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Volumn 80, Issue 24, 2014, Pages 7473-7483

Operon for biosynthesis of lipstatin, the beta-lactone inhibitor of human pancreatic lipase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; ESTERS; GENES; LINOLEIC ACID;

EID: 84917709080     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01765-14     Document Type: Article
Times cited : (30)

References (55)
  • 2
    • 0023626926 scopus 로고
    • Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. I. Producing organism, fermentation, isolation and biological activity
    • Weibel EK, Hadváry P, Hochuli E, Kupfer E, Lengsfeld H. 1987. Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. I. Producing organism, fermentation, isolation and biological activity. J. Antibiot. (Tokyo) 40:1081-1085.
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 1081-1085
    • Weibel, E.K.1    Hadváry, P.2    Hochuli, E.3    Kupfer, E.4    Lengsfeld, H.5
  • 3
    • 84862582505 scopus 로고    scopus 로고
    • Anti-obesity drugs: a review about their effects and safety
    • Kang JG, Park CY. 2012. Anti-obesity drugs: a review about their effects and safety. Diabetes Metab. J. 36:13-25. http://dx.doi.org/10.4093/dmj.2012.36.1.13.
    • (2012) Diabetes Metab. J. , vol.36 , pp. 13-25
    • Kang, J.G.1    Park, C.Y.2
  • 4
    • 1042303480 scopus 로고    scopus 로고
    • XENical in the prevention of diabetes in obese subjects (XENDOS) study: a randomized study of orlistat as an adjunct to lifestyle changes for the prevention of type 2 diabetes in obese patients
    • Torgerson JS, Hauptman J, Boldrin MN, Sjöström L. 2004. XENical in the prevention of diabetes in obese subjects (XENDOS) study: a randomized study of orlistat as an adjunct to lifestyle changes for the prevention of type 2 diabetes in obese patients. Diabetes Care 27:155-161. http://dx.doi.org/10.2337/diacare.27.1.155.
    • (2004) Diabetes Care , vol.27 , pp. 155-161
    • Torgerson, J.S.1    Hauptman, J.2    Boldrin, M.N.3    Sjöström, L.4
  • 5
    • 0024202729 scopus 로고
    • Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin
    • Hadváry P, Lengsfeld H, Wolfe H. 1988. Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin. Biochem. J. 256:357-361.
    • (1988) Biochem. J. , vol.256 , pp. 357-361
    • Hadváry, P.1    Lengsfeld, H.2    Wolfe, H.3
  • 6
    • 0023791240 scopus 로고
    • Mode of action of tetrahydrolipstatin: a derivative of the naturally occurring lipase inhibitor lipstatin
    • Borgström B. 1988. Mode of action of tetrahydrolipstatin: a derivative of the naturally occurring lipase inhibitor lipstatin. Biochim. Biophys. Acta 962:308-316. http://dx.doi.org/10.1016/0005-2760(88)90260-3.
    • (1988) Biochim. Biophys. Acta , vol.962 , pp. 308-316
    • Borgström, B.1
  • 7
    • 1542720382 scopus 로고    scopus 로고
    • Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity
    • Kridel SJ, Axelrod F, Rozenkrantz N, Smith JW. 2004. Orlistat is a novel inhibitor of fatty acid synthase with antitumor activity. Cancer Res. 64:2070-2075. http://dx.doi.org/10.1158/0008-5472.CAN-03-3645.
    • (2004) Cancer Res. , vol.64 , pp. 2070-2075
    • Kridel, S.J.1    Axelrod, F.2    Rozenkrantz, N.3    Smith, J.W.4
  • 8
    • 0023620073 scopus 로고
    • Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. II. Chemistry and structure elucidation
    • Hochuli E, Kupfer E, Maurer R, Meister W, Mercadal Y, Schmidt K. 1987. Lipstatin, an inhibitor of pancreatic lipase, produced by Streptomyces toxytricini. II. Chemistry and structure elucidation. J. Antibiot. (Tokyo) 40:1086-1091. http://dx.doi.org/10.7164/antibiotics.40.1086.
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 1086-1091
    • Hochuli, E.1    Kupfer, E.2    Maurer, R.3    Meister, W.4    Mercadal, Y.5    Schmidt, K.6
  • 9
    • 0023137327 scopus 로고
    • Syntheses of tetrahydrolipstatin and absolute configuration of tetrahydrolipstatin and lipstatin
    • Barbier P, Schneider F. 1987. Syntheses of tetrahydrolipstatin and absolute configuration of tetrahydrolipstatin and lipstatin. Helv. Chim. Acta 70:196-202. http://dx.doi.org/10.1002/hlca.19870700124.
    • (1987) Helv. Chim. Acta , vol.70 , pp. 196-202
    • Barbier, P.1    Schneider, F.2
  • 10
    • 0026757988 scopus 로고
    • Tetrahydrolipstatin: degradation products produced by human carboxyl-ester lipase
    • Stalder H, Oesterhelt G, Borgström B. 1992. Tetrahydrolipstatin: degradation products produced by human carboxyl-ester lipase. Helv. Chim. Acta 75:1593-1603. http://dx.doi.org/10.1002/hlca.19920750513.
    • (1992) Helv. Chim. Acta , vol.75 , pp. 1593-1603
    • Stalder, H.1    Oesterhelt, G.2    Borgström, B.3
  • 16
    • 0020399464 scopus 로고
    • Structural studies on ebelactone A and B, esterase inhibitors produced by actinomycetes
    • Uotani K, Naganawa H, Kondo S, Aoyagi T, Umezawa H. 1982. Structural studies on ebelactone A and B, esterase inhibitors produced by actinomycetes. J. Antibiot. (Tokyo) 35:1495-1499. http://dx.doi.org/10.7164/antibiotics.35.1495.
    • (1982) J. Antibiot. (Tokyo) , vol.35 , pp. 1495-1499
    • Uotani, K.1    Naganawa, H.2    Kondo, S.3    Aoyagi, T.4    Umezawa, H.5
  • 18
    • 0141677993 scopus 로고    scopus 로고
    • Biosynthetic origin of a branched chain analogue of the lipase inhibitor, lipstatin
    • Eisenreich W, Kupfer E, Stohler P, Weber W, Bacher A. 2003. Biosynthetic origin of a branched chain analogue of the lipase inhibitor, lipstatin. J. Med. Chem. 46:4209-4212. http://dx.doi.org/10.1021/jm030780x.
    • (2003) J. Med. Chem. , vol.46 , pp. 4209-4212
    • Eisenreich, W.1    Kupfer, E.2    Stohler, P.3    Weber, W.4    Bacher, A.5
  • 19
    • 0034647515 scopus 로고    scopus 로고
    • Biosynthetic origin of hydrogen atoms in the lipase inhibitor lipstatin
    • Goese M, Eisenreich W, Kupfer E, Stohler P, Weber W, Bacher A. 2000. Biosynthetic origin of hydrogen atoms in the lipase inhibitor lipstatin. J. Biol. Chem. 275:21192-21196. http://dx.doi.org/10.1074/jbc. M003094200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21192-21196
    • Goese, M.1    Eisenreich, W.2    Kupfer, E.3    Stohler, P.4    Weber, W.5    Bacher, A.6
  • 20
    • 0035967765 scopus 로고    scopus 로고
    • Biosynthesis of lipstatin. Incorporation of multiply deuterium-labeled (5Z,8Z)-tetradeca-5,8-dienoic acid and octanoic acid
    • Goese M, Eisenreich W, Kupfer E, Stohler P, Weber W, Leuenberger HG, Bacher A. 2001. Biosynthesis of lipstatin. Incorporation of multiply deuterium-labeled (5Z,8Z)-tetradeca-5,8-dienoic acid and octanoic acid. J. Org. Chem. 66:4673-4678. http://dx.doi.org/10.1021/jo010230b.
    • (2001) J. Org. Chem. , vol.66 , pp. 4673-4678
    • Goese, M.1    Eisenreich, W.2    Kupfer, E.3    Stohler, P.4    Weber, W.5    Leuenberger, H.G.6    Bacher, A.7
  • 22
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • Takayama K, Wang C, Besra GS. 2005. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. Clin. Microbiol. Rev. 18:81-101. http://dx.doi.org/10.1128/CMR.18.1.81-101.2005.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 81-101
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 23
    • 0347719360 scopus 로고    scopus 로고
    • A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms
    • Portevin D, De Sousa-D'Auria C, Houssin C, Grimaldi C, Chami M, Daffé M, Guilhot C. 2004. A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms. Proc. Natl. Acad. Sci. U. S. A. 101:314-319. http://dx.doi.org/10.1073/pnas.0305439101.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 314-319
    • Portevin, D.1    De Sousa-D'Auria, C.2    Houssin, C.3    Grimaldi, C.4    Chami, M.5    Daffé, M.6    Guilhot, C.7
  • 24
    • 0003869903 scopus 로고    scopus 로고
    • Practical Streptomyces genetics
    • John Innes Foundation, Norwich, United Kingdom
    • Kieser T, Bibb MJ, Buttner MJ, Chater KF, Hopwood DA. 2000. Practical Streptomyces genetics. John Innes Foundation, Norwich, United Kingdom.
    • (2000)
    • Kieser, T.1    Bibb, M.J.2    Buttner, M.J.3    Chater, K.F.4    Hopwood, D.A.5
  • 25
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • Gust B, Challis GL, Fowler K, Kieser T, Chater KF. 2003. PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc. Natl. Acad. Sci. U. S. A. 100:1541-1546. http://dx.doi.org/10.1073/pnas.0337542100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 26
    • 0031572413 scopus 로고    scopus 로고
    • High efficiency intergeneric conjugal transfer of plasmid DNA from Escherichia coli to methyl DNArestricting streptomycetes
    • Flett F, Mersinias V, Smith CP. 1997. High efficiency intergeneric conjugal transfer of plasmid DNA from Escherichia coli to methyl DNArestricting streptomycetes. FEMS Microbiol. Lett. 155:223-229. http://dx.doi.org/10.1111/j.1574-6968.1997.tb13882.x.
    • (1997) FEMS Microbiol. Lett. , vol.155 , pp. 223-229
    • Flett, F.1    Mersinias, V.2    Smith, C.P.3
  • 27
    • 49249106618 scopus 로고    scopus 로고
    • The mildiomycin biosynthesis: initial steps for sequential generation of 5-hydroxymethylcytidine 5'-monophosphate and 5-hydroxymethylcytosine in Streptoverticillium rimofaciens ZJU5119
    • Li L, Xu Z, Xu X, Wu J, Zhang Y, He X, Zabriskie TM, Deng Z. 2008. The mildiomycin biosynthesis: initial steps for sequential generation of 5-hydroxymethylcytidine 5'-monophosphate and 5-hydroxymethylcytosine in Streptoverticillium rimofaciens ZJU5119. Chembiochem 9:1286-1294. http://dx.doi.org/10.1002/cbic.200800008.
    • (2008) Chembiochem , vol.9 , pp. 1286-1294
    • Li, L.1    Xu, Z.2    Xu, X.3    Wu, J.4    Zhang, Y.5    He, X.6    Zabriskie, T.M.7    Deng, Z.8
  • 28
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman M, Logan R, O'Brien K, Seno ET, Rao RN, Schoner BE. 1992. Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116:43-49. http://dx.doi.org/10.1016/0378-1119(92)90627-2.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 29
    • 0003903343 scopus 로고
    • Molecular cloning: a laboratory manual
    • 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 30
    • 77955661836 scopus 로고    scopus 로고
    • The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini
    • Demirev AV, Khanal A, Sedai BR, Lim SK, Na MK, Nam DH. 2010. The role of acyl-coenzyme A carboxylase complex in lipstatin biosynthesis of Streptomyces toxytricini. Appl. Microbiol. Biotechnol. 87:1129-1139. http://dx.doi.org/10.1007/s00253-010-2587-2.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1129-1139
    • Demirev, A.V.1    Khanal, A.2    Sedai, B.R.3    Lim, S.K.4    Na, M.K.5    Nam, D.H.6
  • 31
    • 34147132825 scopus 로고    scopus 로고
    • Identifying bacterial genes and endosymbiont DNA with Glimmer
    • Delcher AL, Bratke KA, Powers EC, Salzberg SL. 2007. Identifying bacterial genes and endosymbiont DNA with Glimmer. Bioinformatics 23:673-679. http://dx.doi.org/10.1093/bioinformatics/btm009.
    • (2007) Bioinformatics , vol.23 , pp. 673-679
    • Delcher, A.L.1    Bratke, K.A.2    Powers, E.C.3    Salzberg, S.L.4
  • 35
    • 77955658204 scopus 로고    scopus 로고
    • Fermentation process for lipstatin and method of extracting lipstatin from a fermentation broth
    • Erdei J, Gulyas E, Balogh G, Toth L, Keri V, Csorvasi A. January 2005. Fermentation process for lipstatin and method of extracting lipstatin from a fermentation broth. US patent 6,844,174.
    • (2005)
    • Erdei, J.1    Gulyas, E.2    Balogh, G.3    Toth, L.4    Keri, V.5    Csorvasi January, A.6
  • 37
    • 64249084052 scopus 로고    scopus 로고
    • Methods for in silico prediction of microbial polyketide and nonribosomal peptide biosynthetic pathways from DNA sequence data
    • Bachmann BO, Ravel J. 2009. Methods for in silico prediction of microbial polyketide and nonribosomal peptide biosynthetic pathways from DNA sequence data. Methods Enzymol. 458:181-217. http://dx.doi.org/10.1016/S0076-6879(09)04808-3.
    • (2009) Methods Enzymol. , vol.458 , pp. 181-217
    • Bachmann, B.O.1    Ravel, J.2
  • 38
    • 79959936207 scopus 로고    scopus 로고
    • NRPSpredictor2-a Web server for predicting NRPS adenylation domain specificity
    • Röttig M, Medema MH, Blin K, Weber T, Rausch C, Kohlbacher O. 2011. NRPSpredictor2-a Web server for predicting NRPS adenylation domain specificity. Nucleic Acids Res. 39:W362-W367. http://dx.doi.org/10.1093/nar/gkr323.
    • (2011) Nucleic Acids Res. , vol.39 , pp. W362-W367
    • Röttig, M.1    Medema, M.H.2    Blin, K.3    Weber, T.4    Rausch, C.5    Kohlbacher, O.6
  • 39
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus T, Mootz HD, Marahiel MA. 1999. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol. 6:493-505. http://dx.doi.org/10.1016/S1074-5521(99)80082-9.
    • (1999) Chem. Biol. , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 40
    • 84859078407 scopus 로고    scopus 로고
    • The natural product domain seeker NaPDoS: a phylogeny based bioinformatic tool to classify secondary metabolite gene diversity
    • Ziemert N, Podell S, Penn K, Badger JH, Allen E, Jensen PR. 2012. The natural product domain seeker NaPDoS: a phylogeny based bioinformatic tool to classify secondary metabolite gene diversity. PLoS One 7:e34064. http://dx.doi.org/10.1371/journal.pone.0034064.
    • (2012) PLoS One , vol.7
    • Ziemert, N.1    Podell, S.2    Penn, K.3    Badger, J.H.4    Allen, E.5    Jensen, P.R.6
  • 41
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel MA, Stachelhaus T, Mootz HD. 1997. Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 97:2651-2674. http://dx.doi.org/10.1021/cr960029e.
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 42
    • 84858960389 scopus 로고    scopus 로고
    • Elucidating the biosynthetic pathway for the polyketide-nonribosomal peptide collismycin A: mechanism for formation of the 2,2'-bipyridyl ring
    • Garcia I, Vior NM, Braña AF, González-Sabin J, Rohr J, Moris F, Méndez C, Salas JA. 2012. Elucidating the biosynthetic pathway for the polyketide-nonribosomal peptide collismycin A: mechanism for formation of the 2,2'-bipyridyl ring. Chem. Biol. 19:399-413. http://dx.doi.org/10.1016/j.chembiol.2012.01.014.
    • (2012) Chem. Biol. , vol.19 , pp. 399-413
    • Garcia, I.1    Vior, N.M.2    Braña, A.F.3    González-Sabin, J.4    Rohr, J.5    Moris, F.6    Méndez, C.7    Salas, J.A.8
  • 43
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • Heath RJ, White SW, Rock CO. 2001. Lipid biosynthesis as a target for antibacterial agents. Prog. Lipid Res. 40:467-497. http://dx.doi.org/10.1016/S0163-7827(01)00012-1.
    • (2001) Prog. Lipid Res. , vol.40 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 44
    • 0035196229 scopus 로고    scopus 로고
    • Branched-chain fatty acid biosynthesis in Escherichia coli
    • Smirnova N, Reynolds KA. 2001. Branched-chain fatty acid biosynthesis in Escherichia coli. J. Ind. Microbiol. Biotechnol. 27:246-251. http://dx.doi.org/10.1038/sj.jim.7000185.
    • (2001) J. Ind. Microbiol. Biotechnol. , vol.27 , pp. 246-251
    • Smirnova, N.1    Reynolds, K.A.2
  • 45
    • 0036079707 scopus 로고    scopus 로고
    • Forty years of bacterial fatty acid synthesis
    • Rock CO, Jackowski S. 2002. Forty years of bacterial fatty acid synthesis. Biochem. Biophys. Res. Commun. 292:1155-1166. http://dx.doi.org/10.1006/bbrc.2001.2022.
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 1155-1166
    • Rock, C.O.1    Jackowski, S.2
  • 46
    • 0030885712 scopus 로고    scopus 로고
    • Fatty acid activation
    • Watkins PA. 1997. Fatty acid activation. Prog. Lipid Res. 36:55-83. http://dx.doi.org/10.1016/S0163-7827(97)00004-0.
    • (1997) Prog. Lipid Res. , vol.36 , pp. 55-83
    • Watkins, P.A.1
  • 47
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs)
    • Persson B, Kallberg Y, Oppermann U, Jörnvall H. 2003. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143-144:271-278. http://dx.doi.org/10.1016/S0009-2797(02)00223-5.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jörnvall, H.4
  • 48
    • 58149133711 scopus 로고    scopus 로고
    • Mediumand short-chain dehydrogenase/reductase gene and protein families: the SDR superfamily. Functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh KL, Jörnvall H, Persson B, Oppermann U. 2008. Mediumand 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. http://dx.doi.org/10.1007/s00018-008-8588-y.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jörnvall, H.2    Persson, B.3    Oppermann, U.4
  • 50
    • 20744455042 scopus 로고    scopus 로고
    • Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis
    • Williams GJ, Breazeale SD, Raetz CR, Naismith JH. 2005. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280:23000-23008. http://dx.doi.org/10.1074/jbc. M501534200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23000-23008
    • Williams, G.J.1    Breazeale, S.D.2    Raetz, C.R.3    Naismith, J.H.4
  • 52
    • 0001127245 scopus 로고
    • Ring-closure reactions. 11. The activation parameters for the formation of four-to six-membered lactones from ω-bromoalkanoate ions. The role of the entropy factor in small- and common-ring formation
    • Mandolini L. 1978. Ring-closure reactions. 11. The activation parameters for the formation of four-to six-membered lactones from ω-bromoalkanoate ions. The role of the entropy factor in small- and common-ring formation. J. Am. Chem. Soc. 100:550-554.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 550-554
    • Mandolini, L.1
  • 53
    • 34547731308 scopus 로고    scopus 로고
    • Rv1106c from Mycobacterium tuberculosis is a 3beta-hydroxysteroid dehydrogenase
    • Yang X, Dubnau E, Smith I, Sampson NS. 2007. Rv1106c from Mycobacterium tuberculosis is a 3beta-hydroxysteroid dehydrogenase. Biochemistry 46:9058-9067. http://dx.doi.org/10.1021/bi700688x.
    • (2007) Biochemistry , vol.46 , pp. 9058-9067
    • Yang, X.1    Dubnau, E.2    Smith, I.3    Sampson, N.S.4
  • 55
    • 84881014724 scopus 로고    scopus 로고
    • Biosynthesis of ebelactone A: isotopic tracer, advanced precursor and genetic studies reveal a thioesterase-independent cyclization to give a polyketide β-lactone
    • Wyatt MA, Ahilan Y, Argyropoulos P, Boddy CN, Magarvey NA, Harrison PH. 2013. Biosynthesis of ebelactone A: isotopic tracer, advanced precursor and genetic studies reveal a thioesterase-independent cyclization to give a polyketide β-lactone. J. Antibiot. (Tokyo) 66:421-430. http://dx.doi.org/10.1038/ja.2013.48.
    • (2013) J. Antibiot. (Tokyo) , vol.66 , pp. 421-430
    • Wyatt, M.A.1    Ahilan, Y.2    Argyropoulos, P.3    Boddy, C.N.4    Magarvey, N.A.5    Harrison, P.H.6


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