged NAD+. The Ser153 residue then shares its proton with the phenolic anionic group of Tyr167, and in this way, the latter can serve as a general base in substrate deprotonation during catalysis. Concomitant deprotonation of the (-)-secoisolariciresinol is then presumed to occur via the phenolic anion of Tyr167 with hydride transfer to NAD+, followed by nucleophilic attack to form the (-)-lactol intermediate from (-)-secoisolariciresinol. Subsequent dehydrogenation of the (-)-lactol can then occur by the same process involving Tyr167 as before and a newly bound NAD+ molecule to afford the dibenzyl furanone, (-)-matairesinol
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
no expression detected in leaf and flower. The expression levels of enzyme are not consistent with the amounts of podophyllotxin in the tissues tested
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.331)
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