메뉴 건너뛰기




Volumn , Issue , 2012, Pages 1-30

Berberine bridge enzyme and the family of bicovalent flavoenzymes

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85144677269     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (6)

References (122)
  • 1
    • 79960570256 scopus 로고    scopus 로고
    • Flavogenomics - a genomic and structural view of flavindependent proteins
    • Macheroux P, Kappes B, Ealick SE. Flavogenomics - a genomic and structural view of flavindependent proteins. FEBS J 2011;278:2625-34.
    • (2011) FEBS J , vol.278 , pp. 2625-2634
    • Macheroux, P.1    Kappes, B.2    Ealick, S.E.3
  • 3
    • 0015525666 scopus 로고
    • Studies on succinate dehydrogenase. Site of attachment of the covalently-bound flavin to the peptide chain
    • Salach J, Walker WH, Singer TP, et al. Studies on succinate dehydrogenase. Site of attachment of the covalently-bound flavin to the peptide chain. Eur J Biochem 1972;26:267-78.
    • (1972) Eur J Biochem , vol.26 , pp. 267-278
    • Salach, J.1    Walker, W.H.2    Singer, T.P.3
  • 4
    • 0015186769 scopus 로고
    • The covalently-bound flavin of hepatic monoamine oxidase. 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8alpha position
    • Kearney EB, Salach JI, Walker WH, et al. The covalently-bound flavin of hepatic monoamine oxidase. 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8alpha position. Eur J Biochem 1971;24:321-7.
    • (1971) Eur J Biochem , vol.24 , pp. 321-327
    • Kearney, E.B.1    Salach, J.I.2    Walker, W.H.3
  • 5
    • 0019889043 scopus 로고
    • 8a-(O-tyrosyl)flavin adenine dinucleotide, the prosthetic group of bacterial p-cresol methylhydroxylase
    • McIntire W, Edmondson DE, Hopper DJ, Singer TP. 8a-(O-tyrosyl)flavin adenine dinucleotide, the prosthetic group of bacterial p-cresol methylhydroxylase. Biochemistry 1981; 20:3068-75.
    • (1981) Biochemistry , vol.20 , pp. 3068-3075
    • McIntire, W.1    Edmondson, D.E.2    Hopper, D.J.3    Singer, T.P.4
  • 6
    • 0031941120 scopus 로고    scopus 로고
    • Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs
    • Mewies M, McIntire WS, Scrutton NS. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs. Protein Science 1998;7:7-20.
    • (1998) Protein Science , vol.7 , pp. 7-20
    • Mewies, M.1    McIntire, W.S.2    Scrutton, N.S.3
  • 7
    • 33644689024 scopus 로고    scopus 로고
    • Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: A novel flavinylation of 6-S-cysteinyl, 8a-N1-histidyl FAD
    • Huang CH, Lai WL, Lee MH, et al. Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: A novel flavinylation of 6-S-cysteinyl, 8a-N1-histidyl FAD. J Biol Chem 2005;280:38831-8.
    • (2005) J Biol Chem , vol.280 , pp. 38831-38838
    • Huang, C.H.1    Lai, W.L.2    Lee, M.H.3
  • 8
    • 67650480250 scopus 로고    scopus 로고
    • What's in a covalent bond?: On the role and formation of covalently bound flavin cofactors
    • Heuts DPHM, Scrutton NS, McIntire WS, Fraaije MW. What's in a covalent bond?: On the role and formation of covalently bound flavin cofactors. FEBS J 2009;276:3405-27.
    • (2009) FEBS J , vol.276 , pp. 3405-3427
    • Heuts, D.P.H.M.1    Scrutton, N.S.2    McIntire, W.S.3    Fraaije, M.W.4
  • 9
    • 34548249681 scopus 로고    scopus 로고
    • 6-S-cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity
    • Winkler A, Kutchan TM, Macheroux P. 6-S-cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity. J Biol Chem 2007;282:24437-43.
    • (2007) J Biol Chem , vol.282 , pp. 24437-24443
    • Winkler, A.1    Kutchan, T.M.2    Macheroux, P.3
  • 10
    • 46249099669 scopus 로고    scopus 로고
    • The role of double covalent flavin binding in chito-oligosaccharide oxidase from Fusarium graminearum
    • Heuts DPHM, Winter RT, Damsma GE, Janssen DB, Fraaije MW. The role of double covalent flavin binding in chito-oligosaccharide oxidase from Fusarium graminearum. Biochem J 2008;413:175-83.
    • (2008) Biochem J , vol.413 , pp. 175-183
    • Heuts, D.P.H.M.1    Winter, R.T.2    Damsma, G.E.3    Janssen, D.B.4    Fraaije, M.W.5
  • 11
    • 57649155210 scopus 로고    scopus 로고
    • Functional roles of the 6-S-cysteinyl, 8a-N1-histidyl FAD in glucooligosaccharide oxidase from Acremonium strictum
    • Huang CH, Winkler A, Chen CL, et al. Functional roles of the 6-S-cysteinyl, 8a-N1-histidyl FAD in glucooligosaccharide oxidase from Acremonium strictum. J Biol Chem 2008;283:30990-6.
    • (2008) J Biol Chem , vol.283 , pp. 30990-30996
    • Huang, C.H.1    Winkler, A.2    Chen, C.L.3
  • 12
    • 67749096156 scopus 로고    scopus 로고
    • Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzyme
    • Winkler A, Motz K, Riedl S, Puhl M, Macheroux P, Gruber K. Structural and mechanistic studies reveal the functional role of bicovalent flavinylation in berberine bridge enzyme. J Biol Chem 2009;284:19993-20001.
    • (2009) J Biol Chem , vol.284 , pp. 19993-20001
    • Winkler, A.1    Motz, K.2    Riedl, S.3    Puhl, M.4    Macheroux, P.5    Gruber, K.6
  • 13
    • 77956684330 scopus 로고    scopus 로고
    • Molecular genetics of plant alkaloid biosynthesis
    • In: Cordell GA, ed. San Diego, CA, USA: Academic Press
    • Kutchan TM. Molecular genetics of plant alkaloid biosynthesis. In: Cordell GA, ed. The Alkaloids: Chemistry and Biology. San Diego, CA, USA: Academic Press, 1998;50:257-316.
    • (1998) The Alkaloids: Chemistry and Biology , vol.50 , pp. 257-316
    • Kutchan, T.M.1
  • 14
    • 56249097931 scopus 로고    scopus 로고
    • A concerted mechanism for berberine bridge enzyme
    • Winkler A, Łyskowski A, Riedl S, et al. A concerted mechanism for berberine bridge enzyme. Nat Chem Biol 2008;4:739-41.
    • (2008) Nat Chem Biol , vol.4 , pp. 739-741
    • Winkler, A.1    Łyskowski, A.2    Riedl, S.3
  • 15
    • 42249097714 scopus 로고    scopus 로고
    • Evolutionary and cellular webs in benzylisoquinoline alkaloid biosynthesis
    • Liscombe DK, Facchini PJ. Evolutionary and cellular webs in benzylisoquinoline alkaloid biosynthesis. Curr Opin Biotechnol 2008;19:173-80.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 173-180
    • Liscombe, D.K.1    Facchini, P.J.2
  • 16
    • 0016441957 scopus 로고
    • Conversion of reticuline into scoulerine by a cell free preparation from Macleaya microcarpa cell suspension cultures
    • Rink E, Bohm H. Conversion of reticuline into scoulerine by a cell free preparation from Macleaya microcarpa cell suspension cultures. FEBS Lett 1975;49:396-9.
    • (1975) FEBS Lett , vol.49 , pp. 396-399
    • Rink, E.1    Bohm, H.2
  • 17
    • 0000760039 scopus 로고
    • Purification and characterization of the berberine bridge enzyme from Berberis beaniana cell cultures
    • Steffens P, Nagakura N, Zenk MH. Purification and characterization of the berberine bridge enzyme from Berberis beaniana cell cultures. Phytochem 1985;24:2577-83.
    • (1985) Phytochem , vol.24 , pp. 2577-2583
    • Steffens, P.1    Nagakura, N.2    Zenk, M.H.3
  • 18
    • 0028785275 scopus 로고
    • Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants
    • Kutchan TM, Dirtrich H. Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants. J Biol Chem 1995;270:24475-81.
    • (1995) J Biol Chem , vol.270 , pp. 24475-24481
    • Kutchan, T.M.1    Dirtrich, H.2
  • 20
    • 33746325823 scopus 로고    scopus 로고
    • Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor
    • Winkler A, Hartner F, Kutchan TM, Glieder A, Macheroux P. Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor. J Biol Chem 2006;281:21276-85.
    • (2006) J Biol Chem , vol.281 , pp. 21276-21285
    • Winkler, A.1    Hartner, F.2    Kutchan, T.M.3    Glieder, A.4    Macheroux, P.5
  • 21
    • 0018787423 scopus 로고
    • 8-Mercaptoflavins as active site probes of flavoenzymes
    • Massey V, Ghisla S, Moore EG. 8-Mercaptoflavins as active site probes of flavoenzymes. J Biol Chem 1979;254:9640-50.
    • (1979) J Biol Chem , vol.254 , pp. 9640-9650
    • Massey, V.1    Ghisla, S.2    Moore, E.G.3
  • 22
    • 0021112454 scopus 로고
    • The reaction of 8-mercaptoflavins and flavoproteins with sulfite. Evidence for the role of an active site arginine in D-amino acid oxidase
    • Fitzpatrick PF, Massey V. The reaction of 8-mercaptoflavins and flavoproteins with sulfite. Evidence for the role of an active site arginine in D-amino acid oxidase. J Biol Chem 1983;258:9700-5.
    • (1983) J Biol Chem , vol.258 , pp. 9700-9705
    • Fitzpatrick, P.F.1    Massey, V.2
  • 23
    • 0014670386 scopus 로고
    • The reactivity of flavoproteins with sulfite. Possible relevance to the problem of oxygen reactivity
    • Massey V, Muller F, Feldberg R, et al. The reactivity of flavoproteins with sulfite. Possible relevance to the problem of oxygen reactivity. J Biol Chem 1969;244:3999-4006.
    • (1969) J Biol Chem , vol.244 , pp. 3999-4006
    • Massey, V.1    Muller, F.2    Feldberg, R.3
  • 24
    • 0019023686 scopus 로고
    • Active-site probes of flavoproteins
    • Massey V, Hemmerich P. Active-site probes of flavoproteins. Biochem Soc Trans 1980; 8:246-57.
    • (1980) Biochem Soc Trans , vol.8 , pp. 246-257
    • Massey, V.1    Hemmerich, P.2
  • 25
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije MW, Mattevi A. Flavoenzymes: diverse catalysts with recurrent features. Trends Bio-chem Sci 2000;25:126-32.
    • (2000) Trends Bio-chem Sci , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 27
    • 0034254540 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants
    • Wagner MA, Trickey P, Che ZW, Mathews FS, Jorns MS. Monomeric sarcosine oxidase: 1. Flavin reactivity and active site binding determinants. Biochemistry 2000;39:8813-24.
    • (2000) Biochemistry , vol.39 , pp. 8813-8824
    • Wagner, M.A.1    Trickey, P.2    Che, Z.W.3    Mathews, F.S.4    Jorns, M.S.5
  • 28
    • 0019039047 scopus 로고
    • Identification and properties of the prosthetic group of choline oxidase from Alcaligenes sp
    • Ohta-Fukuyama M, Miyake Y, Emi S, Yamano T. Identification and properties of the prosthetic group of choline oxidase from Alcaligenes sp. J Biochem 1980;88:197-203.
    • (1980) J Biochem , vol.88 , pp. 197-203
    • Ohta-Fukuyama, M.1    Miyake, Y.2    Emi, S.3    Yamano, T.4
  • 29
    • 0018801242 scopus 로고
    • Purification and properties of the bacterial flavoprotein: Thiamin dehydrogenase
    • Gomez-Moreno C, Choy M, Edmondson DE. Purification and properties of the bacterial flavoprotein: thiamin dehydrogenase. J Biol Chem 1979;254:7630-5.
    • (1979) J Biol Chem , vol.254 , pp. 7630-7635
    • Gomez-Moreno, C.1    Choy, M.2    Edmondson, D.E.3
  • 30
    • 0015391962 scopus 로고
    • Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans
    • Bruhmuller M, Mohler H, Decker K. Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Z Naturforsch 1972;27:1073-4.
    • (1972) Z Naturforsch , vol.27 , pp. 1073-1074
    • Bruhmuller, M.1    Mohler, H.2    Decker, K.3
  • 31
    • 0031465118 scopus 로고    scopus 로고
    • Characterization of cholesterol oxidase from Streptomy-ces hygroscopicus and Brevibacterium sterolicum
    • Gadda G, Wels G, Pollegioni L, et al. Characterization of cholesterol oxidase from Streptomy-ces hygroscopicus and Brevibacterium sterolicum. Eur J Biochem 1997;250:369-76.
    • (1997) Eur J Biochem , vol.250 , pp. 369-376
    • Gadda, G.1    Wels, G.2    Pollegioni, L.3
  • 32
    • 0014670427 scopus 로고
    • Flavin-sulfite complexes and their structures
    • Muller F, Massey V. Flavin-sulfite complexes and their structures. J Biol Chem 1969; 244:4007-16.
    • (1969) J Biol Chem , vol.244 , pp. 4007-4016
    • Muller, F.1    Massey, V.2
  • 33
    • 0032574753 scopus 로고    scopus 로고
    • Biochemical and physical characterization of the active FADcontaining form of nitroalkane oxidase from Fusarium oxysporum
    • Gadda G, Fitzpatrick PF. Biochemical and physical characterization of the active FADcontaining form of nitroalkane oxidase from Fusarium oxysporum. Biochemistry 1998; 37:6154-64.
    • (1998) Biochemistry , vol.37 , pp. 6154-6164
    • Gadda, G.1    Fitzpatrick, P.F.2
  • 34
    • 0023040910 scopus 로고
    • Preparation and some properties of 6-substituted flavins as active site probes for flavin enzymes
    • Ghisla S, Massey V, Yagi K. Preparation and some properties of 6-substituted flavins as active site probes for flavin enzymes. Biochemistry 1986;25:3282-9.
    • (1986) Biochemistry , vol.25 , pp. 3282-3289
    • Ghisla, S.1    Massey, V.2    Yagi, K.3
  • 35
    • 33644868234 scopus 로고    scopus 로고
    • Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase
    • Ghanem M, Gadda G. Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase. Biochemistry 2006;45:3437-47.
    • (2006) Biochemistry , vol.45 , pp. 3437-3447
    • Ghanem, M.1    Gadda, G.2
  • 36
    • 0027397187 scopus 로고
    • Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution
    • Hecht HJ, Kalisz HM, Hendle J, Schmid RD, Schomburg D. Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution. J Mol Biol 1993;229:153-72.
    • (1993) J Mol Biol , vol.229 , pp. 153-172
    • Hecht, H.J.1    Kalisz, H.M.2    Hendle, J.3    Schmid, R.D.4    Schomburg, D.5
  • 37
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
    • Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ. 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallogr D Biol Crystallogr 1999;55:969-77.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.J.6
  • 38
    • 0024977935 scopus 로고
    • The active site of spinach glycolate oxidase
    • Lindqvist Y, Branden CI. The active site of spinach glycolate oxidase. J Biol Chem 1989;264:3624-8.
    • (1989) J Biol Chem , vol.264 , pp. 3624-3628
    • Lindqvist, Y.1    Branden, C.I.2
  • 39
    • 0001390566 scopus 로고    scopus 로고
    • Monomeric sarcosine oxidase: Structure of a covalently flavinylated amine oxidizing enzyme
    • Trickey P, Wagner MA, Jorns MS, Mathews FS. Monomeric sarcosine oxidase: Structure of a covalently flavinylated amine oxidizing enzyme. Structure 1999;7:331-45.
    • (1999) Structure , vol.7 , pp. 331-345
    • Trickey, P.1    Wagner, M.A.2    Jorns, M.S.3    Mathews, F.S.4
  • 40
    • 0028244641 scopus 로고
    • Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266
    • Muh U, Massey V, Williams Jr. CH. Lactate monooxygenase. I. Expression of the mycobacterial gene in Escherichia coli and site-directed mutagenesis of lysine 266. J Biol Chem 1994;269:7982-8.
    • (1994) J Biol Chem , vol.269 , pp. 7982-7988
    • Muh, U.1    Massey, V.2    Williams, C.H.3
  • 41
    • 0025278264 scopus 로고
    • Molecular structure of flavocytochrome b2 at 2.4 A resolution
    • Xia ZX, Mathews FS. Molecular structure of flavocytochrome b2 at 2.4 A resolution. J Mol Biol 1990;212:837-63.
    • (1990) J Mol Biol , vol.212 , pp. 837-863
    • Xia, Z.X.1    Mathews, F.S.2
  • 42
    • 2442691690 scopus 로고    scopus 로고
    • Insight into covalent flavinylation and catalysis from redox, spectral, and kinetic analyses of the R474K mutant of the flavoprotein subunit of p-cresol methylhydroxylase
    • Efimov I, Cronin CN, Bergmann DJ, Kuusk V, McIntire WS. Insight into covalent flavinylation and catalysis from redox, spectral, and kinetic analyses of the R474K mutant of the flavoprotein subunit of p-cresol methylhydroxylase. Biochemistry 2004;43:6138-48.
    • (2004) Biochemistry , vol.43 , pp. 6138-6148
    • Efimov, I.1    Cronin, C.N.2    Bergmann, D.J.3    Kuusk, V.4    McIntire, W.S.5
  • 43
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution
    • Vrielink A, Lloyd LF, Blow DM. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution. J Mol Biol 1991;219:533-54.
    • (1991) J Mol Biol , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 44
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg BM, Henriksson G, Pettersson G, Divne C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J Mol Biol 2002; 315:421-34.
    • (2002) J Mol Biol , vol.315 , pp. 421-434
    • Hallberg, B.M.1    Henriksson, G.2    Pettersson, G.3    Divne, C.4
  • 45
    • 0029839452 scopus 로고    scopus 로고
    • Crystal structure of D-amino acid oxidase: A case of active site mirror-image convergent evolution with flavocytochrome b2
    • Mattevi A, Vanoni MA, Todone F, et al. Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2. Proc Natl Acad Sci U S A 1996;93:7496-501.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7496-7501
    • Mattevi, A.1    Vanoni, M.A.2    Todone, F.3
  • 46
    • 0025741770 scopus 로고
    • Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization
    • Macheroux P, Massey V, Thiele DJ, Volokita M. Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: purification and characterization. Biochemistry 1991;30: 4612-9.
    • (1991) Biochemistry , vol.30 , pp. 4612-4619
    • Macheroux, P.1    Massey, V.2    Thiele, D.J.3    Volokita, M.4
  • 47
    • 79251548859 scopus 로고    scopus 로고
    • Biocatalytic enantioselective oxidative C-C coupling by aerobic C-H activation
    • Schrittwieser JH, Resch V, Sattler JH, et al. Biocatalytic enantioselective oxidative C-C coupling by aerobic C-H activation. Angew Chem Int Ed 2011;50:1068-71.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 1068-1071
    • Schrittwieser, J.H.1    Resch, V.2    Sattler, J.H.3
  • 48
    • 80051714884 scopus 로고    scopus 로고
    • Biocatalytic organic synthesis of optically pure (S)-scoulerine and berbine and benzylisoquinoline alkaloids
    • Schrittwieser JH, Resch V, Wallner S, et al. Biocatalytic organic synthesis of optically pure (S)-scoulerine and berbine and benzylisoquinoline alkaloids. J Org Chem 2011;76: 6703-14.
    • (2011) J Org Chem , vol.76 , pp. 6703-6714
    • Schrittwieser, J.H.1    Resch, V.2    Wallner, S.3
  • 50
    • 0142088938 scopus 로고    scopus 로고
    • Alkaloids from Croton fliavens L. and their affinities to GABA-receptors
    • Eisenreich WJ, Hofner G, Bracher F. Alkaloids from Croton fliavens L. and their affinities to GABA-receptors. Nat Prod Res 2003;17:437-40.
    • (2003) Nat Prod Res , vol.17 , pp. 437-440
    • Eisenreich, W.J.1    Hofner, G.2    Bracher, F.3
  • 51
    • 55749104226 scopus 로고    scopus 로고
    • Preparation and structural elucidation of (-)-tetrahydroberberine-(+)-2,3-di(p-toluyl) tartaric acid complex
    • Gao JM, Liu WT, Li ML, Liu HW, Zhang XC, Li ZX. Preparation and structural elucidation of (-)-tetrahydroberberine-(+)-2,3-di(p-toluyl) tartaric acid complex. J Mol Struct 2008;892:466-9.
    • (2008) J Mol Struct , vol.892 , pp. 466-469
    • Gao, J.M.1    Liu, W.T.2    Li, M.L.3    Liu, H.W.4    Zhang, X.C.5    Li, Z.X.6
  • 53
    • 0028148844 scopus 로고
    • Mechanism of the cardiovascular activity of laudanosine: Comparison with papaverine and other benzylisoquinolines
    • Chulia S, Ivorra MD, Lugnier C, Vila E, Noguera MA, D'Ocon P. Mechanism of the cardiovascular activity of laudanosine: comparison with papaverine and other benzylisoquinolines. Br J Pharmacol 1994;113:1377-85.
    • (1994) Br J Pharmacol , vol.113 , pp. 1377-1385
    • Chulia, S.1    Ivorra, M.D.2    Lugnier, C.3    Vila, E.4    Noguera, M.A.5    D'Ocon, P.6
  • 54
    • 20844441926 scopus 로고    scopus 로고
    • Anti-HIV benzylisoquinoline alkaloids and flavonoids from the leaves of Nelumbo nucifera, and structure-activity correlations with related alkaloids
    • Kashiwada Y, Aoshima A, Ikeshiro Y, et al. Anti-HIV benzylisoquinoline alkaloids and flavonoids from the leaves of Nelumbo nucifera, and structure-activity correlations with related alkaloids. Bioorg Med Chem 2005;13:443-8.
    • (2005) Bioorg Med Chem , vol.13 , pp. 443-448
    • Kashiwada, Y.1    Aoshima, A.2    Ikeshiro, Y.3
  • 56
    • 33746361816 scopus 로고    scopus 로고
    • L-Chloroscoulerine mesylate
    • Li J, Jin G, Shen J, Ji R. l-Chloroscoulerine mesylate. Drugs Future 2006;31:379-84.
    • (2006) Drugs Future , vol.31 , pp. 379-384
    • Li, J.1    Jin, G.2    Shen, J.3    Ji, R.4
  • 57
    • 13344267827 scopus 로고
    • Investigations on the biosynthesis of morphine Alkaloids
    • Barton DH, Kirby GW, Steglich W, et al. Investigations on the biosynthesis of morphine Alkaloids. J Chem Soc 1965;65:2423-38.
    • (1965) J Chem Soc , vol.65 , pp. 2423-2438
    • Barton, D.H.1    Kirby, G.W.2    Steglich, W.3
  • 58
    • 3543059896 scopus 로고    scopus 로고
    • Asymmetric synthesis of isoquinoline alkaloids
    • Chrzanowska M, Rozwadowska MD. Asymmetric synthesis of isoquinoline alkaloids. Chem Rev 2004;104:3341-70.
    • (2004) Chem Rev , vol.104 , pp. 3341-3370
    • Chrzanowska, M.1    Rozwadowska, M.D.2
  • 59
    • 0030047733 scopus 로고    scopus 로고
    • Total synthesis of (-)-tetrahydropalmatine via chiral formamidine carbanions: Unexpected behavior with certain ortho-substituted electrophiles
    • Matulenko MA, Meyers AI. Total synthesis of (-)-tetrahydropalmatine via chiral formamidine carbanions: unexpected behavior with certain ortho-substituted electrophiles. J Org Chem 1996;61:573-80.
    • (1996) J Org Chem , vol.61 , pp. 573-580
    • Matulenko, M.A.1    Meyers, A.I.2
  • 60
    • 80052788484 scopus 로고    scopus 로고
    • Biocatalytic oxidative C-C bond formation catalysed by the berberine bridge enzyme: Optimal reaction conditions
    • Resch V, Schrittwieser JH, Wallner S, Macheroux P, Kroutil W. Biocatalytic oxidative C-C bond formation catalysed by the berberine bridge enzyme: Optimal reaction conditions. Adv Synth Catal 2011;353:2377-83.
    • (2011) Adv Synth Catal , vol.353 , pp. 2377-2383
    • Resch, V.1    Schrittwieser, J.H.2    Wallner, S.3    Macheroux, P.4    Kroutil, W.5
  • 61
    • 33747062736 scopus 로고    scopus 로고
    • Crystallization of ΔI-tetrahydrocannabinolic acid (THCA) synthase from Cannabis sativa
    • Shoyama Y, Takeuchi A, Taura F, et al. Crystallization of ΔI-tetrahydrocannabinolic acid (THCA) synthase from Cannabis sativa. Acta Crystallogr Sect F Struct Biol Cryst Commun 2005;61:799-801.
    • (2005) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.61 , pp. 799-801
    • Shoyama, Y.1    Takeuchi, A.2    Taura, F.3
  • 62
    • 0842264011 scopus 로고    scopus 로고
    • Tobacco nectarin V is a flavin-containing berberine bridge enzymelike protein with glucose oxidase activity
    • Carter CJ, Thornburg RW. Tobacco nectarin V is a flavin-containing berberine bridge enzymelike protein with glucose oxidase activity. Plant Physiol 2004;134:460-9.
    • (2004) Plant Physiol , vol.134 , pp. 460-469
    • Carter, C.J.1    Thornburg, R.W.2
  • 63
    • 26444599607 scopus 로고    scopus 로고
    • Primary structure, recombinant expression, and molecular characterization of Phl p 4, a major allergen of timothy grass (Phleum pratense)
    • Nandy A, Petersen A, Wald M, et al. Primary structure, recombinant expression, and molecular characterization of Phl p 4, a major allergen of timothy grass (Phleum pratense). Biochem Biophys Res Commun 2005;337:563-70.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 563-570
    • Nandy, A.1    Petersen, A.2    Wald, M.3
  • 64
    • 79957606715 scopus 로고    scopus 로고
    • Heterologous expression of two FAD-dependent oxidases with (S)-tetrahydroprotoberberine oxidase activity from Argemone mexicana and Berberis wilsoniae in insect cells
    • Gesell A, Chávez MLD, Kramell R, Piotrowski M, Macheroux P, Kutchan TM. Heterologous expression of two FAD-dependent oxidases with (S)-tetrahydroprotoberberine oxidase activity from Argemone mexicana and Berberis wilsoniae in insect cells. Planta 2011;233:1185-97.
    • (2011) Planta , vol.233 , pp. 1185-1197
    • Gesell, A.1    Chávez, M.L.D.2    Kramell, R.3    Piotrowski, M.4    Macheroux, P.5    Kutchan, T.M.6
  • 65
    • 33645027769 scopus 로고    scopus 로고
    • Cloning, expression and immunological characterization of full-length timothy grass pollen allergen Phl p 4, a berberine bridge enzymelike protein with homology to celery allergen Api g 5
    • Dewitt AM, Andersson K, Peltre G, Lidholm J. Cloning, expression and immunological characterization of full-length timothy grass pollen allergen Phl p 4, a berberine bridge enzymelike protein with homology to celery allergen Api g 5. Clin Exp Allergy 2006;36:77-86.
    • (2006) Clin Exp Allergy , vol.36 , pp. 77-86
    • Dewitt, A.M.1    Andersson, K.2    Peltre, G.3    Lidholm, J.4
  • 66
    • 4544339836 scopus 로고    scopus 로고
    • The gene controlling marijuana psychoactivity. Molecular cloning and heterologous expression of ΔI-tetrahydrocannabinolic acid synthase from Cannabis sativa L
    • Sirikantaramas S, Morimoto S, Shoyama Y, et al. The gene controlling marijuana psychoactivity. Molecular cloning and heterologous expression of ΔI-tetrahydrocannabinolic acid synthase from Cannabis sativa L. J Biol Chem 2004;279:39767-74.
    • (2004) J Biol Chem , vol.279 , pp. 39767-39774
    • Sirikantaramas, S.1    Morimoto, S.2    Shoyama, Y.3
  • 67
    • 3042825308 scopus 로고    scopus 로고
    • Is the nectar redox cycle a floral defense against microbial attack
    • Carter C, Thornburg RW. Is the nectar redox cycle a floral defense against microbial attack? Trends Plant Sci 2004;9:320-4.
    • (2004) Trends Plant Sci , vol.9 , pp. 320-324
    • Carter, C.1    Thornburg, R.W.2
  • 68
    • 3242714310 scopus 로고    scopus 로고
    • Isolation and characterisation of a class of carbohydrate oxidases from higher plants, with a role in active defence
    • Custers JH, Harrison SJ, Sela-Buurlage MB, et al. Isolation and characterisation of a class of carbohydrate oxidases from higher plants, with a role in active defence. Plant J 2004; 39:147-60.
    • (2004) Plant J , vol.39 , pp. 147-160
    • Custers, J.H.1    Harrison, S.J.2    Sela-Buurlage, M.B.3
  • 69
    • 0030896799 scopus 로고    scopus 로고
    • Hexose oxidase from the red alga Chondrus crispus. Purification, molecular cloning, and expression in Pichia pastoris
    • Hansen OC, Stougaard P. Hexose oxidase from the red alga Chondrus crispus. Purification, molecular cloning, and expression in Pichia pastoris. J Biol Chem 1997;272:11581-7.
    • (1997) J Biol Chem , vol.272 , pp. 11581-11587
    • Hansen, O.C.1    Stougaard, P.2
  • 70
    • 33745229673 scopus 로고    scopus 로고
    • Characterization of the flavin association in hexose oxidase from Chondrus crispus
    • Rand T, Qvist KB, Walter CP, Poulsen CH. Characterization of the flavin association in hexose oxidase from Chondrus crispus. FEBS J 2006;273:2693-703.
    • (2006) FEBS J , vol.273 , pp. 2693-2703
    • Rand, T.1    Qvist, K.B.2    Walter, C.P.3    Poulsen, C.H.4
  • 71
    • 0031952038 scopus 로고    scopus 로고
    • Purification and characterization of a hexose oxidase with excellent strengthening effects in bread
    • Poulsen C, Høstrup PB. Purification and characterization of a hexose oxidase with excellent strengthening effects in bread. Cereal Chem 1998;75:51-7.
    • (1998) Cereal Chem , vol.75 , pp. 51-57
    • Poulsen, C.1    Høstrup, P.B.2
  • 73
    • 0034809461 scopus 로고    scopus 로고
    • Structural characterization of the 60-kDa Bermuda grass pollen isoallergens, a covalent flavoprotein
    • Liaw SH, Lee DY, Chow LP, Lau GX, Su SN. Structural characterization of the 60-kDa Bermuda grass pollen isoallergens, a covalent flavoprotein. Biochem Biophys Res Commun 2001;280:738-43.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 738-743
    • Liaw, S.H.1    Lee, D.Y.2    Chow, L.P.3    Lau, G.X.4    Su, S.N.5
  • 74
    • 0000959670 scopus 로고
    • The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis
    • Steffens P, Nagakura N, Zenk MH. The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis. Tetrahedron Lett 1984;25:951-2.
    • (1984) Tetrahedron Lett , vol.25 , pp. 951-952
    • Steffens, P.1    Nagakura, N.2    Zenk, M.H.3
  • 75
    • 2142796655 scopus 로고
    • (S)-tetrahydroprotoberberine oxidase the final enzyme in protoberberine biosynthesis
    • Amann M, Nagakura N, Zenk MH. (S)-tetrahydroprotoberberine oxidase the final enzyme in protoberberine biosynthesis. Tetrahedron Lett 1984;25:953-4.
    • (1984) Tetrahedron Lett , vol.25 , pp. 953-954
    • Amann, M.1    Nagakura, N.2    Zenk, M.H.3
  • 76
    • 0024288202 scopus 로고
    • Purification and properties of (S)-tetrahydroprotoberberine oxidase from suspension-cultured cells of Berberis wilsoniae
    • Amann M, Nagakura N, Zenk MH. Purification and properties of (S)-tetrahydroprotoberberine oxidase from suspension-cultured cells of Berberis wilsoniae. Eur J Biochem 1988; 175:17-25.
    • (1988) Eur J Biochem , vol.175 , pp. 17-25
    • Amann, M.1    Nagakura, N.2    Zenk, M.H.3
  • 77
    • 0032143041 scopus 로고    scopus 로고
    • Enzymatic oxidations in the biosynthesis of complex alkaloids
    • Chou WM, Kutchan TM. Enzymatic oxidations in the biosynthesis of complex alkaloids. Plant J 1998;15:289-300.
    • (1998) Plant J , vol.15 , pp. 289-300
    • Chou, W.M.1    Kutchan, T.M.2
  • 78
    • 0028886934 scopus 로고
    • First direct evidence for the mechanism of ΔI-tetrahydrocannabinolic acid biosynthesis
    • Taura F, Morimoto S, Shoyama Y, Mechoulam R. First direct evidence for the mechanism of ΔI-tetrahydrocannabinolic acid biosynthesis. J Am Chem Soc 1995;117 (38):9766-7.
    • (1995) J Am Chem Soc , vol.117 , Issue.38 , pp. 9766-9767
    • Taura, F.1    Morimoto, S.2    Shoyama, Y.3    Mechoulam, R.4
  • 79
    • 0019308268 scopus 로고
    • Constituents of Cannabis sativa L. XVII. A review of the natural constituents
    • Turner CE, Elsohly MA, Boeren EG. Constituents of Cannabis sativa L. XVII. A review of the natural constituents. J Nat Prod 1980;43:169-234.
    • (1980) J Nat Prod , vol.43 , pp. 169-234
    • Turner, C.E.1    Elsohly, M.A.2    Boeren, E.G.3
  • 80
    • 30444457225 scopus 로고    scopus 로고
    • Cannabinoid pharmacology: The first 66 years
    • Pertwee RG. Cannabinoid pharmacology: the first 66 years. Br J Pharmacol 2006;147 Suppl 1:S163-71.
    • (2006) Br J Pharmacol , vol.147 , pp. S163-S171
    • Pertwee, R.G.1
  • 81
    • 84884474728 scopus 로고    scopus 로고
    • Pharmacological actions of cannabinoids
    • Pertwee RG. Pharmacological actions of cannabinoids. Handb Exp Pharmacol 2005; 168:1-51.
    • (2005) Handb Exp Pharmacol , vol.168 , pp. 1-51
    • Pertwee, R.G.1
  • 82
    • 33645502759 scopus 로고    scopus 로고
    • The pharmacology of cannabinoid receptors and their ligands: An overview
    • Pertwee RG. The pharmacology of cannabinoid receptors and their ligands: an overview. Int J Obes 2006;30 Suppl 1:13-8.
    • (2006) Int J Obes , vol.30 , pp. 13-18
    • Pertwee, R.G.1
  • 83
    • 38349156729 scopus 로고    scopus 로고
    • Cannabinoids and multiple sclerosis
    • Pertwee RG. Cannabinoids and multiple sclerosis. Mol Neurobiol 2007;36:45-59.
    • (2007) Mol Neurobiol , vol.36 , pp. 45-59
    • Pertwee, R.G.1
  • 85
    • 0142166330 scopus 로고    scopus 로고
    • Cannabinoids: Potential anticancer agents
    • Guzman M. Cannabinoids: potential anticancer agents. Nat Rev Cancer 2003;3:745-55.
    • (2003) Nat Rev Cancer , vol.3 , pp. 745-755
    • Guzman, M.1
  • 87
    • 34547745966 scopus 로고    scopus 로고
    • Production of ΔI-tetrahydrocannabinolic acid by the biosynthetic enzyme secreted from transgenic Pichia pastoris
    • Taura F, Dono E, Sirikantaramas S, Yoshimura K, Shoyama Y, Morimoto S. Production of ΔI-tetrahydrocannabinolic acid by the biosynthetic enzyme secreted from transgenic Pichia pastoris. Biochem Biophys Res Commun 2007;361:675-80.
    • (2007) Biochem Biophys Res Commun , vol.361 , pp. 675-680
    • Taura, F.1    Dono, E.2    Sirikantaramas, S.3    Yoshimura, K.4    Shoyama, Y.5    Morimoto, S.6
  • 88
    • 84866307017 scopus 로고    scopus 로고
    • Structure and function of ΔI-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa
    • Shoyama Y, Tamada T, Kurihara K, et al. Structure and function of ΔI-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa. J Mol Biol 2012;423:96-105.
    • (2012) J Mol Biol , vol.423 , pp. 96-105
    • Shoyama, Y.1    Tamada, T.2    Kurihara, K.3
  • 89
    • 0033197629 scopus 로고    scopus 로고
    • Nectarin I is a novel, soluble germin-like protein expressed in the nectar of Nicotiana sp
    • Carter C, Graham RA, Thornburg RW. Nectarin I is a novel, soluble germin-like protein expressed in the nectar of Nicotiana sp. Plant Mol Biol 1999;41:207-16.
    • (1999) Plant Mol Biol , vol.41 , pp. 207-216
    • Carter, C.1    Graham, R.A.2    Thornburg, R.W.3
  • 90
    • 0032510788 scopus 로고    scopus 로고
    • Defense activation and enhanced pathogen tolerance induced by Hinf2/infOinf2/inf in transgenic tobacco
    • Chamnongpol S, Willekens H, Moeder W, et al. Defense activation and enhanced pathogen tolerance induced by Hinf2/infOinf2/inf in transgenic tobacco. Proc Natl Acad Sci U S A 1998; 95:5818-23.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5818-5823
    • Chamnongpol, S.1    Willekens, H.2    Moeder, W.3
  • 91
    • 0031448239 scopus 로고    scopus 로고
    • Mechanisms for the generation of reactive oxygen species in plant defence - A broad perspective
    • Bolwell GP, Wojtaszek P. Mechanisms for the generation of reactive oxygen species in plant defence - A broad perspective. Physiol Mol Plant Pathol 1997;51 (6):347-66.
    • (1997) Physiol Mol Plant Pathol , vol.51 , Issue.6 , pp. 347-366
    • Bolwell, G.P.1    Wojtaszek, P.2
  • 92
    • 0029360613 scopus 로고
    • Disease resistance conferred by expression of a gene encoding Hinf2/infOinf2/inf-generating glucose oxidase in transgenic potato plants
    • Wu G, Shortt BJ, Lawrence EB, Levine EB, Fitzsimmons KC, Shah DM. Disease resistance conferred by expression of a gene encoding Hinf2/infOinf2/inf-generating glucose oxidase in transgenic potato plants. Plant Cell 1995;7:1357-68.
    • (1995) Plant Cell , vol.7 , pp. 1357-1368
    • Wu, G.1    Shortt, B.J.2    Lawrence, E.B.3    Levine, E.B.4    Fitzsimmons, K.C.5    Shah, D.M.6
  • 93
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: An early plant response to pathogen infection
    • Wojtaszek P. Oxidative burst: an early plant response to pathogen infection. Biochem J 1997;322:681-92.
    • (1997) Biochem J , vol.322 , pp. 681-692
    • Wojtaszek, P.1
  • 94
    • 0032828662 scopus 로고    scopus 로고
    • Crystallization and preliminary diffraction data of 60-kDa glycosylated pollen isoallergens from Bermuda grass
    • Liaw SH, Lee DY, Yang SY, Su SN. Crystallization and preliminary diffraction data of 60-kDa glycosylated pollen isoallergens from Bermuda grass. J Struct Biol 1999;127:83-7.
    • (1999) J Struct Biol , vol.127 , pp. 83-87
    • Liaw, S.H.1    Lee, D.Y.2    Yang, S.Y.3    Su, S.N.4
  • 95
    • 0034017209 scopus 로고    scopus 로고
    • N-terminal sequences of high molecular weight allergens from celery tuber
    • Ganglberger E, Radauer C, Grimm R, et al. N-terminal sequences of high molecular weight allergens from celery tuber. Clin Exp Allergy 2000;30:566-70.
    • (2000) Clin Exp Allergy , vol.30 , pp. 566-570
    • Ganglberger, E.1    Radauer, C.2    Grimm, R.3
  • 96
    • 0141483499 scopus 로고    scopus 로고
    • Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients
    • Bublin M, Radauer C, Wilson IB, et al. Cross-reactive N-glycans of Api g 5, a high molecular weight glycoprotein allergen from celery, are required for immunoglobulin E binding and activation of effector cells from allergic patients. FASEB J 2003;17:1697-9.
    • (2003) FASEB J , vol.17 , pp. 1697-1699
    • Bublin, M.1    Radauer, C.2    Wilson, I.B.3
  • 100
    • 34948867313 scopus 로고    scopus 로고
    • Changing the substrate specificity of a chitooligosac-charide oxidase from Fusarium graminearum by model-inspired site-directed mutagenesis
    • Heuts DPHM, Janssen DB, Fraaije MW. Changing the substrate specificity of a chitooligosac-charide oxidase from Fusarium graminearum by model-inspired site-directed mutagenesis. FEBS Lett 2007;581:4905-9.
    • (2007) FEBS Lett , vol.581 , pp. 4905-4909
    • Heuts, D.P.H.M.1    Janssen, D.B.2    Fraaije, M.W.3
  • 101
    • 0033083604 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of O-methyltransferas-es common to isoquinoline alkaloid and phenylpropanoid biosynthesis
    • Frick S, Kutchan TM. Molecular cloning and functional expression of O-methyltransferas-es common to isoquinoline alkaloid and phenylpropanoid biosynthesis. Plant J 1999; 17:329-39.
    • (1999) Plant J , vol.17 , pp. 329-339
    • Frick, S.1    Kutchan, T.M.2
  • 102
    • 15444344334 scopus 로고    scopus 로고
    • Analysis of a chemical plant defense mechanism in grasses
    • Frey M, Chomet P, Glawischnig E, et al. Analysis of a chemical plant defense mechanism in grasses. Science 1997;277:696-9.
    • (1997) Science , vol.277 , pp. 696-699
    • Frey, M.1    Chomet, P.2    Glawischnig, E.3
  • 103
    • 0001558039 scopus 로고
    • Phytoalexin accumulation in Arabidopsis thaliana during the hypersensitive reaction to Pseudomonas syringae pv syringae
    • Tsuji J, Jackson EP, Gage DA, Hammerschmidt R, Somerville SC. Phytoalexin accumulation in Arabidopsis thaliana during the hypersensitive reaction to Pseudomonas syringae pv syringae. Plant Physiol 1992;98:1304-9.
    • (1992) Plant Physiol , vol.98 , pp. 1304-1309
    • Tsuji, J.1    Jackson, E.P.2    Gage, D.A.3    Hammerschmidt, R.4    Somerville, S.C.5
  • 104
    • 34247598751 scopus 로고    scopus 로고
    • Phytochemical genomics in Arabidopsis thaliana: A case study for functional identification of flavonoid biosynthesis genes
    • Tohge T, Yonekura-Sakakibara K, Niida R, Watanabe-Takahashi A, Saito K. Phytochemical genomics in Arabidopsis thaliana: A case study for functional identification of flavonoid biosynthesis genes. Pure Appl Chem 2007;79:811-23.
    • (2007) Pure Appl Chem , vol.79 , pp. 811-823
    • Tohge, T.1    Yonekura-Sakakibara, K.2    Niida, R.3    Watanabe-Takahashi, A.4    Saito, K.5
  • 106
    • 10744226660 scopus 로고    scopus 로고
    • Terpenoid metabolism in wild-type and transgenic Arabidopsis plants
    • Aharoni A, Giri AP, Deuerlein S, et al. Terpenoid metabolism in wild-type and transgenic Arabidopsis plants. Plant Cell 2003;15:2866-84.
    • (2003) Plant Cell , vol.15 , pp. 2866-2884
    • Aharoni, A.1    Giri, A.P.2    Deuerlein, S.3
  • 107
    • 0037085468 scopus 로고    scopus 로고
    • Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification
    • Li L, He Z, Pandey GK, Tsuchiya T, Luan S. Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification. J Biol Chem 2002;277:5360-8.
    • (2002) J Biol Chem , vol.277 , pp. 5360-5368
    • Li, L.1    He, Z.2    Pandey, G.K.3    Tsuchiya, T.4    Luan, S.5
  • 108
  • 110
    • 77954296666 scopus 로고    scopus 로고
    • A new bioinformatics analysis tools framework at EMBL-EBI
    • Goujon M, McWilliam H, Li W, et al. A new bioinformatics analysis tools framework at EMBL-EBI. Nucleic Acids Res 2010;38:695-9.
    • (2010) Nucleic Acids Res , vol.38 , pp. 695-699
    • Goujon, M.1    McWilliam, H.2    Li, W.3
  • 112
    • 0026068184 scopus 로고
    • Purification and characterization of a novel glucooligosaccharide oxidase from Acremonium strictum T1
    • Lin SF, Yang TY, Inukai T, Yamasaki M, Tsai YC. Purification and characterization of a novel glucooligosaccharide oxidase from Acremonium strictum T1. Biochim Biophys Acta 1991;1118:41-7.
    • (1991) Biochim Biophys Acta , vol.1118 , pp. 41-47
    • Lin, S.F.1    Yang, T.Y.2    Inukai, T.3    Yamasaki, M.4    Tsai, Y.C.5
  • 113
    • 0027316509 scopus 로고
    • Production of novel oligosaccharide oxidase by wheat bran solid-state fermentation
    • Lin SF, Hu HM, Inukal T, Tsai YC. Production of novel oligosaccharide oxidase by wheat bran solid-state fermentation. Biotechnol Adv 1993;11:417-27.
    • (1993) Biotechnol Adv , vol.11 , pp. 417-427
    • Lin, S.F.1    Hu, H.M.2    Inukal, T.3    Tsai, Y.C.4
  • 114
    • 0034690303 scopus 로고    scopus 로고
    • Characterization of kinetics and thermostability of Acre-monium strictum glucooligosaccharide oxidase
    • Fan Z, Oguntimein GB, Reilly PJ. Characterization of kinetics and thermostability of Acre-monium strictum glucooligosaccharide oxidase. Biotechnol Bioeng 2000;68:231-7.
    • (2000) Biotechnol Bioeng , vol.68 , pp. 231-237
    • Fan, Z.1    Oguntimein, G.B.2    Reilly, P.J.3
  • 115
    • 80051784157 scopus 로고    scopus 로고
    • Altered substrate specificity of the gluco-oligosaccharide oxidase from Acremonium strictum
    • Foumani M, Vuong TV, Master ER. Altered substrate specificity of the gluco-oligosaccharide oxidase from Acremonium strictum. Biotechnol Bioeng 2011;108:2261-9.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2261-2269
    • Foumani, M.1    Vuong, T.V.2    Master, E.R.3
  • 116
    • 34547536569 scopus 로고    scopus 로고
    • Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual fla-voenzyme with a dual active site
    • Alexeev I, Sultana A, Mäntsälä P, Niemi J, Schneider G. Aclacinomycin oxidoreductase (AknOx) from the biosynthetic pathway of the antibiotic aclacinomycin is an unusual fla-voenzyme with a dual active site. Proc Natl Acad Sci U S A 2007;104:6170-5.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6170-6175
    • Alexeev, I.1    Sultana, A.2    Mäntsälä, P.3    Niemi, J.4    Schneider, G.5
  • 117
    • 79960683560 scopus 로고    scopus 로고
    • Tirandamycin biosynthesis is mediated by co-dependent oxidative enzymes
    • Carlson JC, Li S, Gunatilleke SS, et al. Tirandamycin biosynthesis is mediated by co-dependent oxidative enzymes. Nature Chem 2011;3:628-33.
    • (2011) Nature Chem , vol.3 , pp. 628-633
    • Carlson, J.C.1    Li, S.2    Gunatilleke, S.S.3
  • 118
    • 35948952728 scopus 로고    scopus 로고
    • A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation
    • Li YS, Ho JY, Huang CC, et al. A unique flavin mononucleotide-linked primary alcohol oxidase for glycopeptide A40926 maturation. J Am Chem Soc 2007;129:13384-5.
    • (2007) J Am Chem Soc , vol.129 , pp. 13384-13385
    • Li, Y.S.1    Ho, J.Y.2    Huang, C.C.3
  • 119
    • 79955585866 scopus 로고    scopus 로고
    • Characterization of TrdL as a 10-hydroxy dehydrogenase and generation of new analogues from a tirandamycin biosynthetic pathway
    • Mo X, Huang H, Ma J, et al. Characterization of TrdL as a 10-hydroxy dehydrogenase and generation of new analogues from a tirandamycin biosynthetic pathway. Org Lett 2011;13:2212-5.
    • (2011) Org Lett , vol.13 , pp. 2212-2215
    • Mo, X.1    Huang, H.2    Ma, J.3
  • 120
    • 79959540983 scopus 로고    scopus 로고
    • The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis
    • Noinaj N, Bosserman MA, Schickli MA, et al. The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis. J Biol Chem 2011;286:23533-43.
    • (2011) J Biol Chem , vol.286 , pp. 23533-23543
    • Noinaj, N.1    Bosserman, M.A.2    Schickli, M.A.3
  • 121
    • 77951228730 scopus 로고    scopus 로고
    • Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst
    • Abad S, Nahalka J, Bergler G, et al. Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst. Microb Cell Fact 2010;9:24.
    • (2010) Microb Cell Fact , vol.9 , pp. 24
    • Abad, S.1    Nahalka, J.2    Bergler, G.3
  • 122
    • 67651173021 scopus 로고    scopus 로고
    • GilR, an unusual lactone-forming enzyme involved in gilvocarcin biosynthesis
    • Kharel MK, Pahari P, Lian H, Rohr J. GilR, an unusual lactone-forming enzyme involved in gilvocarcin biosynthesis. ChemBioChem 2009;10:1305-8.
    • (2009) ChemBioChem , vol.10 , pp. 1305-1308
    • Kharel, M.K.1    Pahari, P.2    Lian, H.3    Rohr, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.