메뉴 건너뛰기




Volumn 50, Issue 24, 2011, Pages 5535-5543

Flavoprotein hydroxylase PgaE catalyzes two consecutive oxygen-dependent tailoring reactions in angucycline biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CYCLES; FLAVOENZYMES; HYDROXYLASES; IN-VITRO; IN-VIVO; KINETIC PROPERTIES; MULTI-STEP; OXYGEN ATOM; PRODUCT DEGRADATION; REACTION CASCADES; REACTION YIELDS; REACTIVE INTERMEDIATE; REDOX CASCADES; REDUCTASE GENES; SHORT CHAIN ALCOHOLS; SIMPLIFIED MODELS;

EID: 79959274080     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200600k     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 15744392112 scopus 로고    scopus 로고
    • Retymicin, galtamycin B, saquayamycin Z and ribofuranosyllumichrome, novel secondary metabolites from Micromonospora sp. Tü 6368 - I. Taxonomy, fermentation, isolation and biological activities
    • Antal, N., Fiedler, H. P., Stackebrandt, E., Beil, W., Stroch, K., and Zeeck, A. (2005) Retymicin, galtamycin B, saquayamycin Z and ribofuranosyllumichrome, novel secondary metabolites from Micromonospora sp. Tu 6368. I. Taxonomy, fermentation, isolation and biological activities J. Antibiot. 58, 95-102 (Pubitemid 40410230)
    • (2005) Journal of Antibiotics , vol.58 , Issue.2 , pp. 95-102
    • Antal, N.1    Fiedler, H.-P.2    Stackebrandt, E.3    Beil, W.4    Stroch, K.5    Zeeck, A.6
  • 3
    • 0038264240 scopus 로고    scopus 로고
    • Seitomycin: Isolation, structure elucidation and biological activity of a new angucycline antibiotic from a terrestrial streptomycete
    • Abdelfattah, M., Maskey, R. P., Asolkar, R. N., Grun-Wollny, I., and Laatsch, H. (2003) Seitomycin: Isolation, structure elucidation and biological activity of a new angucycline antibiotic from a terrestrial streptomycete J. Antibiot. 56, 539-542 (Pubitemid 36849941)
    • (2003) Journal of Antibiotics , vol.56 , Issue.6 , pp. 539-542
    • Abdelfattah, M.1    Maskey, R.P.2    Asolkar, R.N.3    Grun-Wollny, I.4    Laatsch, H.5
  • 4
    • 36049018701 scopus 로고    scopus 로고
    • Mechanisms underlying the anticancer activities of the angucycline landomycin E
    • DOI 10.1016/j.bcp.2007.08.026, PII S0006295207005874
    • Korynevska, A., Heffeter, P., Matselyukh, B., Elbling, L., Micksche, M., Stoika, R., and Berger, W. (2007) Mechanisms underlying the anticancer activities of the angucycline landomycin E Biochem. Pharmacol. 74, 1713-1726 (Pubitemid 350088682)
    • (2007) Biochemical Pharmacology , vol.74 , Issue.12 , pp. 1713-1726
    • Korynevska, A.1    Heffeter, P.2    Matselyukh, B.3    Elbling, L.4    Micksche, M.5    Stoika, R.6    Berger, W.7
  • 5
    • 60349090133 scopus 로고    scopus 로고
    • Elucidation of oxygenation steps during oviedomycin biosynthesis and generation of derivatives with increased antitumor activity
    • Lombo, F., Abdelfattah, M. S., Brana, A. F., Salas, J. A., Rohr, J., and Mendez, C. (2009) Elucidation of oxygenation steps during oviedomycin biosynthesis and generation of derivatives with increased antitumor activity ChemBioChem 10, 296-303
    • (2009) ChemBioChem , vol.10 , pp. 296-303
    • Lombo, F.1    Abdelfattah, M.S.2    Brana, A.F.3    Salas, J.A.4    Rohr, J.5    Mendez, C.6
  • 8
    • 77953572884 scopus 로고    scopus 로고
    • Enzymatic total synthesis of rabelomycin, an angucycline group antibiotic
    • Kharel, M. K., Pahari, P., Lian, H., and Rohr, J. (2010) Enzymatic total synthesis of rabelomycin, an angucycline group antibiotic Org. Lett. 12, 2814-2817
    • (2010) Org. Lett. , vol.12 , pp. 2814-2817
    • Kharel, M.K.1    Pahari, P.2    Lian, H.3    Rohr, J.4
  • 9
    • 0033977621 scopus 로고    scopus 로고
    • Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin A in Streptomyces fradiae Tu2717
    • Faust, B., Hoffmeister, D., Weitnauer, G., Westrich, L., Haag, S., Schneider, P., Decker, H., Kunzel, E., Rohr, J., and Bechthold, A. (2000) Two new tailoring enzymes, a glycosyltransferase and an oxygenase, involved in biosynthesis of the angucycline antibiotic urdamycin A in Streptomyces fradiae Tu2717 Microbiology 146 (Part 1) 147-154 (Pubitemid 30066316)
    • (2000) Microbiology , vol.146 , Issue.1 , pp. 147-154
    • Faust, B.1    Hoffmeister, D.2    Weitnauer, G.3    Westrich, L.4    Haag, S.5    Schneider, P.6    Decker, H.7    Kunzel, E.8    Rohr, J.9    Bechthold, A.10
  • 10
    • 33845309142 scopus 로고    scopus 로고
    • On the acceptor substrate of C-glycosyl-transferase UrdGT2: Three prejadomycin C-glycosides from an engineered mutant of Streptomyces globisporus 1912 ΔlndE(urdGT2)
    • DOI 10.1002/anie.200603176
    • Baig, I., Kharel, M., Kobylyanskyy, A., Zhu, L., Rebets, Y., Ostash, B., Luzhetskyy, A., Bechthold, A., Fedorenko, V. A., and Rohr, J. (2006) On the acceptor substrate of C-glycosyltransferase UrdGT2: Three prejadomycin C-Glycosides from an engineered mutant of Streptomyces globisporus 1912 ΔlndE(urdGT2) Angew. Chem., Int. Ed. 45, 7842-7846 (Pubitemid 44871359)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.46 , pp. 7842-7846
    • Baig, I.1    Kharel, M.2    Kobylyanskyy, A.3    Zhu, L.4    Rebets, Y.5    Ostash, B.6    Luzhetskyy, A.7    Bechthold, A.8    Fedorenko, V.A.9    Rohr, J.10
  • 11
    • 34548707013 scopus 로고    scopus 로고
    • Artificial reconstruction of two cryptic angucycline antibiotic biosynthetic pathways
    • DOI 10.1002/cbic.200700140
    • Palmu, K., Ishida, K., Mäntsälä, P., Hertweck, C., and Metsä-Ketelä, M. (2007) Artificial reconstruction of two cryptic angucycline antibiotic biosynthetic pathways ChemBioChem 8, 1577-1584 (Pubitemid 47436915)
    • (2007) ChemBioChem , vol.8 , Issue.13 , pp. 1577-1584
    • Palmu, K.1    Ishida, K.2    Mantsala, P.3    Hertweck, C.4    Metsa-Ketela, M.5
  • 12
    • 20444496509 scopus 로고    scopus 로고
    • Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase
    • DOI 10.1074/jbc.M414229200
    • Chen, Y. H., Wang, C. C., Greenwell, L., Rix, U., Hoffmeister, D., Vining, L. C., Rohr, J., and Yang, K. Q. (2005) Functional analyses of oxygenases in jadomycin biosynthesis and identification of JadH as a bifunctional oxygenase/dehydrase J. Biol. Chem. 280, 22508-22514 (Pubitemid 40827908)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22508-22514
    • Chen, Y.-H.1    Wang, C.-C.2    Greenwell, L.3    Rix, U.4    Hoffmeister, D.5    Vining, L.C.6    Rohr, J.7    Yang, K.-Q.8
  • 13
    • 34548172398 scopus 로고    scopus 로고
    • Crystal Structures of Two Aromatic Hydroxylases Involved in the Early Tailoring Steps of Angucycline Biosynthesis
    • DOI 10.1016/j.jmb.2007.06.087, PII S0022283607008777
    • Koskiniemi, H., Metsä-Ketelä, M., Dobritzsch, D., Kallio, P., Korhonen, H., Mäntsälä, P., Schneider, G., and Niemi, J. (2007) Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis J. Mol. Biol. 372, 633-648 (Pubitemid 47313481)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 633-648
    • Koskiniemi, H.1    Metsa-Ketela, M.2    Dobritzsch, D.3    Kallio, P.4    Korhonen, H.5    Mantsala, P.6    Schneider, G.7    Niemi, J.8
  • 14
    • 39149093384 scopus 로고    scopus 로고
    • Sequential Action of Two Flavoenzymes, PgaE and PgaM, in Angucycline Biosynthesis: Chemoenzymatic Synthesis of Gaudimycin C
    • DOI 10.1016/j.chembiol.2007.12.011, PII S1074552108000367
    • Kallio, P., Liu, Z., Mäntsälä, P., Niemi, J., and Metsä-Ketelä, M. (2008) Sequential action of two flavoenzymes, PgaE and PgaM, in angucycline biosynthesis: Chemoenzymatic synthesis of gaudimycin C Chem. Biol. 15, 157-166 (Pubitemid 351253615)
    • (2008) Chemistry and Biology , vol.15 , Issue.2 , pp. 157-166
    • Kallio, P.1    Liu, Z.2    Mantsala, P.3    Niemi, J.4    Metsa-Ketela, M.5
  • 15
    • 0029001789 scopus 로고
    • Structure and mechanism of para-hydroxybenzoate hydroxylase
    • Entsch, B. and van Berkel, W. J. (1995) Structure and mechanism of para-hydroxybenzoate hydroxylase FASEB J. 9, 476-483
    • (1995) FASEB J. , vol.9 , pp. 476-483
    • Entsch, B.1    Van Berkel, W.J.2
  • 16
    • 37549035471 scopus 로고    scopus 로고
    • A nested gene in Streptomyces bacteria encodes a protein involved in quaternary complex formation
    • Kallio, P., Liu, Z., Mäntsälä, P., Niemi, J., and Metsä-Ketelä, M. (2007) A nested gene in Streptomyces bacteria encodes a protein involved in quaternary complex formation J. Mol. Biol. 375, 1212-1221
    • (2007) J. Mol. Biol. , vol.375 , pp. 1212-1221
    • Kallio, P.1    Liu, Z.2    Mäntsälä, P.3    Niemi, J.4    Metsä- Ketelä, M.5
  • 17
    • 33644766092 scopus 로고    scopus 로고
    • Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: Implications for catalytic mechanism and product stereoselectivity
    • DOI 10.1016/j.jmb.2005.12.064, PII S0022283605016402
    • Kallio, P., Sultana, A., Niemi, J., Mäntsälä, P., and Schneider, G. (2006) Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: Implications for catalytic mechanism and product stereoselectivity J. Mol. Biol. 357, 210-220 (Pubitemid 43339326)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.1 , pp. 210-220
    • Kallio, P.1    Sultana, A.2    Niemi, J.3    Mantsala, P.4    Schneider, G.5
  • 18
    • 4544228113 scopus 로고
    • Simple Method of Anaerobic Cultivation, with Removal of Oxygen by a Buffered Glucose Oxidase-Catalase System
    • Fabian, J. (1965) Simple Method of Anaerobic Cultivation, with Removal of Oxygen by a Buffered Glucose Oxidase-Catalase System J. Bacteriol. 89, 921
    • (1965) J. Bacteriol. , vol.89 , pp. 921
    • Fabian, J.1
  • 19
    • 33846575772 scopus 로고    scopus 로고
    • LanV, a bifunctional enzyme: Aromatase and ketoreductase during landomycin A biosynthesis
    • Mayer, A., Taguchi, T., Linnenbrink, A., Hofmann, C., Luzhetskyy, A., and Bechthold, A. (2005) LanV, a bifunctional enzyme: Aromatase and ketoreductase during landomycin A biosynthesis ChemBioChem 6, 2312-2315
    • (2005) ChemBioChem , vol.6 , pp. 2312-2315
    • Mayer, A.1    Taguchi, T.2    Linnenbrink, A.3    Hofmann, C.4    Luzhetskyy, A.5    Bechthold, A.6
  • 20
    • 19944430903 scopus 로고    scopus 로고
    • Identification of the function of gene lndM2 encoding a bifunctional oxygenase-reductase involved in the biosynthesis of the antitumor antibiotic landomycin E by Streptomyces globisporus 1912 supports the originally assigned structure for landomycinone
    • DOI 10.1021/jo0483623
    • Zhu, L., Ostash, B., Rix, U., Nur-E-Alam, M., Mayers, A., Luzhetskyy, A., Mendez, C., Salas, J. A., Bechthold, A., Fedorenko, V., and Rohr, J. (2005) Identification of the function of gene lndM2 encoding a bifunctional oxygenase-reductase involved in the biosynthesis of the antitumor antibiotic landomycin E by Streptomyces globisporus 1912 supports the originally assigned structure for landomycinone J. Org. Chem. 70, 631-638 (Pubitemid 40129427)
    • (2005) Journal of Organic Chemistry , vol.70 , Issue.2 , pp. 631-638
    • Zhu, L.1    Ostash, B.2    Rix, U.3    Nur-E-Alam, M.4    Mayers, A.5    Luzhetskyy, A.6    Mendez, C.7    Salas, J.A.8    Bechthold, A.9    Fedorenko, V.10    Rohr, J.11
  • 21
    • 0028851501 scopus 로고
    • Degradation of homovanillate by a strain of Variovorax paradoxus via ring hydroxylation
    • Allison, N., Turner, J. E., and Wait, R. (1995) Degradation of homovanillate by a strain of Variovorax paradoxus via ring hydroxylation FEMS Microbiol. Lett. 134, 213-219
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 213-219
    • Allison, N.1    Turner, J.E.2    Wait, R.3
  • 22
    • 77149131524 scopus 로고    scopus 로고
    • Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: A theoretical study
    • Tian, B., Tu, Y., Strid, A., and Eriksson, L. A. (2010) Hydroxylation and ring-opening mechanism of an unusual flavoprotein monooxygenase, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase: A theoretical study Chemistry 16, 2557-2566
    • (2010) Chemistry , vol.16 , pp. 2557-2566
    • Tian, B.1    Tu, Y.2    Strid, A.3    Eriksson, L.A.4
  • 23
    • 0030786917 scopus 로고    scopus 로고
    • Unusual mechanism of oxygen atom transfer and product rearrangement in the catalytic reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase
    • DOI 10.1021/bi970089u
    • Chaiyen, P., Brissette, P., Ballou, D. P., and Massey, V. (1997) Unusual mechanism of oxygen atom transfer and product rearrangement in the catalytic reaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase Biochemistry 36, 8060-8070 (Pubitemid 27284183)
    • (1997) Biochemistry , vol.36 , Issue.26 , pp. 8060-8070
    • Chaiyen, P.1    Brissette, P.2    Ballou, D.P.3    Massey, V.4
  • 24
    • 0038377353 scopus 로고    scopus 로고
    • Purification and characterization of a monooxygenase involved in the biosynthetic pathway of the antitumor drug mithramycin
    • DOI 10.1128/JB.185.13.3962-3965.2003
    • Rodriguez, D., Quiros, L. M., Brana, A. F., and Salas, J. A. (2003) Purification and characterization of a monooxygenase involved in the biosynthetic pathway of the antitumor drug mithramycin J. Bacteriol. 185, 3962-3965 (Pubitemid 36735948)
    • (2003) Journal of Bacteriology , vol.185 , Issue.13 , pp. 3962-3965
    • Rodriguez, D.1    Quiros, L.M.2    Brana, A.F.3    Salas, J.A.4
  • 25
    • 29344449110 scopus 로고    scopus 로고
    • Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus
    • DOI 10.1021/ja055750t
    • Gibson, M., Nur-e-alam, M., Lipata, F., Oliveira, M. A., and Rohr, J. (2005) Characterization of kinetics and products of the Baeyer-Villiger oxygenase MtmOIV, the key enzyme of the biosynthetic pathway toward the natural product anticancer drug mithramycin from Streptomyces argillaceus J. Am. Chem. Soc. 127, 17594-17595 (Pubitemid 43003360)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.50 , pp. 17594-17595
    • Gibson, M.1    Nur-E-Alam, M.2    Lipata, F.3    Oliveira, M.A.4    Rohr, J.5
  • 26
    • 66349089237 scopus 로고    scopus 로고
    • Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway
    • Beam, M. P., Bosserman, M. A., Noinaj, N., Wehenkel, M., and Rohr, J. (2009) Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway Biochemistry 48, 4476-4487
    • (2009) Biochemistry , vol.48 , pp. 4476-4487
    • Beam, M.P.1    Bosserman, M.A.2    Noinaj, N.3    Wehenkel, M.4    Rohr, J.5
  • 27
    • 17944386473 scopus 로고    scopus 로고
    • 3 in Streptomyces griseus: Analysis of the Gene Cluster and Rational Design of Novel Chromomycin Analogs
    • DOI 10.1016/S1074-5521(03)00283-7
    • Menendez, N., Nur-e-Alam, M., Brana, A. F., Rohr, J., Salas, J. A., and Mendez, C. (2004) Biosynthesis of the antitumor chromomycin A3 in Streptomyces griseus: Analysis of the gene cluster and rational design of novel chromomycin analogs Chem. Biol. 11, 21-32 (Pubitemid 38203987)
    • (2004) Chemistry and Biology , vol.11 , Issue.1 , pp. 21-32
    • Menendez, N.1    Nur-e-Alam, M.2    Brana, A.F.3    Rohr, J.U.4    Salas, J.A.5    Mendez, C.6
  • 28
    • 79951892996 scopus 로고    scopus 로고
    • Characterization of the Terminal Activation Step Catalyzed by Oxygenase CmmOIV of the Chromomycin Biosynthetic Pathway from Streptomyces griseus
    • Bosserman, M. A., Flarez, A. B., Shaaban, K. A., Braaa, A. F., Salas, J. A., Méndez, C., and Rohr, J. (2011) Characterization of the Terminal Activation Step Catalyzed by Oxygenase CmmOIV of the Chromomycin Biosynthetic Pathway from Streptomyces griseus Biochemistry 50, 1421-1428
    • (2011) Biochemistry , vol.50 , pp. 1421-1428
    • Bosserman, M.A.1    Flarez, A.B.2    Shaaban, K.A.3    Braaa, A.F.4    Salas, J.A.5    Méndez, C.6    Rohr, J.7
  • 29
    • 20444493372 scopus 로고    scopus 로고
    • The oxidative ring cleavage in jadomycin biosynthesis: A multistep oxygenation cascade in a biosynthetic black box
    • DOI 10.1002/cbic.200400395
    • Rix, U., Wang, C., Chen, Y., Lipata, F. M., Remsing Rix, L. L., Greenwell, L. M., Vining, L. C., Yang, K., and Rohr, J. (2005) The oxidative ring cleavage in jadomycin biosynthesis: A multistep oxygenation cascade in a biosynthetic black box ChemBioChem 6, 838-845 (Pubitemid 40873744)
    • (2005) ChemBioChem , vol.6 , Issue.5 , pp. 838-845
    • Rix, U.1    Wang, C.2    Chen, Y.3    Lipata, F.M.4    Rix, L.L.R.5    Greenwell, L.M.6    Vining, L.C.7    Yang, K.8    Rohr, J.9
  • 31
    • 58149133711 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh, K. L., Jornvall, H., Persson, B., and Oppermann, U. (2008) Medium- and short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes Cell. Mol. Life Sci. 65, 3895-3906
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jornvall, H.2    Persson, B.3    Oppermann, U.4
  • 33
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/ reductases (SDRs)
    • DOI 10.1016/S0009-2797(02)00223-5, PII S0009279702002235
    • Persson, B., Kallberg, Y., Oppermann, U., and Jornvall, H. (2003) Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs) Chem.-Biol. Interact. 143-144, 271-278 (Pubitemid 36253590)
    • (2003) Chemico-Biological Interactions , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jornvall, H.4
  • 35
    • 0037126640 scopus 로고    scopus 로고
    • Structure of bacterial 3β/17β-hydroxysteroid dehydrogenase at 1.2 Å resolution: A model for multiple steroid recognition
    • DOI 10.1021/bi0203684
    • Benach, J., Filling, C., Oppermann, U. C., Roversi, P., Bricogne, G., Berndt, K. D., Jornvall, H., and Ladenstein, R. (2002) Structure of bacterial 3ß/17ß-hydroxysteroid dehydrogenase at 1.2 Å resolution: A model for multiple steroid recognition Biochemistry 41, 14659-14668 (Pubitemid 35476868)
    • (2002) Biochemistry , vol.41 , Issue.50 , pp. 14659-14668
    • Benach, J.1    Filling, C.2    Oppermann, U.C.T.3    Roversi, P.4    Bricogne, G.5    Berndt, K.D.6    Jornvall, H.7    Ladenstein, R.8
  • 38
    • 0037415047 scopus 로고    scopus 로고
    • Urdamycin L: A novel metabolic shunt product that provides evidence for the role of the urdM gene in the urdamycin A biosynthetic pathway of Streptomyces fradiae TÜ 2717
    • DOI 10.1002/cbic.200390002
    • Rix, U., Remsing, L. L., Hoffmeister, D., Bechthold, A., and Rohr, J. (2003) Urdamycin L: A novel metabolic shunt product that provides evidence for the role of the urdM gene in the urdamycin A biosynthetic pathway of Streptomyces fradiae TU 2717 ChemBioChem 4, 109-111 (Pubitemid 36114218)
    • (2003) ChemBioChem , vol.4 , Issue.1 , pp. 109-111
    • Rix, U.1    Remsing, L.L.2    Hoffmeister, D.3    Bechthold, A.4    Rohr, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.