EC |
1.14.19.74 |
Accepted name: |
(+)-piperitol/(+)-sesamin synthase |
Reaction: |
(1) (+)-pinoresinol + [reduced NADPH-hemoprotein reductase] + O2 = (+)-piperitol + [oxidized NADPH-hemoprotein reductase] + 2 H2O (2) (+)-piperitol + [reduced NADPH-hemoprotein reductase] + O2 = (+)-sesamin + [oxidized NADPH-hemoprotein reductase] + 2 H2O |
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For diagram of sesamin biosynthesis, click here |
Other name(s): |
CYP81Q1; CYP81Q2; PS; PSS; SS; piperitol synthase; sesamin synthase |
Systematic name: |
(+)-pinoresinol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (cyclizing) |
Comments: |
A cytochrome P-450 (heme-thiolate) protein. Isolated from Sesamum indicum (sesame) and S. radiatum (black sesame). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ono, E., Nakai, M., Fukui, Y., Tomimori, N., Fukuchi-Mizutani, M., Saito, M., Satake, H., Tanaka, T., Katsuta, M., Umezawa, T. and Tanaka, Y. Formation of two methylenedioxy bridges by a Sesamum CYP81Q protein yielding a furofuran lignan, (+)-sesamin. Proc. Natl. Acad. Sci. USA 103 (2006) 10116–10121. [PMID: 16785429] |
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[EC 1.14.19.74 created 2018] |
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EC |
1.17.9.2 |
Accepted name: |
(+)-pinoresinol hydroxylase |
Reaction: |
(+)-pinoresinol + 2 oxidized azurin + H2O = (+)-6-hydroxypinoresinol + 2 reduced azurin + 2 H+ |
Other name(s): |
pinoresinol α-hydroxylase; pinAB (gene names) |
Systematic name: |
(+)-pinoresinol:azurin oxidoreductase |
Comments: |
Contains FAD. This enzyme, characterized from the bacterium Pseudomonas sp. SG-MS2, catalyses the incorporation of an oxygen atom originating from a water molecule into position C-6 of the lignan (+)-pinoresinol. The enzyme consists of a flavoprotein subunit and a c-type cytochrome subunit. Electrons that originate in the substrate are transferred via the FAD cofactor and the cytochrome subunit to the blue-copper protein azurin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Shettigar, M., Balotra, S., Kasprzak, A., Pearce, S.L., Lacey, M.J., Taylor, M.C., Liu, J.W., Cahill, D., Oakeshott, J.G. and Pandey, G. Oxidative catabolism of (+)-pinoresinol is initiated by an unusual flavocytochrome encoded by translationally coupled genes within a cluster of (+)-pinoresinol-coinduced genes in Pseudomonas sp. strain SG-MS2. Appl. Environ. Microbiol. 86 (2020) e00375-20. [PMID: 32198167] |
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[EC 1.17.9.2 created 2020] |
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EC |
1.23.1.1 |
Accepted name: |
(+)-pinoresinol reductase |
Reaction: |
(+)-lariciresinol + NADP+ = (+)-pinoresinol + NADPH + H+ |
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For diagram of matairesinol biosynthesis, click here |
Glossary: |
(+)-lariciresinol = 4-[(2S,3R,4R)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(+)-pinoresinol = (1S,3aR,4S,6aR)-4,4-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol) |
Other name(s): |
pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (+)-pinoresinol/(+)-lariciresinol; (+)-pinoresinol-(+)-lariciresinol reductase; PLR |
Systematic name: |
(+)-lariciresinol:NADP+ oxidoreductase |
Comments: |
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that further reduces the product to the lignan (–)-secoisolariciresinol [EC 1.23.1.2, (+)-lariciresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6]. The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L. and Lewis, N.G. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. J. Biol. Chem. 268 (1993) 27026–27033. [PMID: 8262939] |
2. |
Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A. and Lewis, N.G. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. J. Biol. Chem. 271 (1996) 29473–29482. [DOI] [PMID: 8910615] |
3. |
Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995] |
4. |
Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. J. Biol. Chem. 278 (2003) 50714–50723. [DOI] [PMID: 13129921] |
5. |
Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599] |
6. |
Bayindir, Ü., Alfermann, A.W. and Fuss, E. Hinokinin biosynthesis in Linum corymbulosum Reichenb. Plant J. 55 (2008) 810–820. [DOI] [PMID: 18489708] |
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[EC 1.23.1.1 created 2013] |
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EC |
1.23.1.2 |
Accepted name: |
(+)-lariciresinol reductase |
Reaction: |
(–)-secoisolariciresinol + NADP+ = (+)-lariciresinol + NADPH + H+ |
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For diagram of matairesinol biosynthesis, click here |
Glossary: |
(+)-lariciresinol = 4-[(2S,3R,4R)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-secoisolariciresinol = (2R,3R)-2,3-bis[(4-hydroxy-3-methoxyphenyl)methyl]butane-1,4-diol |
Other name(s): |
pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (+)-pinoresinol/(+)-lariciresinol; (+)-pinoresinol-(+)-lariciresinol reductase; PLR |
Systematic name: |
(–)-secoisolariciresinol:NADP+ oxidoreductase |
Comments: |
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (+)-pinoresinol [EC 1.23.1.1, (+)-pinoresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L. and Lewis, N.G. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. J. Biol. Chem. 268 (1993) 27026–27033. [PMID: 8262939] |
2. |
Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A. and Lewis, N.G. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. J. Biol. Chem. 271 (1996) 29473–29482. [DOI] [PMID: 8910615] |
3. |
Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995] |
4. |
Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. J. Biol. Chem. 278 (2003) 50714–50723. [DOI] [PMID: 13129921] |
5. |
Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599] |
6. |
Bayindir, Ü., Alfermann, A.W. and Fuss, E. Hinokinin biosynthesis in Linum corymbulosum Reichenb. Plant J. 55 (2008) 810–820. [DOI] [PMID: 18489708] |
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[EC 1.23.1.2 created 2013] |
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EC |
1.23.1.3 |
Accepted name: |
(–)-pinoresinol reductase |
Reaction: |
(–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+ |
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For diagram of (–)-lariciresinol biosynthesis, click here |
Glossary: |
(–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol) |
Other name(s): |
pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR |
Systematic name: |
(–)-lariciresinol:NADP+ oxidoreductase |
Comments: |
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995] |
2. |
Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599] |
3. |
Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [DOI] [PMID: 18347017] |
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[EC 1.23.1.3 created 2013] |
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EC |
1.23.1.4 |
Accepted name: |
(–)-lariciresinol reductase |
Reaction: |
(+)-secoisolariciresinol + NADP+ = (–)-lariciresinol + NADPH + H+ |
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For diagram of (#150)-lariciresinol biosynthesis, click here |
Glossary: |
(–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(+)-secoisolariciresinol = (2S,3S)-2,3-bis[(4-hydroxy-3-methoxyphenyl)methyl]butane-1,4-diol |
Other name(s): |
pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR |
Systematic name: |
(+)-secoisolariciresinol:NADP+ oxidoreductase |
Comments: |
The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (–)-pinoresinol [EC 1.23.1.3, (–)-pinoresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1] and Linum corymbulosum [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995] |
2. |
Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599] |
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[EC 1.23.1.4 created 2013] |
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