BRENDA - Enzyme Database
show all sequences of 1.1.1.331

Investigation and expression of the secoisolariciresinol dehydrogenase gene involved in podophyllotoxin biosynthesis

Arneaud, S.L.; Porter, J.R.; Mol. Biotechnol. 57, 961-973 (2015)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
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
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
Podophyllum peltatum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(-)-secoisolariciresinol + 2 NAD+
Podophyllum peltatum
-
(-)-matairesinol + 2 NADH + 2 H+
-
-
?
(-)-secoisolariciresinol + 2 NAD+
Phialocephala podophylli
-
(-)-matairesinol + 2 NADH + 2 H+
-
-
?
(-)-secoisolariciresinol + 2 NAD+
Phialocephala podophylli PPE7
-
(-)-matairesinol + 2 NADH + 2 H+
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Phialocephala podophylli
A0A0M5K823
isolated from the rhizomes of Podophyllum peltatum
-
Phialocephala podophylli PPE7
A0A0M5K823
isolated from the rhizomes of Podophyllum peltatum
-
Podophyllum peltatum
A0A0M4J2R3
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(-)-secoisolariciresinol + 2 NAD+
-
743278
Podophyllum peltatum
(-)-matairesinol + 2 NADH + 2 H+
-
-
-
?
(-)-secoisolariciresinol + 2 NAD+
-
743278
Phialocephala podophylli
(-)-matairesinol + 2 NADH + 2 H+
-
-
-
?
(-)-secoisolariciresinol + 2 NAD+
-
743278
Phialocephala podophylli PPE7
(-)-matairesinol + 2 NADH + 2 H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 32000, about, sequence calculation
Podophyllum peltatum
More
the enzyme forms a homotetramer composed of an alpha/beta single domain structure with a dinucleotide-binding Rossmann fold for the binding of NAD+ and an active site with a highly conserved catalytic triad of amino acids, Ser153, Tyr167 and Lys171
Podophyllum peltatum
Synonyms
Synonyms
Commentary
Organism
PpSD
-
Podophyllum peltatum
SDH_Pp7
-
Podophyllum peltatum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Phialocephala podophylli
30
-
assay at
Podophyllum peltatum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
assay at
Phialocephala podophylli
8.8
-
assay at
Podophyllum peltatum
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Phialocephala podophylli
NAD+
-
Podophyllum peltatum
Cloned(Commentary) (protein specific)
Commentary
Organism
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
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
Podophyllum peltatum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Phialocephala podophylli
NAD+
-
Podophyllum peltatum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(-)-secoisolariciresinol + 2 NAD+
Podophyllum peltatum
-
(-)-matairesinol + 2 NADH + 2 H+
-
-
?
(-)-secoisolariciresinol + 2 NAD+
Phialocephala podophylli
-
(-)-matairesinol + 2 NADH + 2 H+
-
-
?
(-)-secoisolariciresinol + 2 NAD+
Phialocephala podophylli PPE7
-
(-)-matairesinol + 2 NADH + 2 H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(-)-secoisolariciresinol + 2 NAD+
-
743278
Podophyllum peltatum
(-)-matairesinol + 2 NADH + 2 H+
-
-
-
?
(-)-secoisolariciresinol + 2 NAD+
-
743278
Phialocephala podophylli
(-)-matairesinol + 2 NADH + 2 H+
-
-
-
?
(-)-secoisolariciresinol + 2 NAD+
-
743278
Phialocephala podophylli PPE7
(-)-matairesinol + 2 NADH + 2 H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 32000, about, sequence calculation
Podophyllum peltatum
More
the enzyme forms a homotetramer composed of an alpha/beta single domain structure with a dinucleotide-binding Rossmann fold for the binding of NAD+ and an active site with a highly conserved catalytic triad of amino acids, Ser153, Tyr167 and Lys171
Podophyllum peltatum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Phialocephala podophylli
30
-
assay at
Podophyllum peltatum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
assay at
Phialocephala podophylli
8.8
-
assay at
Podophyllum peltatum
General Information
General Information
Commentary
Organism
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
Phialocephala podophylli
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
Podophyllum peltatum
additional information
the enzyme forms a homotetramer composed of an alpha/beta single domain structure with a dinucleotide-binding Rossmann fold for the binding of NAD+ and an active site with a highly conserved catalytic triad of amino acids, Ser153, Tyr167 and Lys171
Podophyllum peltatum
physiological function
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
Phialocephala podophylli
physiological function
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
Podophyllum peltatum
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
Phialocephala podophylli
metabolism
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway
Podophyllum peltatum
additional information
the enzyme forms a homotetramer composed of an alpha/beta single domain structure with a dinucleotide-binding Rossmann fold for the binding of NAD+ and an active site with a highly conserved catalytic triad of amino acids, Ser153, Tyr167 and Lys171
Podophyllum peltatum
physiological function
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
Phialocephala podophylli
physiological function
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
Podophyllum peltatum
Other publictions for EC 1.1.1.331
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743611
Shiraishi
De novo transcriptomes of For ...
Forsythia koreana
PLoS ONE
11
e0164805
2016
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1
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-
-
-
-
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1
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9
-
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3
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1
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4
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1
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1
1
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1
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3
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1
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1
3
3
1
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-
743278
Arneaud
Investigation and expression ...
Phialocephala podophylli, Phialocephala podophylli PPE7, Podophyllum peltatum
Mol. Biotechnol.
57
961-973
2015
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2
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3
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8
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2
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3
2
2
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2
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5
5
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-
741681
Kuo
Bioconversion of pinoresinol ...
Dysosma pleiantha
Appl. Environ. Microbiol.
80
2687-2692
2014
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-
1
-
1
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1
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1
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5
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1
3
2
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2
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2
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742033
Morimoto
Seasonal alteration in amount ...
Forsythia x intermedia
Biol. Pharm. Bull.
36
1519-1523
2013
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3
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1
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2
2
-
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743768
Wankhede
Expressed sequence tags and m ...
Sinopodophyllum hexandrum
Protoplasma
250
1239-1249
2013
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1
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1
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6
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5
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1
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1
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5
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1
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1
1
1
1
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720203
Lan
-
Molecular cloning and characte ...
Dysosma tsayuensis
J. Med. Plant Res.
4
484-489
2010
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1
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1
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1
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5
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1
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5
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1
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1
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720614
Moinuddin
Secoisolariciresinol dehydroge ...
Podophyllum peltatum
Org. Biomol. Chem.
4
808-816
2006
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3
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4
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1
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1
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1
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3
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1
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1
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719829
Youn
Crystal structures of apo-form ...
Podophyllum peltatum
J. Biol. Chem.
280
12917-12926
2005
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1
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4
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1
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720350
Okunishi
-
Stereochemistry of matairesino ...
Daphne genkwa, Daphne odora
J. Wood Sci.
50
77-81
2004
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719805
Xia
Secoisolariciresinol dehydroge ...
Forsythia x intermedia, Podophyllum peltatum
J. Biol. Chem.
276
12614-12623
2001
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2
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2
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