Information on EC 1.1.1.331 - secoisolariciresinol dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.331
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RECOMMENDED NAME
GeneOntology No.
secoisolariciresinol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(-)-secoisolariciresinol + 2 NAD+ = (-)-matairesinol + 2 NADH + 2 H+
show the reaction diagram
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
249765-11-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
Daphne odora
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3500
wild-type, pH 8.8, 22°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Daphne odora
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Manually annotated by BRENDA team
low expression
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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