메뉴 건너뛰기




Volumn 1 JUL, Issue , 2010, Pages

Biochemistry and occurrence of O-demethylation in plant metabolism

Author keywords

2 oxoglutarate Fe(II) dependent dioxygenase; Benzylisoquinoline alkaloid biosynthesis; N demethylation; O demethylation

Indexed keywords


EID: 78649505567     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2010.00014     Document Type: Article
Times cited : (49)

References (45)
  • 1
    • 14644431741 scopus 로고    scopus 로고
    • A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilus SYK-6
    • Abe, T., Masai, E., Miyauchi, K., Katayama, Y., and Fukuda, M. (2005). A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilus SYK-6. J. Bacteriol. 187, 2030-2037.
    • (2005) J. Bacteriol , vol.187 , pp. 2030-2037
    • Abe, T.1    Masai, E.2    Miyauchi, K.3    Katayama, Y.4    Fukuda, M.5
  • 2
    • 0034668117 scopus 로고    scopus 로고
    • Novel flavonol 2-oxoglutarate depend- ent dioxygenase: affinity purification, characterization, and kinetic properties
    • Anzellotti, D., and Ibrahim, R. K. (2000). Novel flavonol 2-oxoglutarate depend- ent dioxygenase: affinity purification, characterization, and kinetic properties. Arch. Biochem. Biophys. 382, 161-172.
    • (2000) Arch. Biochem. Biophys , vol.382 , pp. 161-172
    • Anzellotti, D.1    Ibrahim, R.K.2
  • 3
    • 0034960661 scopus 로고    scopus 로고
    • Metabolism of ipecac alkaloids cephaeline and emetine by human hepatic microsomal cytochrome P450s, and their inhibitory effects on P450 enzyme activities
    • Asano, T., Kushida, H., Sadakane, C., Ishihara, K., Wakui, Y., Yanagisawa, T., Kimura, M., Kamei, H., and Yoshida, T. (2001). Metabolism of ipecac alkaloids cephaeline and emetine by human hepatic microsomal cytochrome P450s, and their inhibitory effects on P450 enzyme activities. Biol. Pharm. Bull. 24, 678-682.
    • (2001) Biol. Pharm. Bull , vol.24 , pp. 678-682
    • Asano, T.1    Kushida, H.2    Sadakane, C.3    Ishihara, K.4    Wakui, Y.5    Yanagisawa, T.6    Kimura, M.7    Kamei, H.8    Yoshida, T.9
  • 4
    • 0026578923 scopus 로고
    • Importance of tetrahydrofolate and ATP in the anaerobic O-demethylation reaction for phenylmethylethers
    • Berman, M. H., and Frazer, A. C. (1992). Importance of tetrahydrofolate and ATP in the anaerobic O-demethylation reaction for phenylmethylethers. Appl. Environ. Microbiol. 58, 925-931.
    • (1992) Appl. Environ. Microbiol , vol.58 , pp. 925-931
    • Berman, M.H.1    Frazer, A.C.2
  • 6
    • 58149234237 scopus 로고    scopus 로고
    • Biodegradation of 2,4,6-TCA by the white-rot fungus Phelbia radiata is initiated by a phase I (O-demethylation)-phase II (O-conjugation) reactions system: implications for the chlorine cycle
    • Campoy, S., Àlvarez-Rodríguez, M. L., Recio, E., Rumbero, A., and Coque, J. J. R. (2009). Biodegradation of 2,4,6-TCA by the white-rot fungus Phelbia radiata is initiated by a phase I (O-demethylation)-phase II (O-conjugation) reactions system: implications for the chlorine cycle. Environ. Microbiol. 11, 99-110.
    • (2009) Environ. Microbiol , vol.11 , pp. 99-110
    • Campoy, S.1    Àlvarez-Rodríguez, M.L.2    Recio, E.3    Rumbero, A.4    Coque, J.J.R.5
  • 7
    • 0034045259 scopus 로고    scopus 로고
    • Bioconversion of ferulic acid into vanillic acid by means of a vanillate-negative mutant of Pseudomonas fluorescens strain BF13
    • Civolani, C., Barghini, P., Roncetti, A. R., Ruzzi, M., and Schiesser, A. (2000). Bioconversion of ferulic acid into vanillic acid by means of a vanillate-negative mutant of Pseudomonas fluorescens strain BF13. Appl. Environ. Microbiol. 66, 2311-2317.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 2311-2317
    • Civolani, C.1    Barghini, P.2    Roncetti, A.R.3    Ruzzi, M.4    Schiesser, A.5
  • 8
    • 33746056508 scopus 로고    scopus 로고
    • Kinetic isotope effects implicate a single oxidant for cytochrome P450-mediated O-dealkylation, N-oxygenation, and aromatic hydroxylation of 6-methoxyquinoline
    • Dowers, T. S., and Jones, J. P. (2006). Kinetic isotope effects implicate a single oxidant for cytochrome P450-mediated O-dealkylation, N-oxygenation, and aromatic hydroxylation of 6-methoxyquinoline. Drug Metab. Dispos. 34, 1288-1290.
    • (2006) Drug Metab. Dispos , vol.34 , pp. 1288-1290
    • Dowers, T.S.1    Jones, J.P.2
  • 9
    • 69049107348 scopus 로고    scopus 로고
    • Crystral structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation
    • Dumitru, R., Jiang, W. Z., Weeks, D. P., and Wilson, M. A. (2009). Crystral structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation. J. Mol. Biol. 392, 498-510.
    • (2009) J. Mol. Biol , vol.392 , pp. 498-510
    • Dumitru, R.1    Jiang, W.Z.2    Weeks, D.P.3    Wilson, M.A.4
  • 10
    • 70350715080 scopus 로고    scopus 로고
    • Benzoxazinoid biosynthesis, a model for evolution of secondary metabolic pathways in plants
    • Frey, M., Schullehner, K., Dick, R., Fiesselmann, A., and Gierl, A. (2009). Benzoxazinoid biosynthesis, a model for evolution of secondary metabolic pathways in plants. Phytochemistry 70, 1645-1651.
    • (2009) Phytochemistry , vol.70 , pp. 1645-1651
    • Frey, M.1    Schullehner, K.2    Dick, R.3    Fiesselmann, A.4    Gierl, A.5
  • 11
    • 69949174213 scopus 로고    scopus 로고
    • CYP719B1 is salutaridine synthase, the C-C phenol-coupling enzyme of morphine biosynthesis in opium poppy
    • Gesell, A., Rolf, M., Ziegler, J., Díaz Chávez, M. L., Huang, F. C., and Kutchan, T. M. (2009). CYP719B1 is salutaridine synthase, the C-C phenol-coupling enzyme of morphine biosynthesis in opium poppy. J. Biol. Chem. 284, 24432-24442.
    • (2009) J. Biol. Chem , vol.284 , pp. 24432-24442
    • Gesell, A.1    Rolf, M.2    Ziegler, J.3    Díaz Chávez, M.L.4    Huang, F.C.5    Kutchan, T.M.6
  • 13
    • 69949188699 scopus 로고    scopus 로고
    • Mammalian cytochrome P450 enzymes catalyze the phenol-coupling step in endogenous morphine biosynthesis
    • Grobe, N., Zhang, B., Fisinger, U., Kutchan, T. M., Zenk, M. H., and Guengerich, F. P. (2009). Mammalian cytochrome P450 enzymes catalyze the phenol-coupling step in endogenous morphine biosynthesis. J. Biol. Chem. 284, 24425-24431.
    • (2009) J. Biol. Chem , vol.284 , pp. 24425-24431
    • Grobe, N.1    Zhang, B.2    Fisinger, U.3    Kutchan, T.M.4    Zenk, M.H.5    Guengerich, F.P.6
  • 14
    • 33745934443 scopus 로고    scopus 로고
    • The genetics and biochemistry of floral pigments
    • Grotewold, E. (2006). The genetics and biochemistry of floral pigments. Annu. Rev. Plant Biol. 57, 761-780.
    • (2006) Annu. Rev. Plant Biol , vol.57 , pp. 761-780
    • Grotewold, E.1
  • 15
    • 77949847651 scopus 로고    scopus 로고
    • Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy
    • Hagel, J. M., and Facchini, P. J. (2010). Dioxygenases catalyze the O-demethylation steps of morphine biosynthesis in opium poppy. Nat. Chem. Biol. 6, 273-275.
    • (2010) Nat. Chem. Biol , vol.6 , pp. 273-275
    • Hagel, J.M.1    Facchini, P.J.2
  • 16
    • 53749090789 scopus 로고    scopus 로고
    • 1H nuclear magnetic resonance metabolite profiling as a functional genomics platform to investigate alkaloid biosynthesis in opium poppy
    • 1H nuclear magnetic resonance metabolite profiling as a functional genomics platform to investigate alkaloid biosynthesis in opium poppy. Plant Physiol. 147, 1805-1821.
    • (2008) Plant Physiol , vol.147 , pp. 1805-1821
    • Hagel, J.M.1    Weljie, A.M.2    Vogel, H.J.3    Facchini, P.J.4
  • 17
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger, R. P. (2004). Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. 39, 21-68.
    • (2004) Crit. Rev. Biochem. Mol. Biol , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 18
    • 84901860154 scopus 로고    scopus 로고
    • We two alone will sing: the two-substrate α-keto acid-dependent oxygenases
    • He, P., and Moran, G. R. (2009). We two alone will sing: the two-substrate α-keto acid-dependent oxygenases. Curr. Opin. Chem. Biol. 13, 443-450.
    • (2009) Curr. Opin. Chem. Biol , vol.13 , pp. 443-450
    • He, P.1    Moran, G.R.2
  • 19
    • 42249110738 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CYP80G2, a cytochrome P450 that catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells
    • Ikezawa, N., Iwasa, K., and Sato, F. (2008). Molecular cloning and characterization of CYP80G2, a cytochrome P450 that catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells. J. Biol. Chem. 283, 8810-8821.
    • (2008) J. Biol. Chem , vol.283 , pp. 8810-8821
    • Ikezawa, N.1    Iwasa, K.2    Sato, F.3
  • 20
    • 51449121245 scopus 로고    scopus 로고
    • Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl-CoA by a 2-oxoglutarte-dependent dioxygenase in Arabidopsis thaliana
    • Kai, K., Mizutani, M., Kawamura, N., Yamamoto, R., Tamai, M., Yamaguchi, H., Sakata, K., and Shimizu, B. (2008). Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl-CoA by a 2-oxoglutarte-dependent dioxygenase in Arabidopsis thaliana. Plant J. 55, 989-999.
    • (2008) Plant J , vol.55 , pp. 989-999
    • Kai, K.1    Mizutani, M.2    Kawamura, N.3    Yamamoto, R.4    Tamai, M.5    Yamaguchi, H.6    Sakata, K.7    Shimizu, B.8
  • 23
    • 39449130475 scopus 로고    scopus 로고
    • Versatility of biological nonheme Fe(II) centers in oxygen activation reactions
    • Kovaleva, E. G., and Lipscombe, J. D. (2008). Versatility of biological nonheme Fe(II) centers in oxygen activation reactions. Nat. Chem. Biol. 4, 186-193.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 186-193
    • Kovaleva, E.G.1    Lipscombe, J.D.2
  • 24
    • 0028785275 scopus 로고
    • Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants
    • Kutchan, T. M., and Dittrich, H. (1995). Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants. J. Bioahem. 270, 24475-24481.
    • (1995) J. Bioahem , vol.270 , pp. 24475-24481
    • Kutchan, T.M.1    Dittrich, H.2
  • 25
    • 38849204943 scopus 로고    scopus 로고
    • Structure, function and evolution of plant O-methyltransferases
    • Lam, K. C., Ibrahim, R., Behdad, B., and Dayanandan, S. (2007). Structure, function and evolution of plant O-methyltransferases. Genome 50, 1001-1013.
    • (2007) Genome , vol.50 , pp. 1001-1013
    • Lam, K.C.1    Ibrahim, R.2    Behdad, B.3    Dayanandan, S.4
  • 26
    • 0035887386 scopus 로고    scopus 로고
    • Human cyto- chrome P450 2A6 is the major enzyme involved in the metabolism of three alkoxyethers used as oxyfuels
    • Le Gal, A., Dréano, Y., Gervasi, P. G., and Berthou, F. (2001). Human cyto- chrome P450 2A6 is the major enzyme involved in the metabolism of three alkoxyethers used as oxyfuels. Toxicol. Lett. 124, 47-58.
    • (2001) Toxicol. Lett , vol.124 , pp. 47-58
    • Le Gal, A.1    Dréano, Y.2    Gervasi, P.G.3    Berthou, F.4
  • 27
    • 34250332680 scopus 로고    scopus 로고
    • Functional analysis of norcoclaurine synthase in Coptis japonica
    • Minami, H., Dubouzet, E., Iwasa, K., and Sato, F. (2007). Functional analysis of norcoclaurine synthase in Coptis japonica. J. Biol. Chem. 282, 6274-6282.
    • (2007) J. Biol. Chem , vol.282 , pp. 6274-6282
    • Minami, H.1    Dubouzet, E.2    Iwasa, K.3    Sato, F.4
  • 28
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast, N., and Shi, Y. (2010). Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu. Rev. Biochem. 78, 155-179.
    • (2010) Annu. Rev. Biochem , vol.78 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 29
    • 0031846628 scopus 로고    scopus 로고
    • Cytochrome P450 2D6 catalyzes the O-demethylation of the psychoactive alkaloid ibogaine to 12-hydroxyibogamine
    • Obach, R. S., Pablo, J., and Mash, D. C. (1998). Cytochrome P450 2D6 catalyzes the O-demethylation of the psychoactive alkaloid ibogaine to 12-hydroxyibogamine. Drug Metab. Dispos. 26, 764-768.
    • (1998) Drug Metab. Dispos , vol.26 , pp. 764-768
    • Obach, R.S.1    Pablo, J.2    Mash, D.C.3
  • 30
    • 28844436465 scopus 로고    scopus 로고
    • Boldine and its antioxidant or health-promoting properties
    • O'Brien, P., Carrasco-Pozo, C., and Speisky, H. (2006). Boldine and its antioxidant or health-promoting properties. Chem. Biol. Interact. 159, 1-17.
    • (2006) Chem. Biol. Interact , vol.159 , pp. 1-17
    • O'Brien, P.1    Carrasco-Pozo, C.2    Speisky, H.3
  • 31
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: an application to display phylogenetic trees on personal computers
    • Page, R. D. (1996). TREEVIEW: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12, 357-358.
    • (1996) Comput. Appl. Biosci , vol.12 , pp. 357-358
    • Page, R.D.1
  • 32
    • 33744731484 scopus 로고    scopus 로고
    • Metabolism of isovanillate, vanillate, and veratrate by Comamonas testosteroni strain BR6020
    • Providenti, M. A., O'Brien, J. M., Ruff, J., Cook, A. M., and Lambert, I. B. (2006). Metabolism of isovanillate, vanillate, and veratrate by Comamonas testosteroni strain BR6020. J. Bacteriol. 188, 3862-3869.
    • (2006) J. Bacteriol , vol.188 , pp. 3862-3869
    • Providenti, M.A.1    O'Brien, J.M.2    Ruff, J.3    Cook, A.M.4    Lambert, I.B.5
  • 33
    • 34249869010 scopus 로고    scopus 로고
    • The diverse and pervasive chemistries of the α-keto acid dependent enzymes
    • Purpero, V., and Moran, G. R. (2007). The diverse and pervasive chemistries of the α-keto acid dependent enzymes. J. Biol. Inorg. Chem. 12, 587-601.
    • (2007) J. Biol. Inorg. Chem , vol.12 , pp. 587-601
    • Purpero, V.1    Moran, G.R.2
  • 34
    • 33845899754 scopus 로고
    • Biosynthesis of the protoberberine alkaloid jatrorrhizine
    • Rueffer, M., Ekundayo, O., Nagakura, N., and Zenk, M. H. (1983). Biosynthesis of the protoberberine alkaloid jatrorrhizine. Tetrahedron Lett. 24, 2643-2644.
    • (1983) Tetrahedron Lett , vol.24 , pp. 2643-2644
    • Rueffer, M.1    Ekundayo, O.2    Nagakura, N.3    Zenk, M.H.4
  • 35
    • 5744232885 scopus 로고    scopus 로고
    • The Simple Plant Isoquinolines
    • Berkeley, CA: Transform Press
    • Shulgin, A. T., and Perry, W. E. (2002). The Simple Plant Isoquinolines. Berkeley, CA: Transform Press.
    • (2002)
    • Shulgin, A.T.1    Perry, W.E.2
  • 37
    • 26844498333 scopus 로고    scopus 로고
    • Conversion of nicotine to nornicotine in Nicotiana tabacum is mediated by CYP82E4, a cytochrome P450 monooxygenase
    • Siminszky, B., Gavilano, L., Bowen, S. W., and Dewey, R. E. (2005). Conversion of nicotine to nornicotine in Nicotiana tabacum is mediated by CYP82E4, a cytochrome P450 monooxygenase. Proc. Natl. Acad. Sci. U.S.A. 102, 14919-14924.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 14919-14924
    • Siminszky, B.1    Gavilano, L.2    Bowen, S.W.3    Dewey, R.E.4
  • 38
    • 77953366823 scopus 로고    scopus 로고
    • Biosynthesis of glucosinolates - gene discovery and beyond
    • Sønderby, I. E., Geu-Flores, F., and Halkier, B. A. (2010). Biosynthesis of glucosinolates - gene discovery and beyond. Trends Plant Sci. 15, 283-290.
    • (2010) Trends Plant Sci , vol.15 , pp. 283-290
    • Sønderby, I.E.1    Geu-Flores, F.2    Halkier, B.A.3
  • 39
    • 70350044889 scopus 로고    scopus 로고
    • New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme
    • Wang, B., Yang, L. P., Zhang, X. Z., Huang, S. Q., Bartlam, M., and Zhou, S. F. (2009). New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme. Drug Metab. Rev. 41, 573-643.
    • (2009) Drug Metab. Rev , vol.41 , pp. 573-643
    • Wang, B.1    Yang, L.P.2    Zhang, X.Z.3    Huang, S.Q.4    Bartlam, M.5    Zhou, S.F.6
  • 42
    • 44949108257 scopus 로고    scopus 로고
    • Gibberellin metabolism and its regulation
    • Yamaguchi, S. (2008). Gibberellin metabolism and its regulation. Annu. Rev. Plant Biol. 59, 225-251.
    • (2008) Annu. Rev. Plant Biol , vol.59 , pp. 225-251
    • Yamaguchi, S.1
  • 43
    • 74049151209 scopus 로고    scopus 로고
    • A non-heme iron-mediated chemical demethylation in DNA and RNA
    • Yi, C., Yang, C. G., and He, C. (2009). A non-heme iron-mediated chemical demethylation in DNA and RNA. Acc. Chem. Res. 42, 519-529.
    • (2009) Acc. Chem. Res , vol.42 , pp. 519-529
    • Yi, C.1    Yang, C.G.2    He, C.3
  • 44
    • 5544323881 scopus 로고    scopus 로고
    • Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase - the ethylene forming enzyme
    • Zhang, Z., Ren, J. S., Clifton, I. J., and Schofield, C. J. (2004). Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase - the ethylene forming enzyme. Chem. Biol. 11, 1383-1394.
    • (2004) Chem. Biol , vol.11 , pp. 1383-1394
    • Zhang, Z.1    Ren, J.S.2    Clifton, I.J.3    Schofield, C.J.4
  • 45
    • 44949127129 scopus 로고    scopus 로고
    • Alkaloid biosynthesis: metabolism and trafficking
    • Ziegler, J., and Facchini, P. J. (2008). Alkaloid biosynthesis: metabolism and trafficking. Annu. Rev. Plant Biol. 59, 735-769.
    • (2008) Annu. Rev. Plant Biol , vol.59 , pp. 735-769
    • Ziegler, J.1    Facchini, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.