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
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Manually annotated by BRENDA team
i.e Dysosma pleiantha
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Phialocephala podophylli
isolated from the rhizomes of Podophyllum peltatum
UniProt
Manually annotated by BRENDA team
Phialocephala podophylli PPE7
isolated from the rhizomes of Podophyllum peltatum
UniProt
Manually annotated by BRENDA team
cvs. Yada and Jobrang
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.231
(-)-secoisolariciresinol
pH 8.8, 20C, recombinant His-tagged enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3500
wild-type, pH 8.8, 22C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
recombinant His-tagged fusion enzyme Sdh-PpH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
recombinant His-tagged Sdh
22
recombinant His-tagged fusion enzyme Sdh-PpH
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29200
x * 29200, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme SDH and bifunctional fusion enzyme PLR-SDH from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, cloning and expression in Escherichiaa coli strain JM109. Confirmation that the SD gene sequence originates from Phialocephala podophylli strain PPE7 fungal gDNA and is not a product from amplification of Podophyllum peltatum gDNA plant contamination is achieved through PCR amplification of any contaminating rbcL plant gene sequences in the PPE7 fungal gDNA template samples
Phialocephala podophylli
expression in Escherichia coli
gene FkSIRD, DNA and amino acid sequence determination and analysis from Forsythia genome, phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
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gene PhSDH, sequence comparisons, semiquantitative RT-PCR expression analysis
gene sdh-PpH, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain M15. Genes plr-PpH, encoding pinoresinol-lariciresinol reductase (PLR), and sdh-PpH are linked to form two bifunctional fusion genes, plr-sdh and sdh-plr, which are expressed as functional His-tagged proteins in Escherichia coli strain M15. Establishment of a high-efficiency system for the conversion of (+)-pinoresinol to (-)-matairesinol in Escherichia coli expressing a Sdh-PpH fusion protein
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
all of the enzymes responsible for the biosynthesis of lignan aglycones, also SIRD, are upregulated in callus
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the enzyme expression is induced by wounding and methyl jasmonate, while UV light induces short peaks of the enzyme expression after 6 h intervals, expression pattern of PhSDH in different tissues and under abiotic stress, overview
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
additional information