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
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
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
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
seasonal alteration in amounts of major lignans, such as pinoresinol, matairesinol, and arctigenin, analysis of gene expression profile of secoisolariciresinol dehydrogenase (SIRD) and other related enzymes in the leaves of Forsythia suspense from April to November. The SIRD expression is prominent from April to May, not detected in June to July, and then increases again from September to November. All of the lignans in the leaf continuously increase from April to June, reach the maximal level in June, and then decrease
tissue- and species-specific expression of the lignan biosynthesis-related gene FkSIRD, transcriptome analysis, overview. The expression levels of DIR, PLR, SIRD, and MOMT are 40fold, 5fold, 50fold, and 2fold higher in callus than in leaf, respectively
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
the enzyme is part of the podophyllotoxin, PPT, biosynthetic pathway, overview. Podophyllotoxin is an important aryltetralin lignan, that possesses antitumor and antihyperlipidemic activities
the enzyme SIRD is involved in the biosynthesis of lignan matairesinol in Forsythia. The leaves show seasonal alteration in amounts of major lignans, such as pinoresinol, matairesinol, and arctigenin, gene expression profile of secoisolariciresinol dehydrogenase (SIRD) and other related enzymes in the leaves of Forsythia suspense from April to November: all of the lignans in the leaf continuously increase from April to June, reach the maximal level in June, and then decrease
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
the enzyme secoisolariciresinol dehydrogenase facilitates the dehydrogenation of secoisolariciresinol to form matairesinol, a mid-pathway intermediate product in podophyllotoxin, PPT, biosynthesis
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
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
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
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
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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
the two genes, termed plr-PpH and sdh-PpH, encoding pinoresinol-lariciresinol reductase (PLR) and secoisolariciresinol dehydrogenase (SDH), are linked to form two bifunctional fusion genes, plr-sdh and sdh-plr, which are expressed in Escherichia coli and purified. The proteins are linked via a (GGGGS)4 protein linker to maintain flexibility. Bioconversion in vitro at 22°C for 60 min shows that the conversion efficiency of fusion protein PLR-SDH is higher than that of the mixture of recombinant PLR and reacombinant SDH. The percent conversion of (+)-pinoresinol to matairesinol is 49.8% using PLR-SDH and only 17.7% using a mixture of rPLR and rSDH. Conversion of (+)-pinoresinol by fusion protein SDH-PLR stops at the intermediate product, secoisolariciresinol. In vivo, (+)-pinoresinol is completely converted to matairesinol by living recombinant Escherichia coli expressing PLR-SDH without addition of cofactors
the two genes, termed plr-PpH and sdh-PpH, encoding pinoresinol-lariciresinol reductase (PLR) and secoisolariciresinol dehydrogenase (SDH), are linked to form two bifunctional fusion genes, plr-sdh and sdh-plr, which are expressed in Escherichia coli and purified. The proteins are linked via a (GGGGS)4 protein linker to maintain flexibility. Bioconversion in vitro at 22°C for 60 min shows that the conversion efficiency of fusion protein PLR-SDH is higher than that of the mixture of recombinant PLR and reacombinant SDH. The percent conversion of (+)-pinoresinol to matairesinol is 49.8% using PLR-SDH and only 17.7% using a mixture of rPLR and rSDH. Conversion of (+)-pinoresinol by fusion protein SDH-PLR stops at the intermediate product, secoisolariciresinol. In vivo, (+)-pinoresinol is completely converted to matairesinol by living recombinant Escherichia coli expressing PLR-SDH without addition of cofactors
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
gene FkSIRD, DNA and amino acid sequence determination and analysis from Forsythia genome, phylogenetic analysis, quantitative RT-PCR enzyme 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
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
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
Lan, X.; Ren, S.; Yang, Y.; Chen, M.; Yang, C.; Quan, H.; Zhong, G.; Liao, Z.
Molecular cloning and characterization of the secoisolariciresinol dehydrogenase gene involved in podophyllotoxin biosynthetic pathway from Tibet Dysosma
De novo transcriptomes of Forsythia koreana using a novel assembly method insight into tissue- and species-specific expression of lignan biosynthesis-related gene