메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Genes encoding norcoclaurine synthase occur as tandem fusions in the Papaveraceae

Author keywords

[No Author keywords available]

Indexed keywords

ALKALOID; BENZYLISOQUINOLINE DERIVATIVE; COMPLEMENTARY DNA; LIGASE; NORCOCLAURINE SYNTHASE; PLANT PROTEIN; RECOMBINANT PROTEIN;

EID: 85006743879     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep39256     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 0001322468 scopus 로고
    • (S)-Norcoclaurine is the central intermediate in benzylisoquinoline alkaloid biosynthesis
    • Stadler, R., Kutchan, T. M. & Zenk, M. H. (S)-Norcoclaurine is the central intermediate in benzylisoquinoline alkaloid biosynthesis. Phytochemistry 28, 1083-1086 (1989).
    • (1989) Phytochemistry , vol.28 , pp. 1083-1086
    • Stadler, R.1    Kutchan, T.M.2    Zenk, M.H.3
  • 2
    • 84986720789 scopus 로고
    • A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline reticuline
    • Stadler, R. & Zenk, M. H. A revision of the generally accepted pathway for the biosynthesis of the benzyltetrahydroisoquinoline reticuline. Liebigs Ann. Chem. 555-562 (1990).
    • (1990) Liebigs Ann. Chem , pp. 555-562
    • Stadler, R.1    Zenk, M.H.2
  • 3
    • 79952855766 scopus 로고    scopus 로고
    • Phosphate mediated biomimetic synthesis of tetrahydroisoquinoline alkaloids
    • Pesnot, T., Gershater, M. C., Ward, J. M. & Hailes, H. C. Phosphate mediated biomimetic synthesis of tetrahydroisoquinoline alkaloids. Chem. Commun. 47, 3242-3244 (2011).
    • (2011) Chem. Commun , vol.47 , pp. 3242-3244
    • Pesnot, T.1    Gershater, M.C.2    Ward, J.M.3    Hailes, H.C.4
  • 4
    • 84878001183 scopus 로고    scopus 로고
    • Biochemical genomics to investigate benzylisoquinoline alkaloid biosynthesis in opium poppy and related plants
    • Hagel, J. M. & Facchini, P. J. Biochemical genomics to investigate benzylisoquinoline alkaloid biosynthesis in opium poppy and related plants. Plant Cell Physiol. 54, 647-672 (2013).
    • (2013) Plant Cell Physiol , vol.54 , pp. 647-672
    • Hagel, J.M.1    Facchini, P.J.2
  • 5
    • 0034778394 scopus 로고    scopus 로고
    • Isolation and partial characterization of norcoclaurine synthase, the first committed step in benzylisoquinoline alkaloid biosynthesis, from opium poppy
    • Samanani, N. & Facchini, P. J. Isolation and partial characterization of norcoclaurine synthase, the first committed step in benzylisoquinoline alkaloid biosynthesis, from opium poppy. Planta 213, 898-906 (2001).
    • (2001) Planta , vol.213 , pp. 898-906
    • Samanani, N.1    Facchini, P.J.2
  • 6
    • 0037072805 scopus 로고    scopus 로고
    • Purification and characterization of norcoclaurine synthase the first committed enzyme in benzylisoquinoline alkaloid biosynthesis in plants
    • Samanani, N. & Facchini, P. J. Purification and characterization of norcoclaurine synthase. The first committed enzyme in benzylisoquinoline alkaloid biosynthesis in plants. J. Biol. Chem. 277, 33878-33883 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 33878-33883
    • Samanani, N.1    Facchini, P.J.2
  • 7
    • 6444243887 scopus 로고    scopus 로고
    • Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis
    • Samanani, N., Liscombe, D. K. & Facchini, P. J. Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis. Plant J. 40, 302-313 (2004).
    • (2004) Plant J , vol.40 , pp. 302-313
    • Samanani, N.1    Liscombe, D.K.2    Facchini, P.J.3
  • 8
    • 20444396193 scopus 로고    scopus 로고
    • Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms
    • Liscombe, D. K., MacLeod, B. P., Loukanina, N., Nandi, O. I. & Facchini, P. J. Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms. Phytochemistry 66, 2501-2520 (2005).
    • (2005) Phytochemistry , vol.66 , pp. 2501-2520
    • Liscombe, D.K.1    MacLeod, B.P.2    Loukanina, N.3    Nandi, O.I.4    Facchini, P.J.5
  • 9
    • 84909606614 scopus 로고    scopus 로고
    • Enlarging the toolbox for allergen epitope definition with an allergen-Type model protein
    • Berkner, H. et al. Enlarging the toolbox for allergen epitope definition with an allergen-Type model protein. PLoS ONE 9, e11169 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e11169
    • Berkner, H.1
  • 10
    • 34548478116 scopus 로고    scopus 로고
    • Mechanistic studies on norcoclaurine synthase of benzylisoquinoline alkaloid biosynthesis: An enzymatic Pictet-Spengler reaction
    • Luk, L. Y., Bunn, S., Liscombe, D. K., Facchini, P. J. & Tanner, M. E. Mechanistic studies on norcoclaurine synthase of benzylisoquinoline alkaloid biosynthesis: An enzymatic Pictet-Spengler reaction. Biochemistry 46, 10153-10161 (2007).
    • (2007) Biochemistry , vol.46 , pp. 10153-10161
    • Luk, L.Y.1    Bunn, S.2    Liscombe, D.K.3    Facchini, P.J.4    Tanner, M.E.5
  • 11
    • 77951848665 scopus 로고    scopus 로고
    • Norcoclaurine synthase: Mechanism of an enantioselective Pictet-Spengler catalyzing enzyme
    • Bonamore, A., Barba, M., Botta, B., Boffi, A. & Macone, A. Norcoclaurine synthase: Mechanism of an enantioselective Pictet-Spengler catalyzing enzyme. Molecules 15, 2070-2078 (2010).
    • (2010) Molecules , vol.15 , pp. 2070-2078
    • Bonamore, A.1    Barba, M.2    Botta, B.3    Boffi, A.4    Macone, A.5
  • 12
    • 48149084475 scopus 로고    scopus 로고
    • Conformation, catalytic site, and enzymatic mechanism of the PR10 allergenrelated enzyme norcoclaurine synthase
    • Berkner, H., Schweimer, K., Matecko, I. & Rösch, P. Conformation, catalytic site, and enzymatic mechanism of the PR10 allergenrelated enzyme norcoclaurine synthase. Biochem. J. 413, 281-290 (2008).
    • (2008) Biochem. J , vol.413 , pp. 281-290
    • Berkner, H.1    Schweimer, K.2    Matecko, I.3    Rösch, P.4
  • 13
    • 41949092539 scopus 로고    scopus 로고
    • Cloning, expression, crystallization and preliminary X-ray data analysis of norcoclaurine synthase from Thalictrum flavum
    • Pasquo, A. et al. Cloning, expression, crystallization and preliminary X-ray data analysis of norcoclaurine synthase from Thalictrum flavum. Acta Crystallogr. F64, 281-283 (2008).
    • (2008) Acta Crystallogr , vol.64 , pp. 281-283
    • Pasquo, A.1
  • 14
    • 59449099013 scopus 로고    scopus 로고
    • Structural basis of enzymatic (S)-norcoclaurine biosynthesis
    • Ilari, A. et al. Structural basis of enzymatic (S)-norcoclaurine biosynthesis. J. Biol. Chem. 284, 897-904 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 897-904
    • Ilari, A.1
  • 15
    • 77956389962 scopus 로고    scopus 로고
    • An enzymatic, stereoselective synthesis of (S)-norcoclaurine
    • Bonamore, A. et al. An enzymatic, stereoselective synthesis of (S)-norcoclaurine. Green Chem. 12, 1623-1627 (2010).
    • (2010) Green Chem , vol.12 , pp. 1623-1627
    • Bonamore, A.1
  • 16
    • 84856214491 scopus 로고    scopus 로고
    • Biocatalytic production of tetrahydroisoquinolines
    • Ruff, B. M., Brase, S. & OConnor, S. E. Biocatalytic production of tetrahydroisoquinolines. Tetrahedron Lett. 53, 1071-1074 (2012).
    • (2012) Tetrahedron Lett , vol.53 , pp. 1071-1074
    • Ruff, B.M.1    Brase, S.2    Oconnor, S.E.3
  • 17
    • 84922782409 scopus 로고    scopus 로고
    • Asymmetric synthesis of tetrahydroisoquinolines by enzymatic Pictet-Spengler reaction
    • Nishihachijo, M. et al. Asymmetric synthesis of tetrahydroisoquinolines by enzymatic Pictet-Spengler reaction. Biosci. Biotechnol. Biochem. 78, 701-707 (2014).
    • (2014) Biosci. Biotechnol. Biochem , vol.78 , pp. 701-707
    • Nishihachijo, M.1
  • 18
    • 44949247292 scopus 로고    scopus 로고
    • Microbial production of plant benzylisoquinoline alkaloids
    • Minami, H. et al. Microbial production of plant benzylisoquinoline alkaloids. Proc. Natl. Acad. Sci. USA 105, 7393-7398 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7393-7398
    • Minami, H.1
  • 19
    • 49949088247 scopus 로고    scopus 로고
    • Production of benzylisoquinoline alkaloids in Saccharomyces cerevisiae
    • Hawkins, K. M. & Smolke, C. D. Production of benzylisoquinoline alkaloids in Saccharomyces cerevisiae. Nat. Chem. Biol. 4, 564-573 (2008).
    • (2008) Nat. Chem. Biol , vol.4 , pp. 564-573
    • Hawkins, K.M.1    Smolke, C.D.2
  • 20
    • 79957546214 scopus 로고    scopus 로고
    • A bacterial platform for fermentative production of plant alkaloids
    • Nakagawa, A. et al. A bacterial platform for fermentative production of plant alkaloids. Nat. Commun. 2, 326 (2011).
    • (2011) Nat. Commun , vol.2 , pp. 326
    • Nakagawa, A.1
  • 21
    • 84931573824 scopus 로고    scopus 로고
    • An enzyme-coupled biosensor enables (S)-reticuline production in yeast from glucose
    • DeLoache, W. C. et al. An enzyme-coupled biosensor enables (S)-reticuline production in yeast from glucose. Nat. Chem. Biol. 11, 465-471 (2015).
    • (2015) Nat. Chem. Biol , vol.11 , pp. 465-471
    • DeLoache, W.C.1
  • 22
    • 84938063531 scopus 로고    scopus 로고
    • De novo production of the key branch point benzylisoquinoline alkaloid reticuline in yeast
    • Trenchard, I. J., Siddiqui, M. S., Thodey, K. & Smolke, C. D. De novo production of the key branch point benzylisoquinoline alkaloid reticuline in yeast. Metab. Eng. 31, 74-83 (2015).
    • (2015) Metab. Eng , vol.31 , pp. 74-83
    • Trenchard, I.J.1    Siddiqui, M.S.2    Thodey, K.3    Smolke, C.D.4
  • 23
    • 84941346066 scopus 로고    scopus 로고
    • Complete biosynthesis of opioids in yeast
    • Galanie, S. et al. Complete biosynthesis of opioids in yeast. Science 349, 1095-1100 (2015).
    • (2015) Science , vol.349 , pp. 1095-1100
    • Galanie, S.1
  • 24
    • 84957553896 scopus 로고    scopus 로고
    • Total biosynthesis of opiates by stepwise fermentation using engineered Escherichia coli
    • Nakagawa, A. et al. Total biosynthesis of opiates by stepwise fermentation using engineered Escherichia coli. Nat. Commun. 7, 10390 (2016).
    • (2016) Nat. Commun , vol.7 , pp. 10390
    • Nakagawa, A.1
  • 25
    • 84869046649 scopus 로고    scopus 로고
    • The catalytic potential of Coptis japonica NCS2 revealed-development and utilisation of a fluorescamine-based assay
    • Pesnot, T., Gershater, M. C., Ward, J. M. & Hailes, H. C. The catalytic potential of Coptis japonica NCS2 revealed-development and utilisation of a fluorescamine-based assay. Adv. Synth. Catal. 354, 2997-3008 (2012).
    • (2012) Adv. Synth. Catal , vol.354 , pp. 2997-3008
    • Pesnot, T.1    Gershater, M.C.2    Ward, J.M.3    Hailes, H.C.4
  • 26
    • 84925636078 scopus 로고    scopus 로고
    • Dopamine-first mechanism enables the rational engineering of the norcoclaurine synthase aldehyde activity profile
    • Lichman, B. R. et al. Dopamine-first mechanism enables the rational engineering of the norcoclaurine synthase aldehyde activity profile. FEBS J. 282, 1137-1151 (2015).
    • (2015) FEBS J , vol.282 , pp. 1137-1151
    • Lichman, B.R.1
  • 27
    • 84874990225 scopus 로고    scopus 로고
    • Engineering specialized metabolic pathways-is there room for enzyme improvement?
    • Bar-Even, A. & Tawfik, D. S. Engineering specialized metabolic pathways-is there room for enzyme improvement? Curr. Opin. Biotechnol. 24, 310-319 (2012).
    • (2012) Curr. Opin. Biotechnol , vol.24 , pp. 310-319
    • Bar-Even, A.1    Tawfik, D.S.2
  • 28
    • 84879541446 scopus 로고    scopus 로고
    • Transcriptome analysis based on next-generation sequencing of non-model plants producing specialized metabolites of biotechnological interest
    • Xiao, M. et al. Transcriptome analysis based on next-generation sequencing of non-model plants producing specialized metabolites of biotechnological interest. J. Biotechnol. 166, 122-134 (2013).
    • (2013) J. Biotechnol , vol.166 , pp. 122-134
    • Xiao, M.1
  • 29
    • 78649499936 scopus 로고    scopus 로고
    • Norcoclaurine synthase is a member of the pathogenesis-related 10/Bet v1 protein family
    • Lee, E. J. & Facchini, P. J. Norcoclaurine synthase is a member of the pathogenesis-related 10/Bet v1 protein family. Plant Cell 22, 3489-3503 (2010).
    • (2010) Plant Cell , vol.22 , pp. 3489-3503
    • Lee, E.J.1    Facchini, P.J.2
  • 30
    • 34250332680 scopus 로고    scopus 로고
    • Functional analysis of norcoclaurine synthase in Coptis japonica
    • Minami, H., Dubouzet, E., Iwasa, K. & Sato, F. Functional analysis of norcoclaurine synthase in Coptis japonica. J. Biol. Chem. 282, 6274-6282 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 6274-6282
    • Minami, H.1    Dubouzet, E.2    Iwasa, K.3    Sato, F.4
  • 31
    • 84860361674 scopus 로고    scopus 로고
    • Subcellular localization of sanguinarine biosynthetic enzymes in cultured opium poppy cells
    • Hagel, J. M. & Facchini, P. J. Subcellular localization of sanguinarine biosynthetic enzymes in cultured opium poppy cells. In Vitro Cell Devel. Biol. Plant 48, 233-240 (2012).
    • (2012) Vitro Cell Devel. Biol. Plant , vol.48 , pp. 233-240
    • Hagel, J.M.1    Facchini, P.J.2
  • 32
    • 84877156114 scopus 로고    scopus 로고
    • Effect of signal peptide on stability and folding of Escherichia coli thioredoxin
    • Singh, P. et al. Effect of signal peptide on stability and folding of Escherichia coli thioredoxin. PLoS ONE 8, e63442 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e63442
    • Singh, P.1
  • 34
    • 84939563893 scopus 로고    scopus 로고
    • Stereochemical inversion of (S)-reticuline by a cytochrome P450 fusion in opium poppy
    • Farrow, S. C., Hagel, J. M., Beaudoin, G. A., Burns, D. C. & Facchini, P. J. Stereochemical inversion of (S)-reticuline by a cytochrome P450 fusion in opium poppy. Nat. Chem. Biol. 11, 728-732 (2015).
    • (2015) Nat. Chem. Biol , vol.11 , pp. 728-732
    • Farrow, S.C.1    Hagel, J.M.2    Beaudoin, G.A.3    Burns, D.C.4    Facchini, P.J.5
  • 35
    • 84937845964 scopus 로고    scopus 로고
    • Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein
    • Winzer, T. et al. Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein. Science 349, 309-312 (2015).
    • (2015) Science , vol.349 , pp. 309-312
    • Winzer, T.1
  • 36
    • 84860840868 scopus 로고    scopus 로고
    • Integration of deep transcript and targeted metabolite profiles for eight cultivars of opium poppy
    • Desgagne-Penix, I., Farrow, S. C., Cram, D., Nowak, J. & Facchini, P. J. Integration of deep transcript and targeted metabolite profiles for eight cultivars of opium poppy. Plant Mol. Biol. 79, 295-313 (2012).
    • (2012) Plant Mol. Biol , vol.79 , pp. 295-313
    • Desgagne-Penix, I.1    Farrow, S.C.2    Cram, D.3    Nowak, J.4    Facchini, P.J.5
  • 37
    • 0034333196 scopus 로고    scopus 로고
    • Rapid automatic detection and alignment of repeats in protein sequences
    • Heger, A. & Holm, L. Rapid automatic detection and alignment of repeats in protein sequences. Prot. Struct. Funct. Genet. 41, 224-237 (2000).
    • (2000) Prot. Struct. Funct. Genet , vol.41 , pp. 224-237
    • Heger, A.1    Holm, L.2
  • 38
    • 34347260322 scopus 로고    scopus 로고
    • Frozen competent yeast cells that can be transformed with high efficiency using the LiAc/SS carrier DNA/PEG method
    • Gietz, R. D. & Schiestl, R. H. Frozen competent yeast cells that can be transformed with high efficiency using the LiAc/SS carrier DNA/PEG method. Nat. Protocols 2, 1-4 (2007).
    • (2007) Nat. Protocols , vol.2 , pp. 1-4
    • Gietz, R.D.1    Schiestl, R.H.2
  • 39
    • 0042121237 scopus 로고    scopus 로고
    • Multiple sequence alignment with the Clustal series of programs
    • Chenna, R. et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res. 31, 3497-3500 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 3497-3500
    • Chenna, R.1
  • 40
    • 84896122676 scopus 로고    scopus 로고
    • EasyClone: Method for iterative chromosomal integration of multiple genes in Saccharomyces cerevisiae
    • Jensen, N. B. et al. EasyClone: method for iterative chromosomal integration of multiple genes in Saccharomyces cerevisiae. FEMS Yeast Res. 14, 238-248 (2014).
    • (2014) FEMS Yeast Res , vol.14 , pp. 238-248
    • Jensen, N.B.1
  • 41
    • 84964258842 scopus 로고    scopus 로고
    • Plug-And-play benzylisoquinoline alkaloid biosynthetic gene discovery in engineered yeast
    • Morris, J. S. et al. Plug-And-play benzylisoquinoline alkaloid biosynthetic gene discovery in engineered yeast. Methods Enzymol. 575, 143-178 (2016).
    • (2016) Methods Enzymol , vol.575 , pp. 143-178
    • Morris, J.S.1
  • 42
    • 72449148338 scopus 로고    scopus 로고
    • Targeted metabolite and transcript profiling for elucidating enzyme function: Isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species
    • Liscombe, D. K., Ziegler, J., Schmidt, J., Ammer, C. & Facchini, P. J. Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species. Plant J. 60, 729-743 (2009).
    • (2009) Plant J , vol.60 , pp. 729-743
    • Liscombe, D.K.1    Ziegler, J.2    Schmidt, J.3    Ammer, C.4    Facchini, P.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.