메뉴 건너뛰기




Volumn 287, Issue 7, 2012, Pages 5112-5121

Characterization of SfmD as a heme peroxidase that catalyzes the regioselective hydroxylation of 3-methyltyrosine to 3-hydroxy-5-methyltyrosine in saframycin A biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ANTITUMOR ANTIBIOTICS; BIOCHEMICAL ASSAY; BIOSYNTHETIC PATHWAY; CORE STRUCTURE; HEME BINDING; HEME PEROXIDASE; HETEROLOGOUS EXPRESSION; HYPOTHETICAL PROTEIN; IN-VITRO; KINETIC STUDY; MAGNETIC CIRCULAR DICHROISMS; MECHANISTIC STUDIES; METHYLTRANSFERASES; REGIO-SELECTIVE; TETRAHYDROISOQUINOLINES; WILD TYPES;

EID: 84856866295     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.306316     Document Type: Article
Times cited : (35)

References (40)
  • 1
    • 0036558479 scopus 로고    scopus 로고
    • Chemistry and biology of the tetrahydroisoquinoline antitumor antibiotics
    • DOI 10.1021/cr010212u
    • Scott, J. D., and Williams, R. M. (2002) Chemistry and biology of the tetrahydroisoquinoline antitumor antibiotics. Chem. Rev. 102, 1669-1730 (Pubitemid 35377652)
    • (2002) Chemical Reviews , vol.102 , Issue.5 , pp. 1669-1730
    • Scott, J.D.1    Williams, R.M.2
  • 2
    • 0017652901 scopus 로고
    • New antibiotics saframycins A, B, C, D, and E
    • Arai, T., Takahashi, K., and Kubo, A. (1977) New antibiotics saframycins A, B, C, D, and E. J. Antibiot. 30, 1015-1018
    • (1977) J. Antibiot. , vol.30 , pp. 1015-1018
    • Arai, T.1    Takahashi, K.2    Kubo, A.3
  • 3
    • 61549104994 scopus 로고    scopus 로고
    • Development of Yondelis (trabectedin, ET-743). A semisynthetic process solves the supply problem
    • Cuevas, C., and Francesch, A. (2009) Development of Yondelis (trabectedin, ET-743). A semisynthetic process solves the supply problem. Nat. Prod. Rep. 26, 322-337
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 322-337
    • Cuevas, C.1    Francesch, A.2
  • 4
    • 0021954321 scopus 로고
    • Biosynthetic studies on saframycin A, a quinone antitumor antibiotic produced by streptomyces lavendulae
    • Mikami, Y., Takahashi, K., Yazawa, K., Arai, T., Namikoshi, M., Iwasaki, S., and Okuda, S. (1985) Biosynthetic studies on saframycin A, a quinone antitumor antibiotic produced by Streptomyces lavendulae. J. Biol. Chem. 260, 344-348 (Pubitemid 15164057)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.1 , pp. 344-348
    • Mikami, Y.1    Takahashi, K.2    Yazawa, K.3
  • 5
    • 0022545734 scopus 로고
    • Incorporation of 3'-methyltyrosine and 5'-methyl-DOPA into naphthyridinomycin
    • Palaniswamy, V. A., and Gould, S. J. (1986) The incorporation of 3′-methyltyrosine and 5′-methyl DOPA into naphthyridinomycin. J. Am. Chem. Soc. 108, 5651-5652 (Pubitemid 16023310)
    • (1986) Journal of the American Chemical Society , vol.108 , Issue.18 , pp. 5651-5652
    • Palaniswamy, V.A.1    Gould, S.J.2
  • 6
    • 37549065124 scopus 로고    scopus 로고
    • Characterization of the saframycin A gene cluster from Streptomyces lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system for assembling the unusual tetrapeptidyl skeleton in an iterative manner
    • Li, L., Deng, W., Song, J., Ding, W., Zhao, Q.-F., Peng, C., Song, W.-W., Tang, G.-L., and Liu, W. (2008) Characterization of the saframycin A gene cluster from Streptomyces lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. J. Bacteriol. 190, 251-263
    • (2008) J. Bacteriol. , vol.190 , pp. 251-263
    • Li, L.1    Deng, W.2    Song, J.3    Ding, W.4    Zhao, Q.-F.5    Peng, C.6    Song, W.-W.7    Tang, G.-L.8    Liu, W.9
  • 8
    • 67649437201 scopus 로고    scopus 로고
    • Biosynthesis of 3-hydroxy-5-methyl-o-methyltyrosine in the saframycin/ safracin biosynthetic pathway
    • Fu, C. Y., Tang, M. C., Peng, C., Li, L., He, Y. L., Liu, W., and Tang, G. L. (2009) Biosynthesis of 3-hydroxy-5-methyl-o-methyltyrosine in the saframycin/ safracin biosynthetic pathway. J. Microbiol. Biotechnol. 19, 439-446
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 439-446
    • Fu, C.Y.1    Tang, M.C.2    Peng, C.3    Li, L.4    He, Y.L.5    Liu, W.6    Tang, G.L.7
  • 9
    • 77952542213 scopus 로고    scopus 로고
    • Reconstruction of the saframycin core scaffold defines dual Pictet-Spengler mechanisms
    • Koketsu, K., Watanabe, K., Suda, H., Oguri, H., and Oikawa, H. (2010) Reconstruction of the saframycin core scaffold defines dual Pictet-Spengler mechanisms. Nat. Chem. Biol. 6, 408-410
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 408-410
    • Koketsu, K.1    Watanabe, K.2    Suda, H.3    Oguri, H.4    Oikawa, H.5
  • 10
    • 0032852842 scopus 로고    scopus 로고
    • Tetrahydropterin-dependent amino acid hydroxylases
    • Fitzpatrick, P. F. (1999) Tetrahydropterin-dependent amino acid hydroxylases. Ann. Rev. Biochem. 68, 355-381
    • (1999) Ann. Rev. Biochem. , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 12
    • 43949100296 scopus 로고    scopus 로고
    • Characterization of the two-component, FAD-dependent monooxygenase SgcC that requires carrier protein-tethered substrates for the biosynthesis of the enediyne antitumor antibiotic C-1027
    • DOI 10.1021/ja710601d
    • Lin, S., Van Lanen, S. G., and Shen, B. (2008) Characterization of the two-component, FAD-dependent monooxygenase SgcC that requires carrier protein-tethered substrates for the biosynthesis of the enediyne antitumor antibiotic C-1027. J. Am. Chem. Soc. 130, 6616-6623 (Pubitemid 351706127)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.20 , pp. 6616-6623
    • Lin, S.1    Van Lanen, S.G.2    Shen, B.3
  • 14
    • 0348041999 scopus 로고    scopus 로고
    • Chemoselectivity of the Ruthenium-Catalyzed Hydrative Diyne Cyclization: Total Synthesis of (+)-Cylindricine C, D, and E
    • DOI 10.1021/ol035752n
    • Trost, B. M., and Rudd, M. T. (2003) Chemoselectivity of the rutheniumcatalyzed hydrative diyne cyclization: total synthesis of (+)-cylindricine C, D, and E. Org. Lett. 5, 4599-4602 (Pubitemid 37532980)
    • (2003) Organic Letters , vol.5 , Issue.24 , pp. 4599-4602
    • Trost, B.M.1    Rudd, M.T.2
  • 15
    • 0034741488 scopus 로고    scopus 로고
    • Direct synthesis of Fmoc-protected amino acids using organozinc chemistry: Application to polymethoxylated phenylalanines and 4-oxoamino acids
    • Deboves, H. J., Montalbetti, C. A., and Jackson, R. F. (2001) Direct synthesis of Fmoc-protected amino acids using organozinc chemistry: application to polymethoxylated phenylalanines and 4-oxoamino acids. J. Chem. Soc. Perkin Trans. 1, 1876-1884
    • (2001) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1876-1884
    • Deboves, H.J.1    Montalbetti, C.A.2    Jackson, R.F.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 18
    • 77953743782 scopus 로고    scopus 로고
    • Human liver microsomal cytochrome P450 3A enzymes involved in thalidomide 5-hydroxylation and formation of a glutathione conjugate
    • Chowdhury, G., Murayama, N., Okada, Y., Uno, Y., Shimizu, M., Shibata, N., Guengerich, F. P., and Yamazaki H. (2010) Human liver microsomal cytochrome P450 3A enzymes involved in thalidomide 5-hydroxylation and formation of a glutathione conjugate. Chem. Res. Toxicol. 23, 1018-1024
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1018-1024
    • Chowdhury, G.1    Murayama, N.2    Okada, Y.3    Uno, Y.4    Shimizu, M.5    Shibata, N.6    Guengerich, F.P.7    Yamazaki, H.8
  • 19
    • 0023664844 scopus 로고
    • Purification to homogeneity and initial physical characterization of secondary amine monooxygenase
    • Alberta, J. A., and Dawson, J. H. (1987) Purification to homogeneity and initial physical characterization of secondary amine monooxygenase. J. Biol. Chem. 262, 11857-11863
    • (1987) J. Biol. Chem. , vol.262 , pp. 11857-11863
    • Alberta, J.A.1    Dawson, J.H.2
  • 20
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen, R., Marver, H. S., and Schmid, R. (1968) The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl. Acad. Sci. U.S.A. 61, 748-755
    • (1968) Proc. Natl. Acad. Sci. U.S.A. , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 21
    • 0025728865 scopus 로고
    • Prostaglandin endoperoxide synthase: Structure and catalysis
    • Smith, W. L., and Marnett, L. J. (1991) Prostaglandin endoperoxide synthase: structure and catalysis. Biochim. Biophys. Acta 1083, 1-17
    • (1991) Biochim. Biophys. Acta , vol.1083 , pp. 1-17
    • Smith, W.L.1    Marnett, L.J.2
  • 22
    • 43949096904 scopus 로고    scopus 로고
    • Characterization of TioF, a tryptophan 2,3-dioxygenase involved in 3-hydroxyquinaldic acid formation during thiocoraline biosynthesis
    • DOI 10.1039/b801391h
    • Sheoran, A., King, A., Velasco, A., Pero, J. M., and Garneau-Tsodikova, S. (2008) Characterization of TioF, a tryptophan 2,3-dioxygenase involved in 3-hydroxyquinaldic acid formation during thiocoraline biosynthesis. Mol. Biosyst. 4, 622-628 (Pubitemid 351706306)
    • (2008) Molecular BioSystems , vol.4 , Issue.6 , pp. 622-628
    • Sheoran, A.1    King, A.2    Velasco, A.3    Pero, J.M.4    Garneau-Tsodikova, S.5
  • 23
    • 0000982535 scopus 로고
    • Imidazole- And alkylamine-ligated iron (II, III) chlorin complexes as models for histidine and lysine coordination to iron in dihydroporphyrin- containing proteins: Characterization with magnetic circular dichroism spectroscopy
    • Huff, A. M., Chang, C. K., Cooper, D. K., Smith, K. M., and Dawson, J. H. (1993) Imidazole- and alkylamine-ligated iron (II, III) chlorin complexes as models for histidine and lysine coordination to iron in dihydroporphyrin- containing proteins: characterization with magnetic circular dichroism spectroscopy. Inorg. Chem. 32, 1460-1466
    • (1993) Inorg. Chem. , vol.32 , pp. 1460-1466
    • Huff, A.M.1    Chang, C.K.2    Cooper, D.K.3    Smith, K.M.4    Dawson, J.H.5
  • 24
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • Sugano, Y. (2009) DyP-type peroxidases comprise a novel heme peroxidase family. Cell. Mol. Life Sci. 66, 1387-1403
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1387-1403
    • Sugano, Y.1
  • 26
    • 77954267927 scopus 로고    scopus 로고
    • Thirty years of heme peroxidase structural biology
    • Poulos, T. L. (2010) Thirty years of heme peroxidase structural biology. Arch. Biochem. Biophys. 500, 3-12
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 3-12
    • Poulos, T.L.1
  • 27
    • 0002791918 scopus 로고
    • (Lever, A. B. P., and Gray, H. B., eds) Addison-Wesley, Reading, MA
    • Palmer, G. (1983) in Iron Porphyrins: Part II (Lever, A. B. P., and Gray, H. B., eds) pp. 43-88, Addison-Wesley, Reading, MA
    • (1983) Iron Porphyrins: Part II , pp. 43-88
    • Palmer, G.1
  • 28
    • 0029797089 scopus 로고    scopus 로고
    • EPR detection and characterization of lignin peroxidase porphyrin pi- cation radical
    • DOI 10.1021/bi961297+
    • Khindaria, A., and Aust, S. D. (1996) EPR detection and characterization of lignin peroxidase porphyrin pi-cation radical. Biochemistry 35, 13107-13111 (Pubitemid 26349461)
    • (1996) Biochemistry , vol.35 , Issue.40 , pp. 13107-13111
    • Khindaria, A.1    Aust, S.D.2
  • 30
    • 22544463357 scopus 로고    scopus 로고
    • The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus
    • DOI 10.1042/BJ20041894
    • Allen, J. W., Leach, N., and Ferguson, S. J. (2005) The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus. Biochem. J. 389, 587-592 (Pubitemid 41021162)
    • (2005) Biochemical Journal , vol.389 , Issue.2 , pp. 587-592
    • Allen, J.W.A.1    Leach, N.2    Ferguson, S.J.3
  • 31
    • 0842304657 scopus 로고    scopus 로고
    • Distinct roles of endoplasmic reticulum cytochrome b5 and fused cytochrome b5-like domain for rat delta6-desaturase activity
    • DOI 10.1194/jlr.M300339-JLR200
    • Guillou, H., D'Andrea, S., Rioux, V., Barnouin, R., Dalaine, S., Pedrono, F., Jan, S., and Legrand, P. (2004) Distinct roles of endoplasmic reticulum cytochrome b5 and fused cytochrome b5-like domain for rat δ6-desaturase activity. J. Lipid Res. 45, 32-40 (Pubitemid 38176612)
    • (2004) Journal of Lipid Research , vol.45 , Issue.1 , pp. 32-40
    • Guillou, H.1    D'Andrea, S.2    Rioux, V.3    Barnouin, R.4    Dalaine, S.5    Pedrono, F.6    Jan, S.7    Legrand, P.8
  • 32
    • 33747453769 scopus 로고    scopus 로고
    • Heme: A versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases
    • DOI 10.1038/sj.cr.7310086, PII 7310086
    • Mense, S. M., and Zhang, L. (2006) Heme: a versatile signaling molecule controlling the activities of diverse regulators ranging from transcription factors to MAP kinases. Cell Res. 16, 681-692 (Pubitemid 44258921)
    • (2006) Cell Research , vol.16 , Issue.8 , pp. 681-692
    • Mense, S.M.1    Zhang, L.2
  • 33
    • 0031594596 scopus 로고    scopus 로고
    • The genes ImbB1 and ImbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A
    • DOI 10.1007/s002030050578
    • Neusser, D., Schmidt, H., Spizèk, J., Novotnà, J., Peschke, U., Kaschabeck, S., Tichy, P., and Piepersberg, W. (1998) The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of L-tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A. Arch. Microbiol. 169, 322-332 (Pubitemid 28189536)
    • (1998) Archives of Microbiology , vol.169 , Issue.4 , pp. 322-332
    • Neusser, D.1    Schmidt, H.2    Spizek, J.3    Novotna, J.4    Peschke, U.5    Kaschabeck, S.6    Tichy, P.7    Piepersberg, W.8
  • 34
    • 0020574431 scopus 로고
    • Biosynthesis of the antitumor antibiotic CC-1065 by Streptomyces zelensis
    • Hurley, L. H., and Rokem, J. S. (1983) Biosynthesis of the antitumor antibiotic CC-1065 by Streptomyces zelensis. J. Antibiot. 36, 383-390 (Pubitemid 13080575)
    • (1983) Journal of Antibiotics , vol.36 , Issue.4 , pp. 383-390
    • Hurley, L.H.1    Rokem, J.S.2
  • 35
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • DOI 10.1016/j.bbagen.2006.07.017, PII S0304416506002133
    • Hannemann, F., Bichet, A., Ewen, K. M., and Bernhardt, R. (2007) Cytochrome P450 systems-biological variations of electron transport chains. Biochim. Biophys. Acta 1770, 330-344 (Pubitemid 46157074)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.3 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 37
    • 33749051652 scopus 로고    scopus 로고
    • Heme-thiolate haloperoxidases: Versatile biocatalysts with biotechnological and environmental significance
    • Hofrichter, M., and Ullrich, R. (2006) Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance. Appl. Microbiol. Biotechnol. 71, 276-288
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 276-288
    • Hofrichter, M.1    Ullrich, R.2
  • 39
    • 0017264610 scopus 로고
    • A study of the supposed hydroxylation of tyrosine catalysed by peroxidase
    • Smith, P. I., and Swan, G. A. (1976) A study of the supposed hydroxylation of tyrosine catalysed by peroxidase. Biochem. J. 153, 403-408
    • (1976) Biochem. J. , vol.153 , pp. 403-408
    • Smith, P.I.1    Swan, G.A.2
  • 40
    • 80054756991 scopus 로고    scopus 로고
    • A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin
    • Connor, K. L., Colabroy, K. L., and Gerratana, B. (2011) A heme peroxidase with a functional role as an L-tyrosine hydroxylase in the biosynthesis of anthramycin. Biochemistry. 50, 8926-8936
    • (2011) Biochemistry , vol.50 , pp. 8926-8936
    • Connor, K.L.1    Colabroy, K.L.2    Gerratana, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.