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Volumn 109, Issue 16, 2012, Pages 6024-6029

Biosynthetic pathway toward carbohydrate-like moieties of alnumycins contains unusual steps for C-C bond formation and cleavage

Author keywords

Biosynthesis; Natural product; Ribose 5 phosphate; Streptomyces

Indexed keywords

1,3 DIOXOLANE; ALNA PROTEIN; ALNB PROTEIN; ALNUMYCIN B; ALNUMYCIN C; ALNUMYCIN D; BICYCLO[3.3.0]2',4',6' TRIOXAOCTAN 3' BETA OL; CARBOHYDRATE; CARBON 13; DIOXANE; GLYCOSIDASE; HALOACID; POLYKETIDE; PSEUDOURIDINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RIBOSE 5 PHOSPHATE; UNCLASSIFIED DRUG;

EID: 84860012599     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201530109     Document Type: Article
Times cited : (30)

References (30)
  • 1
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • Weymouth-Wilson AC (1997) The role of carbohydrates in biologically active natural products. Nat Prod Rep 14:99-110.
    • (1997) Nat Prod Rep , vol.14 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 4
    • 0028206164 scopus 로고
    • Structure by NMR of antitumor drugs aclacinomycin A and aclacinomycin B complexed to D(CGTACG)
    • Yang DZ, Wang AHJ (1994) Structure by NMR of antitumor drugs aclacinomycin A and aclacinomycin B complexed to D(CGTACG). Biochemistry 33:6595-6604.
    • (1994) Biochemistry , vol.33 , pp. 6595-6604
    • Yang, D.Z.1    Wang, A.H.J.2
  • 6
    • 34247626294 scopus 로고    scopus 로고
    • Unusual sugar biosynthesis and natural product glycodiversification
    • DOI 10.1038/nature05814, PII NATURE05814
    • Thibodeaux CJ, Melancon CE, Liu HW (2007) Unusual sugar biosynthesis and natural product glycodiversification. Nature 446:1008-1016. (Pubitemid 46676062)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1008-1016
    • Thibodeaux, C.J.1    Melancon, C.E.2    Liu, H.-W.3
  • 7
    • 0034872489 scopus 로고    scopus 로고
    • Glycosides in Medicine: The role of glycosidic residue in biological activity
    • Kren V, Martínková L (2001) Glycosides in medicine: The role of glycosidic residue in biological activity. Curr Med Chem 8:1303-1328. (Pubitemid 32791798)
    • (2001) Current Medicinal Chemistry , vol.8 , Issue.11 , pp. 1303-1328
    • Kren, V.1    Martinkove, L.2
  • 8
    • 0029990425 scopus 로고    scopus 로고
    • Specificity of C-glycoside complexation by mannose/glucose specific lectins
    • DOI 10.1021/bi951916z
    • Weatherman RV, Mortell KH, Chervenak M, Kiessling LL, Toone EJ (1996) Specificity of C-glycoside complexation by mannose/glucose specific lectins. Biochemistry 35:3619-3624. (Pubitemid 26092582)
    • (1996) Biochemistry , vol.35 , Issue.11 , pp. 3619-3624
    • Weatherman, R.V.1    Mortell, K.H.2    Chervenak, M.3    Kiessling, L.L.4    Toone, E.J.5
  • 9
    • 29244446754 scopus 로고    scopus 로고
    • Structure, activity, synthesis and biosynthesis of aryl-C-glycosides
    • DOI 10.1039/b407364a
    • Bililign T, Griffith BR, Thorson JS (2005) Structure, activity, synthesis and biosynthesis of aryl-C-glycosides. Nat Prod Rep 22:742-760. (Pubitemid 41830840)
    • (2005) Natural Product Reports , vol.22 , Issue.6 , pp. 742-760
    • Bililign, T.1    Griffith, B.R.2    Thorson, J.S.3
  • 10
    • 29444453052 scopus 로고    scopus 로고
    • Bioactive C-glycosides from bacterial secondary metabolism
    • Hultin PG (2005) Bioactive C-glycosides from bacterial secondary metabolism. Curr Top Med Chem 5:1299-1331.
    • (2005) Curr Top Med Chem , vol.5 , pp. 1299-1331
    • Hultin, P.G.1
  • 11
    • 34547651180 scopus 로고    scopus 로고
    • Structure and Action of the C-C Bond-forming Glycosyltransferase UrdGT2 Involved in the Biosynthesis of the Antibiotic Urdamycin
    • DOI 10.1016/j.jmb.2007.06.005, PII S0022283607007875
    • Mittler M, Bechthold A, Schulz GE (2007) Structure and action of the C-C bond-forming glycosyltransferase UrdGT2 involved in the biosynthesis of the antibiotic urdamycin. J Mol Biol 372:67-76. (Pubitemid 47223216)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.1 , pp. 67-76
    • Mittler, M.1    Bechthold, A.2    Schulz, G.E.3
  • 12
    • 0031948321 scopus 로고    scopus 로고
    • Alnumycin a new naphthoquinone antibiotic produced by an endophytic Streptomyces sp. [1]
    • Bieber B, Nuske J, Ritzau M, Grafe U (1998) Alnumycin a new naphthoquinone antibiotic produced by an endophytic Streptomyces sp. J Antibiot 51:381-382. (Pubitemid 28174957)
    • (1998) Journal of Antibiotics , vol.51 , Issue.3 , pp. 381-382
    • Bieber, B.1    Nuske, J.2    Ritzau, M.3    Grafe, U.4
  • 13
    • 0031843807 scopus 로고    scopus 로고
    • K1115 A, a new anthraquinone that inhibits the binding of activator protein-1 (AP-1) to its recognition sites. II. Taxonomy, fermentation, isolation, physico-chemical properties and structure determination
    • Naruse N, Goto M, Watanabe Y, Terasawa T, Dobashi K (1998) K1115 A, a new anthraquinone that inhibits the binding of activator protein-1 (AP-1) to its recognition sites. II. Taxonomy, fermentation, isolation, physico-chemical properties and structure determination. J Antibiot 51:545-552. (Pubitemid 28336290)
    • (1998) Journal of Antibiotics , vol.51 , Issue.6 , pp. 545-552
    • Naruse, N.1    Goto, M.2    Watanabe, Y.3    Terasawa, T.4    Dobashi, K.5
  • 14
    • 53649108989 scopus 로고    scopus 로고
    • Characterization of the alnumycin gene cluster reveals unusual gene products for pyran ring formation and dioxan biosynthesis
    • Oja T, et al. (2008) Characterization of the alnumycin gene cluster reveals unusual gene products for pyran ring formation and dioxan biosynthesis. Chem Biol 15:1046-1057.
    • (2008) Chem Biol , vol.15 , pp. 1046-1057
    • Oja, T.1
  • 17
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: Evolution of a catalytic scaffold
    • DOI 10.1016/j.tibs.2004.07.008, PII S0968000404001793
    • Allen KN, Dunaway-Mariano D (2004) Phosphoryl group transfer: Evolution of a catalytic scaffold. Trends Biochem Sci 29:495-503. (Pubitemid 39158873)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.9 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 18
    • 33746922036 scopus 로고    scopus 로고
    • Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes
    • DOI 10.1016/j.jmb.2006.06.049, PII S0022283606007777
    • Burroughs AM, Allen KN, Dunaway-Mariano D, Aravind L (2006) Evolutionary genomics of the HAD superfamily: Understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes. J Mol Biol 361:1003-1034. (Pubitemid 44192587)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.5 , pp. 1003-1034
    • Burroughs, A.M.1    Allen, K.N.2    Dunaway-Mariano, D.3    Aravind, L.4
  • 19
    • 33748579951 scopus 로고    scopus 로고
    • Engineering of glycosidases and glycosyltransferases
    • DOI 10.1016/j.cbpa.2006.07.015, PII S1367593106001116, Analytical Techniques/Mechanisms
    • Hancock SM, Vaughan MD, Withers SG (2006) Engineering of glycosidases and glycosyltransferases. Curr Opin Chem Biol 10:509-519. (Pubitemid 44375059)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 509-519
    • Hancock, S.M.1    Vaughan, M.D.2    Withers, S.G.3
  • 20
    • 0025837029 scopus 로고
    • Organization and functions of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor
    • Caballero JL, Martinez E, Malpartida F, Hopwood DA (1991) Organization and functions of the actVA region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor. Mol Gen Genet 230:401-412.
    • (1991) Mol Gen Genet , vol.230 , pp. 401-412
    • Caballero, J.L.1    Martinez, E.2    Malpartida, F.3    Hopwood, D.A.4
  • 22
    • 77950626884 scopus 로고    scopus 로고
    • Cofactor-independent oxidases and oxygenases
    • Fetzner S, Steiner R (2010) Cofactor-independent oxidases and oxygenases. Appl Microbiol Biotechnol 86:791-804.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 791-804
    • Fetzner, S.1    Steiner, R.2
  • 23
    • 48349128546 scopus 로고    scopus 로고
    • Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: Mechanistic implications
    • Gabison L, et al. (2008) Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: Mechanistic implications. BMC Struct Biol 8:32-39.
    • (2008) BMC Struct Biol , vol.8 , pp. 32-39
    • Gabison, L.1
  • 24
    • 0036406502 scopus 로고    scopus 로고
    • Urate oxidase: Single-turnover stopped-flow techniques for detecting two discrete enzyme-bound intermediates
    • Tipton PA (2002) Urate oxidase: Single-turnover stopped-flow techniques for detecting two discrete enzyme-bound intermediates. Methods Enzymol 354:310-319.
    • (2002) Methods Enzymol , vol.354 , pp. 310-319
    • Tipton, P.A.1
  • 25
    • 0027337582 scopus 로고
    • 1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin
    • Hayes JD, Judah DJ, Neal GE (1993) Resistance to aflatoxin B1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin. Cancer Res 53:3887-3894. (Pubitemid 23267683)
    • (1993) Cancer Research , vol.53 , Issue.17 , pp. 3887-3894
    • Hayes, J.D.1    Judah, D.J.2    Neal, G.E.3
  • 26
    • 77958550609 scopus 로고    scopus 로고
    • Identification and characterization of two families of F420 H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation
    • Taylor MC, et al. (2010) Identification and characterization of two families of F420 H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation. Mol Microbiol 78:561-575.
    • (2010) Mol Microbiol , vol.78 , pp. 561-575
    • Taylor, M.C.1
  • 27
    • 84155192367 scopus 로고    scopus 로고
    • Identification of late-stage glycosylation steps in the biosynthetic pathway of the anthracycline nogalamycin
    • Siitonen V, et al. (2012) Identification of late-stage glycosylation steps in the biosynthetic pathway of the anthracycline nogalamycin. ChemBioChem 13:120-128.
    • (2012) ChemBioChem , vol.13 , pp. 120-128
    • Siitonen, V.1
  • 29
    • 0018840878 scopus 로고
    • Streptomyces albus G mutants defective in the SalGI restriction- modification system
    • Chater KF, Wilde LC (1980) Streptomyces albus G mutants defective in the SalGI restriction- modification system. J Gen Microbiol 116:323-334. (Pubitemid 10145310)
    • (1980) Journal of General Microbiology , vol.116 , Issue.2 , pp. 323-334
    • Chater, K.F.1    Wilde, L.C.2
  • 30
    • 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, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.