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Information on EC 1.1.1.331 - secoisolariciresinol dehydrogenase and Organism(s) Podophyllum peltatum and UniProt Accession Q94KL8

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IUBMB Comments
Isolated from the plants Forsythia intermedia and Podophyllum peltatum [1-3]. An intermediate lactol is detected in vitro.
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This record set is specific for:
Podophyllum peltatum
UNIPROT: Q94KL8
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The taxonomic range for the selected organisms is: Podophyllum peltatum
The enzyme appears in selected viruses and cellular organisms
Synonyms
secoisolariciresinol dehydrogenase, ppsdh, sdh-pph, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
(-)-secoisolariciresinol + 2 NAD+
(-)-matairesinol + 2 NADH + 2 H+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
physiological function
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SILD_PODPE
278
0
29253
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
x * 32000, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32000, calculated
homotetramer
4 * 32000, about, sequence calculation
additional information
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
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene SDH_Pp7, DNA and amino acid sequence determination and analysis, sequence comparisons, cloning and expression in Escherichia coli strain JM109, compatible codon optimization for expression in the heterologous host Pichia pastoris
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xia, Z.Q.; Costa, M.A.; Pelissier, H.C.; Davin, L.B.; Lewis, N.G.
Secoisolariciresinol dehydrogenase purification, cloning, and functional expression. Implications for human health protection
J. Biol. Chem.
276
12614-12623
2001
Forsythia x intermedia (Q94KL7), Forsythia x intermedia, Podophyllum peltatum (Q94KL8), Podophyllum peltatum
Manually annotated by BRENDA team
Youn, B.; Moinuddin, S.G.; Davin, L.B.; Lewis, N.G.; Kang, C.
Crystal structures of apo-form and binary/ternary complexes of Podophyllum secoisolariciresinol dehydrogenase, an enzyme involved in formation of health-protecting and plant defense lignans
J. Biol. Chem.
280
12917-12926
2005
Podophyllum peltatum (Q94KL8)
Manually annotated by BRENDA team
Moinuddin, S.G.; Youn, B.; Bedgar, D.L.; Costa, M.A.; Helms, G.L.; Kang, C.; Davin, L.B.; Lewis, N.G.
Secoisolariciresinol dehydrogenase: mode of catalysis and stereospecificity of hydride transfer in Podophyllum peltatum
Org. Biomol. Chem.
4
808-816
2006
Podophyllum peltatum (Q94KL8), Podophyllum peltatum
Manually annotated by BRENDA team
Arneaud, S.L.; Porter, J.R.
Investigation and expression of the secoisolariciresinol dehydrogenase gene involved in podophyllotoxin biosynthesis
Mol. Biotechnol.
57
961-973
2015
Phialocephala podophylli (A0A0M5K823), Phialocephala podophylli PPE7 (A0A0M5K823), Podophyllum peltatum (A0A0M4J2R3), Podophyllum peltatum
Manually annotated by BRENDA team