메뉴 건너뛰기




Volumn 48, Issue 2, 2013, Pages 98-122

Structural analysis of protein-protein interactions in type i polyketide synthases

Author keywords

Antibiotics; Biosynthesis; Fatty acid synthase; Macromolecular docking; Mutagenesis; Natural products; Protein NMR; X ray crystallography

Indexed keywords

ACYL CARRIER PROTEIN; ACYLTRANSFERASE; ENOYLREDUCTASE; FATTY ACID SYNTHASE; KETOREDUCTASE; KETOSYNTHASE; OXIDOREDUCTASE; POLYKETIDE SYNTHASE; SYNTHETASE; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

EID: 84875629932     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2012.745476     Document Type: Review
Times cited : (36)

References (165)
  • 1
    • 0029092263 scopus 로고
    • The thioesterase of the erythromycin-producing polyketide synthase - Mechanistic studies invitro to investigate its mode of action and substrate-specificity
    • Aggarwal R, Caffrey P, Leadlay PF, et al. (1995). The thioesterase of the erythromycin-producing polyketide synthase - mechanistic studies invitro to investigate its mode of action and substrate-specificity. J Chem Soc, Chem Commun 1519-20
    • (1995) J Chem Soc, Chem Commun , pp. 1519-1520
    • Aggarwal, R.1    Caffrey, P.2    Leadlay, P.F.3
  • 2
    • 33748792266 scopus 로고    scopus 로고
    • Structural basis for macrolactonization by the pikromycin thioesterase
    • Akey DL, Kittendorf JD, Giraldes JW, et al. (2006). Structural basis for macrolactonization by the pikromycin thioesterase. Nat Chem Biol 2:537-42
    • (2006) Nat Chem Biol , vol.2 , pp. 537-542
    • Akey, D.L.1    Kittendorf, J.D.2    Giraldes, J.W.3
  • 3
    • 73449104701 scopus 로고    scopus 로고
    • Crystal structures of dehydratase domains from the curacin polyketide biosynthetic pathway
    • Akey DL, Razelun JR, Tehranisa J, et al. (2010). Crystal structures of dehydratase domains from the curacin polyketide biosynthetic pathway. Structure 18:94-105
    • (2010) Structure , vol.18 , pp. 94-105
    • Akey, D.L.1    Razelun, J.R.2    Tehranisa, J.3
  • 4
    • 34547933299 scopus 로고    scopus 로고
    • Solution structure and proposed domain domain recognition interface of an acyl carrier protein domain from a modular polyketide synthase
    • Alekseyev VY, Liu CW, Cane DE, et al. (2007). Solution structure and proposed domain domain recognition interface of an acyl carrier protein domain from a modular polyketide synthase. Protein Sci 16:2093-107
    • (2007) Protein Sci , vol.16 , pp. 2093-2107
    • Alekseyev, V.Y.1    Liu, C.W.2    Cane, D.E.3
  • 5
    • 84863966874 scopus 로고    scopus 로고
    • Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis
    • Ames BD, Nguyen C, Bruegger J, et al. (2012). Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis. Proc Nat Acad Sci USA 109:11144-9
    • (2012) Proc Nat Acad Sci USA , vol.109 , pp. 11144-11149
    • Ames, B.D.1    Nguyen, C.2    Bruegger, J.3
  • 6
    • 84861450800 scopus 로고    scopus 로고
    • Modeling holo-ACP:DH and holo- ACP:KR complexes of modular polyketide synthases: A docking and molecular dynamics study
    • Anand S, Mohanty D. (2012). Modeling holo-ACP:DH and holo- ACP:KR complexes of modular polyketide synthases: a docking and molecular dynamics study. BMC Struct Biol 12:10
    • (2012) BMC Struct Biol , vol.12 , pp. 10
    • Anand, S.1    Mohanty, D.2
  • 7
    • 17844385334 scopus 로고    scopus 로고
    • Structure and molecular organization of mammalian fatty acid synthase
    • Asturias FJ, Chadick JZ, Cheung IK, et al. (2005). Structure and molecular organization of mammalian fatty acid synthase. Nat Struct Mol Biol 12:225-32
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 225-232
    • Asturias, F.J.1    Chadick, J.Z.2    Cheung, I.K.3
  • 8
    • 0034703754 scopus 로고    scopus 로고
    • Lovastatin nonaketide synthase catalyzes an intramolecular Diels-Alder reaction of a substrate analogue
    • Auclair K, Sutherland A, Kennedy J, et al. (2000). Lovastatin nonaketide synthase catalyzes an intramolecular Diels-Alder reaction of a substrate analogue. J Am Chem Soc 122:11519-20
    • (2000) J Am Chem Soc , vol.122 , pp. 11519-11520
    • Auclair, K.1    Sutherland, A.2    Kennedy, J.3
  • 9
    • 0030267847 scopus 로고    scopus 로고
    • A functional chimeric modular polyketide synthase generated via domain replacement
    • Bedford D, Jacobsen JR, Luo G, et al. (1996). A functional chimeric modular polyketide synthase generated via domain replacement. Chem Biol 3:827-31
    • (1996) Chem Biol , vol.3 , pp. 827-831
    • Bedford, D.1    Jacobsen, J.R.2    Luo, G.3
  • 10
    • 59649102440 scopus 로고    scopus 로고
    • Conformational flexibility of metazoan fatty acid synthase enables catalysis
    • Brignole EJ, Smith S, Asturias FJ. (2009). Conformational flexibility of metazoan fatty acid synthase enables catalysis. Nat Struct Mol Biol 16:190-7
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 190-197
    • Brignole, E.J.1    Smith, S.2    Asturias, F.J.3
  • 11
    • 0041412707 scopus 로고    scopus 로고
    • The structure of docking domains in modular polyketide synthases
    • Broadhurst RW, Nietlispach D, Wheatcroft MP, et al. (2003). The structure of docking domains in modular polyketide synthases. Chem Biol 10:723-31
    • (2003) Chem Biol , vol.10 , pp. 723-731
    • Broadhurst, R.W.1    Nietlispach, D.2    Wheatcroft, M.P.3
  • 12
    • 70349907839 scopus 로고    scopus 로고
    • Segmental isotopic labeling of a central domain in a multidomain protein by protein trans-splicing using only one robust DnaE intein
    • Busche AE, Aranko AS, Talebzadeh-Farooji M, et al. (2009). Segmental isotopic labeling of a central domain in a multidomain protein by protein trans-splicing using only one robust DnaE intein. Angew Chem Int Ed Engl 48:6128-31
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 6128-6131
    • Busche, A.E.1    Aranko, A.S.2    Talebzadeh-Farooji, M.3
  • 13
    • 84857511627 scopus 로고    scopus 로고
    • Characterization of molecular interactions between ACP and halogenase domains in the curacin A polyketide synthase
    • Busche AE, Gottstein D, Hein C, et al. (2012). Characterization of molecular interactions between ACP and halogenase domains in the curacin A polyketide synthase. ACS Chem Biol 7:378-86
    • (2012) ACS Chem Biol , vol.7 , pp. 378-386
    • Busche, A.E.1    Gottstein, D.2    Hein, C.3
  • 14
    • 77956261727 scopus 로고    scopus 로고
    • Programming of erythromycin biosynthesis by a modular polyketide synthase
    • Cane DE. (2010). Programming of erythromycin biosynthesis by a modular polyketide synthase. J Biol Chem 285:27517-23
    • (2010) J Biol Chem , vol.285 , pp. 27517-27523
    • Cane, D.E.1
  • 15
    • 0033485280 scopus 로고    scopus 로고
    • The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases
    • Cane DE, Walsh CT. (1999). The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases. Chem Biol 6:R319-25
    • (1999) Chem Biol , vol.6
    • Cane, D.E.1    Walsh, C.T.2
  • 16
    • 84860128454 scopus 로고    scopus 로고
    • Acyl carrier protein structural classification and normal mode analysis
    • Cantu DC, Forrester MJ, Charov K, et al. (2012). Acyl carrier protein structural classification and normal mode analysis. Protein Sci 21:655-66
    • (2012) Protein Sci , vol.21 , pp. 655-666
    • Cantu, D.C.1    Forrester, M.J.2    Charov, K.3
  • 17
    • 8144227950 scopus 로고    scopus 로고
    • Human fatty acid synthase: Structure and substrate selectivity of the thioesterase domain
    • Chakravarty B, Gu Z, Chirala SS, et al. (2004). Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. Proc Nat Acad Sci USA 101:15567-72
    • (2004) Proc Nat Acad Sci USA , vol.101 , pp. 15567-15572
    • Chakravarty, B.1    Gu, Z.2    Chirala, S.S.3
  • 18
    • 58149095417 scopus 로고    scopus 로고
    • Biosynthesis of polyketide synthase extender units
    • Chan YA, Podevels AM, Kevany BM, et al. (2009). Biosynthesis of polyketide synthase extender units. Nat Prod Rep 26:90-114
    • (2009) Nat Prod Rep , vol.26 , pp. 90-114
    • Chan, Y.A.1    Podevels, A.M.2    Kevany, B.M.3
  • 19
    • 79959331623 scopus 로고    scopus 로고
    • Probing the interactions of an acyl carrier protein domain from the 6-deoxyerythronolide B synthase
    • Charkoudian LK, Liu CW, Capone S, et al. (2011). Probing the interactions of an acyl carrier protein domain from the 6-deoxyerythronolide B synthase. Protein Sci 20:1244-55
    • (2011) Protein Sci , vol.20 , pp. 1244-1255
    • Charkoudian, L.K.1    Liu, C.W.2    Capone, S.3
  • 20
    • 34447547495 scopus 로고    scopus 로고
    • Structure-based dissociation of a type i polyketide synthase module
    • Chen AY, Cane DE, Khosla C. (2007). Structure-based dissociation of a type I polyketide synthase module. Chem Biol 14:784-92
    • (2007) Chem Biol , vol.14 , pp. 784-792
    • Chen, A.Y.1    Cane, D.E.2    Khosla, C.3
  • 21
    • 33644950516 scopus 로고    scopus 로고
    • Extender unit and acyl carrier protein specificity of ketosynthase domains of the 6-deoxyerythronolide B synthase
    • Chen AY, Schnarr NA, Kim CY, et al. (2006). Extender unit and acyl carrier protein specificity of ketosynthase domains of the 6-deoxyerythronolide B synthase. J Am Chem Soc 128:3067-74
    • (2006) J Am Chem Soc , vol.128 , pp. 3067-3074
    • Chen, A.Y.1    Schnarr, N.A.2    Kim, C.Y.3
  • 22
    • 0037452928 scopus 로고    scopus 로고
    • Type i polyketide synthase requiring a discrete acyltransferase for polyketide biosynthesis
    • Cheng YQ, Tang GL, Shen B. (2003). Type I polyketide synthase requiring a discrete acyltransferase for polyketide biosynthesis. Proc Nat Acad Sci USA 100:3149-54
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 3149-3154
    • Cheng, Y.Q.1    Tang, G.L.2    Shen, B.3
  • 23
    • 64149117037 scopus 로고    scopus 로고
    • Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway
    • Claxton HB, Akey DL, Silver MK, et al. (2009). Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway. J Biol Chem 284:5021-9
    • (2009) J Biol Chem , vol.284 , pp. 5021-5029
    • Claxton, H.B.1    Akey, D.L.2    Silver, M.K.3
  • 24
    • 34250790717 scopus 로고    scopus 로고
    • Polyketides, proteins and genes in fungi: Programmed nano-machines begin to reveal their secrets
    • Cox RJ. (2007). Polyketides, proteins and genes in fungi: programmed nano-machines begin to reveal their secrets. Org Biomol Chem 5:2010-26
    • (2007) Org Biomol Chem , vol.5 , pp. 2010-2026
    • Cox, R.J.1
  • 25
    • 70350496678 scopus 로고    scopus 로고
    • Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization
    • Crawford JM, Korman TP, Labonte JW, et al. (2009). Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461:1139-43
    • (2009) Nature , vol.461 , pp. 1139-1143
    • Crawford, J.M.1    Korman, T.P.2    Labonte, J.W.3
  • 26
    • 42049099494 scopus 로고    scopus 로고
    • Deconstruction of iterative multidomain polyketide synthase function
    • Crawford JM, Thomas PM, Scheerer JR, et al. (2008). Deconstruction of iterative multidomain polyketide synthase function. Science 320:243-6
    • (2008) Science , vol.320 , pp. 243-246
    • Crawford, J.M.1    Thomas, P.M.2    Scheerer, J.R.3
  • 27
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)
    • Crump MP, Crosby J, Dempsey CE, et al. (1997). Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry 36:6000-8
    • (1997) Biochemistry , vol.36 , pp. 6000-6008
    • Crump, M.P.1    Crosby, J.2    Dempsey, C.E.3
  • 28
    • 13244267005 scopus 로고    scopus 로고
    • The hotdog fold: Wrapping up a superfamily of thioesterases and dehydratases
    • Dillon SC, Bateman A. (2004). The hotdog fold: wrapping up a superfamily of thioesterases and dehydratases. BMC Bioinform 5:109.
    • (2004) BMC Bioinform , vol.5 , pp. 109
    • Dillon, S.C.1    Bateman, A.2
  • 29
    • 76249090018 scopus 로고    scopus 로고
    • PKS and NRPS release mechanisms
    • Du L, Lou L. (2010). PKS and NRPS release mechanisms. Nat Prod Rep 27:255-78
    • (2010) Nat Prod Rep , vol.27 , pp. 255-278
    • Du, L.1    Lou, L.2
  • 30
    • 54349095025 scopus 로고    scopus 로고
    • An ACP structural switch: Conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein
    • Evans SE, Williams C, Arthur CJ, et al. (2008). An ACP structural switch: conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein. ChemBioChem 9:2424-32
    • (2008) ChemBioChem , vol.9 , pp. 2424-2432
    • Evans, S.E.1    Williams, C.2    Arthur, C.J.3
  • 31
    • 65649101867 scopus 로고    scopus 로고
    • Probing the Interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2)
    • Evans SE, Williams C, Arthur CJ, et al. (2009). Probing the Interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2). J Mol Biol 389:511-28
    • (2009) J Mol Biol , vol.389 , pp. 511-528
    • Evans, S.E.1    Williams, C.2    Arthur, C.J.3
  • 32
    • 0038457084 scopus 로고    scopus 로고
    • Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus
    • Findlow SC, Winsor C, Simpson TJ, et al. (2003). Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus. Biochemistry 42:8423-33
    • (2003) Biochemistry , vol.42 , pp. 8423-8433
    • Findlow, S.C.1    Winsor, C.2    Simpson, T.J.3
  • 33
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: Logic, machinery, and mechanisms
    • Fischbach MA, Walsh CT. (2006). Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms. Chem Rev 106:3468-96
    • (2006) Chem Rev , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 34
    • 49649129083 scopus 로고    scopus 로고
    • Dynamic thiolation- thioesterase structure of a non-ribosomal peptide synthetase
    • Frueh DP, Arthanari H, Koglin A, et al. (2008). Dynamic thiolation- thioesterase structure of a non-ribosomal peptide synthetase. Nature 454:903-6
    • (2008) Nature , vol.454 , pp. 903-906
    • Frueh, D.P.1    Arthanari, H.2    Koglin, A.3
  • 35
    • 0035068075 scopus 로고    scopus 로고
    • Identification of Claisen cyclase domain in fungal polyketide synthase WA, a naphthopyrone synthase of Aspergillus nidulans
    • Fujii I, Watanabe A, Sankawa U, et al. (2001). Identification of Claisen cyclase domain in fungal polyketide synthase WA, a naphthopyrone synthase of Aspergillus nidulans. Chem Biol 8:189-97
    • (2001) Chem Biol , vol.8 , pp. 189-197
    • Fujii, I.1    Watanabe, A.2    Sankawa, U.3
  • 36
    • 79954598176 scopus 로고    scopus 로고
    • Terminal alkene formation by the thioesterase of curacin A biosynthesis: Structure of a decarboxylating thioesterase
    • Gehret JJ, Gu L, Gerwick WH, et al. (2011). Terminal alkene formation by the thioesterase of curacin A biosynthesis: structure of a decarboxylating thioesterase. J Biol Chem 286:14445-54
    • (2011) J Biol Chem , vol.286 , pp. 14445-14454
    • Gehret, J.J.1    Gu, L.2    Gerwick, W.H.3
  • 37
    • 33748785161 scopus 로고    scopus 로고
    • Structural and mechanistic insights into polyketide macrolactonization from polyketide- based affinity labels
    • Giraldes JW, Akey DL, Kittendorf JD, et al. (2006). Structural and mechanistic insights into polyketide macrolactonization from polyketide- based affinity labels. Nat Chem Biol 2:531-6
    • (2006) Nat Chem Biol , vol.2 , pp. 531-536
    • Giraldes, J.W.1    Akey, D.L.2    Kittendorf, J.D.3
  • 38
    • 0033574768 scopus 로고    scopus 로고
    • Dissecting and exploiting intermodular communication in polyketide synthases
    • Gokhale RS, Tsuji SY, Cane DE, et al. (1999). Dissecting and exploiting intermodular communication in polyketide synthases. Science 284:482-5
    • (1999) Science , vol.284 , pp. 482-485
    • Gokhale, R.S.1    Tsuji, S.Y.2    Cane, D.E.3
  • 39
    • 77958461812 scopus 로고    scopus 로고
    • Mechanism and stereospecificity of a fully saturating polyketide synthase module: Nanchangmycin synthase module 2 and its dehydratase domain
    • Guo X, Liu T, Valenzano CR, et al. (2010). Mechanism and stereospecificity of a fully saturating polyketide synthase module: nanchangmycin synthase module 2 and its dehydratase domain. J Am Chem Soc 132:14694-6
    • (2010) J Am Chem Soc , vol.132 , pp. 14694-14696
    • Guo, X.1    Liu, T.2    Valenzano, C.R.3
  • 40
    • 79957506998 scopus 로고    scopus 로고
    • Binding and pK(a) modulation of a polycyclic substrate analogue in a type II polyketide acyl carrier protein
    • Haushalter RW, Filipp FV, Ko KS, et al. (2011). Binding and pK(a) modulation of a polycyclic substrate analogue in a type II polyketide acyl carrier protein. ACS Chem Biol 6:413-18
    • ACS Chem Biol , vol.6 , pp. 413-418
    • Haushalter, R.W.1    Filipp, F.V.2    Ko, K.S.3
  • 41
    • 43549087362 scopus 로고    scopus 로고
    • An orthogonal purification strategy for isolating crosslinked domains of modular synthases
    • Haushalter RW, Worthington AS, Hur GH, et al. (2008). An orthogonal purification strategy for isolating crosslinked domains of modular synthases. Bioorg Med Chem Lett 18:3039-42
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 3039-3042
    • Haushalter, R.W.1    Worthington, A.S.2    Hur, G.H.3
  • 42
    • 0028841535 scopus 로고
    • Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl- CoA:acyl carrier protein transacylase domains in modular polyketide synthases
    • Haydock SF, Aparicio JF, Molnar I, et al. (1995). Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl- CoA:acyl carrier protein transacylase domains in modular polyketide synthases. FEBS Lett 374:246-8
    • (1995) FEBS Lett , vol.374 , pp. 246-248
    • Haydock, S.F.1    Aparicio, J.F.2    Molnar, I.3
  • 43
    • 69249202590 scopus 로고    scopus 로고
    • The biosynthetic logic of polyketide diversity
    • Hertweck C. (2009). The biosynthetic logic of polyketide diversity. Angew Chem Int Ed Engl 48:4688-716
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 4688-4716
    • Hertweck, C.1
  • 44
    • 24744433982 scopus 로고    scopus 로고
    • Evolutionary implications of bacterial polyketide synthases
    • Jenke-Kodama H, Sandmann A, Muller R, et al. (2005). Evolutionary implications of bacterial polyketide synthases. Mol Biol Evol 22:2027-39
    • (2005) Mol Biol Evol , vol.22 , pp. 2027-2039
    • Jenke-Kodama, H.1    Sandmann, A.2    Muller, R.3
  • 45
    • 0032570557 scopus 로고    scopus 로고
    • Differential affinity labeling of the two subunits of the homodimeric animal fatty acid synthase allows isolation of heterodimers consisting of subunits that have been independently modified
    • Joshi AK, Rangan VS, Smith S. (1998a). Differential affinity labeling of the two subunits of the homodimeric animal fatty acid synthase allows isolation of heterodimers consisting of subunits that have been independently modified. J Biol Chem 273:4937-43
    • (1998) J Biol Chem , vol.273 , pp. 4937-4943
    • Joshi, A.K.1    Rangan, V.S.2    Smith, S.3
  • 46
    • 0037330531 scopus 로고    scopus 로고
    • Engineering of an active animal fatty acid synthase dimer with only one competent subunit
    • Joshi AK, Rangan VS, Witkowski A, et al. (2003). Engineering of an active animal fatty acid synthase dimer with only one competent subunit. Chem Biol 10:169-73
    • (2003) Chem Biol , vol.10 , pp. 169-173
    • Joshi, A.K.1    Rangan, V.S.2    Witkowski, A.3
  • 47
    • 0031050460 scopus 로고    scopus 로고
    • Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro
    • Joshi AK, Witkowski A, Smith S. (1997). Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 36:2316-22
    • (1997) Biochemistry , vol.36 , pp. 2316-2322
    • Joshi, A.K.1    Witkowski, A.2    Smith, S.3
  • 48
    • 0032562216 scopus 로고    scopus 로고
    • The malonyl/acetyltransferase and beta-ketoacyl synthase domains of the animal fatty acid synthase can cooperate with the acyl carrier protein domain of either subunit
    • Joshi AK, Witkowski A, Smith S. (1998b). The malonyl/acetyltransferase and beta-ketoacyl synthase domains of the animal fatty acid synthase can cooperate with the acyl carrier protein domain of either subunit. Biochemistry 37:2515-23
    • (1998) Biochemistry , vol.37 , pp. 2515-2523
    • Joshi, A.K.1    Witkowski, A.2    Smith, S.3
  • 49
    • 78650660868 scopus 로고    scopus 로고
    • Molecular recognition between ketosynthase and acyl carrier protein domains of the 6-deoxyerythronolide B synthase
    • Kapur S, Chen AY, Cane DE, et al. (2010). Molecular recognition between ketosynthase and acyl carrier protein domains of the 6-deoxyerythronolide B synthase. Proc Nat Acad Sci USA 107:22066-71
    • (2010) Proc Nat Acad Sci USA , vol.107 , pp. 22066-22071
    • Kapur, S.1    Chen, A.Y.2    Cane, D.E.3
  • 50
    • 84858184688 scopus 로고    scopus 로고
    • Reprogramming a module of the 6-deoxyerythronolide B synthase for iterative chain elongation
    • Kapur S, Lowry B, Yuzawa S, et al. (2012). Reprogramming a module of the 6-deoxyerythronolide B synthase for iterative chain elongation. Proc Nat Acad Sci USA 109:4110-5
    • (2012) Proc Nat Acad Sci USA , vol.109 , pp. 4110-4115
    • Kapur, S.1    Lowry, B.2    Yuzawa, S.3
  • 51
    • 43549100873 scopus 로고    scopus 로고
    • Mechanism based protein crosslinking of domains from the 6-deoxyerythronolide B synthase
    • Kapur S, Worthington A, Tang Y, et al. (2008). Mechanism based protein crosslinking of domains from the 6-deoxyerythronolide B synthase. Bioorg Med Chem Lett 18:3034-8
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 3034-3038
    • Kapur, S.1    Worthington, A.2    Tang, Y.3
  • 52
    • 58149133711 scopus 로고    scopus 로고
    • The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh K, Jornvall H, Persson B, et al. (2008). The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell Mol Life Sci 65:3895-906
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3895-3906
    • Kavanagh, K.1    Jornvall, H.2    Persson, B.3
  • 53
    • 34547945950 scopus 로고    scopus 로고
    • A tylosin ketoreductase reveals how chirality is determined in polyketides
    • Keatinge-Clay AT. (2007). A tylosin ketoreductase reveals how chirality is determined in polyketides. Chem Biol 14:898-908
    • (2007) Chem Biol , vol.14 , pp. 898-908
    • Keatinge-Clay, A.T.1
  • 54
    • 56249096167 scopus 로고    scopus 로고
    • Crystal structure of the erythromycin polyketide synthase dehydratase
    • Keatinge-Clay AT. (2008). Crystal structure of the erythromycin polyketide synthase dehydratase. J Mol Biol 384:941-53
    • (2008) J Mol Biol , vol.384 , pp. 941-953
    • Keatinge-Clay, A.T.1
  • 55
    • 84871840984 scopus 로고    scopus 로고
    • The structures of type i polyketide synthases
    • Keatinge-Clay AT. (2012). The structures of type I polyketide synthases. Nat Prod Rep 29:1050-73
    • (2012) Nat Prod Rep , vol.29 , pp. 1050-1073
    • Keatinge-Clay, A.T.1
  • 57
    • 0037314870 scopus 로고    scopus 로고
    • Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl- CoA:ACP transacylase
    • Keatinge-Clay AT, Shelat AA, Savage DF, et al. (2003). Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl- CoA:ACP transacylase. Structure 11:147-54
    • (2003) Structure , vol.11 , pp. 147-154
    • Keatinge-Clay, A.T.1    Shelat, A.A.2    Savage, D.F.3
  • 58
    • 33645962845 scopus 로고    scopus 로고
    • The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases
    • Keatinge-Clay AT, Stroud RM. (2006). The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases. Structure 14:737-48
    • (2006) Structure , vol.14 , pp. 737-748
    • Keatinge-Clay, A.T.1    Stroud, R.M.2
  • 59
    • 0033591447 scopus 로고    scopus 로고
    • Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
    • Kennedy J, Auclair K, Kendrew SG, et al. (1999). Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284:1368-72
    • (1999) Science , vol.284 , pp. 1368-1372
    • Kennedy, J.1    Auclair, K.2    Kendrew, S.G.3
  • 60
    • 77956289715 scopus 로고    scopus 로고
    • Conformational switch triggered by alpha-ketoglutarate in a halogenase of curacin A biosynthesis
    • Khare D, Wang B, Gu LC, et al. (2010). Conformational switch triggered by alpha-ketoglutarate in a halogenase of curacin A biosynthesis. Proc Nat Acad Sci USA 107:14099-104
    • (2010) Proc Nat Acad Sci USA , vol.107 , pp. 14099-14104
    • Khare, D.1    Wang, B.2    Gu, L.C.3
  • 61
    • 69549096251 scopus 로고    scopus 로고
    • Structures and mechanisms of polyketide synthases
    • Khosla C. (2009). Structures and mechanisms of polyketide synthases. J Org Chem 74:6416-20
    • (2009) J Org Chem , vol.74 , pp. 6416-6420
    • Khosla, C.1
  • 62
    • 0032860405 scopus 로고    scopus 로고
    • Tolerance and specificity of polyketide synthases
    • Khosla C, Gokhale RS, Jacobsen JR, et al. (1999). Tolerance and specificity of polyketide synthases. Annu Rev Biochem 68:219-53
    • (1999) Annu Rev Biochem , vol.68 , pp. 219-253
    • Khosla, C.1    Gokhale, R.S.2    Jacobsen, J.R.3
  • 63
    • 34547930907 scopus 로고    scopus 로고
    • Structure and mechanism of the 6-deoxyerythronolide B synthase
    • Khosla C, Tang Y, Chen AY, et al. (2007). Structure and mechanism of the 6-deoxyerythronolide B synthase. Annu Rev Biochem 76:195-221
    • (2007) Annu Rev Biochem , vol.76 , pp. 195-221
    • Khosla, C.1    Tang, Y.2    Chen, A.Y.3
  • 64
    • 10644295401 scopus 로고    scopus 로고
    • The structure of (3R)- hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa
    • Kimber MS, Martin F, Lu Y, et al. (2004). The structure of (3R)- hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa. J Biol Chem 279:52593-602
    • (2004) J Biol Chem , vol.279 , pp. 52593-52602
    • Kimber, M.S.1    Martin, F.2    Lu, Y.3
  • 65
    • 49649122848 scopus 로고    scopus 로고
    • Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
    • Koglin A, Lohr F, Bernhard F, et al. (2008). Structural basis for the selectivity of the external thioesterase of the surfactin synthetase. Nature 454:907-11
    • (2008) Nature , vol.454 , pp. 907-911
    • Koglin, A.1    Lohr, F.2    Bernhard, F.3
  • 66
    • 22144451059 scopus 로고    scopus 로고
    • Production of the tubulin destabilizer disorazol in Sorangium cellulosum: Biosynthetic machinery and regulatory genes
    • Kopp M, Irschik H, Pradella S, et al. (2005). Production of the tubulin destabilizer disorazol in Sorangium cellulosum: biosynthetic machinery and regulatory genes. ChemBioChem 6:1277-86
    • (2005) ChemBioChem , vol.6 , pp. 1277-1286
    • Kopp, M.1    Irschik, H.2    Pradella, S.3
  • 67
    • 77950901720 scopus 로고    scopus 로고
    • Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis
    • Korman TP, Crawford JM, Labonte JW, et al. (2010). Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc Nat Acad Sci USA 107:6246-51
    • (2010) Proc Nat Acad Sci USA , vol.107 , pp. 6246-6251
    • Korman, T.P.1    Crawford, J.M.2    Labonte, J.W.3
  • 68
    • 67650138601 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the thioesterase CalE7 in enediyne biosynthesis
    • Kotaka M, Kong R, Qureshi I, et al. (2009). Structure and catalytic mechanism of the thioesterase CalE7 in enediyne biosynthesis. J Biol Chem 284:15739-49
    • (2009) J Biol Chem , vol.284 , pp. 15739-15749
    • Kotaka, M.1    Kong, R.2    Qureshi, I.3
  • 69
    • 0347994901 scopus 로고    scopus 로고
    • Phylogenomic analysis of type i polyketide synthase genes in pathogenic and saprobic ascomycetes
    • Kroken S, Glass NL, Taylor JW, et al. (2003). Phylogenomic analysis of type I polyketide synthase genes in pathogenic and saprobic ascomycetes. Proc Nat Acad Sci USA 100:15670-5
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 15670-15675
    • Kroken, S.1    Glass, N.L.2    Taylor, J.W.3
  • 70
    • 0344875194 scopus 로고    scopus 로고
    • Enhancing the modularity of the modular polyketide synthases: Transacylation in modular polyketide synthases catalyzed by malonyl-CoA:ACP transacylase
    • Kumar P, Koppisch AT, Cane DE, et al. (2003). Enhancing the modularity of the modular polyketide synthases: transacylation in modular polyketide synthases catalyzed by malonyl-CoA:ACP transacylase. J Am Chem Soc 125:14307-12
    • (2003) J Am Chem Soc , vol.125 , pp. 14307-14312
    • Kumar, P.1    Koppisch, A.T.2    Cane, D.E.3
  • 71
    • 77956942908 scopus 로고    scopus 로고
    • Mutagenesis of a modular polyketide synthase enoylreductase domain reveals insights into catalysis and stereospecificity
    • Kwan DH, Leadlay PF. (2010). Mutagenesis of a modular polyketide synthase enoylreductase domain reveals insights into catalysis and stereospecificity. ACS Chem Biol 5:829-38
    • (2010) ACS Chem Biol , vol.5 , pp. 829-838
    • Kwan, D.H.1    Leadlay, P.F.2
  • 72
    • 56049119642 scopus 로고    scopus 로고
    • Prediction and manipulation of the stereochemistry of enoylreduction in modular polyketide synthases
    • Kwan DH, Sun Y, Schulz F, et al. (2008). Prediction and manipulation of the stereochemistry of enoylreduction in modular polyketide synthases. Chem Biol 15:1231-40
    • (2008) Chem Biol , vol.15 , pp. 1231-1240
    • Kwan, D.H.1    Sun, Y.2    Schulz, F.3
  • 73
    • 1542320193 scopus 로고    scopus 로고
    • Manipulation of carrier proteins in antibiotic biosynthesis
    • La Clair JJ, Foley TL, Schegg TR, et al. (2004). Manipulation of carrier proteins in antibiotic biosynthesis. Chem Biol 11:195-201
    • (2004) Chem Biol , vol.11 , pp. 195-201
    • La Clair, J.J.1    Foley, T.L.2    Schegg, T.R.3
  • 74
    • 0030294470 scopus 로고    scopus 로고
    • A new enzyme superfamily - The phosphopantetheinyl transferases
    • Lambalot RH, Gehring AM, Flugel RS, et al. (1996). A new enzyme superfamily - the phosphopantetheinyl transferases. Chem Biol 3:923-36
    • (1996) Chem Biol , vol.3 , pp. 923-936
    • Lambalot, R.H.1    Gehring, A.M.2    Flugel, R.S.3
  • 75
    • 0034730088 scopus 로고    scopus 로고
    • Substrate specificity of the loading didomain of the erythromycin polyketide synthase
    • Lau J, Cane DE, Khosla C. (2000). Substrate specificity of the loading didomain of the erythromycin polyketide synthase. Biochemistry 39:10514-20
    • (2000) Biochemistry , vol.39 , pp. 10514-10520
    • Lau, J.1    Cane, D.E.2    Khosla, C.3
  • 76
    • 0033514424 scopus 로고    scopus 로고
    • Dissecting the role of acyltransferase domains of modular polyketide synthases in the choice and stereochemical fate of extender units
    • Lau J, Fu H, Cane DE, et al. (1999). Dissecting the role of acyltransferase domains of modular polyketide synthases in the choice and stereochemical fate of extender units. Biochemistry 38:1643-51
    • (1999) Biochemistry , vol.38 , pp. 1643-1651
    • Lau, J.1    Fu, H.2    Cane, D.E.3
  • 77
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site
    • Leesong M, Henderson BS, Gillig JR, et al. (1996). Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4:253-64
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3
  • 78
    • 0037472114 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein
    • Li Q, Khosla C, Puglisi JD, et al. (2003). Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein. Biochemistry 42:4648-57
    • (2003) Biochemistry , vol.42 , pp. 4648-4657
    • Li, Q.1    Khosla, C.2    Puglisi, J.D.3
  • 79
    • 77954937832 scopus 로고    scopus 로고
    • Classification, prediction, and verification of the regioselectivity of fungal polyketide synthase product template domains
    • Li Y, Xu W, Tang Y. (2010). Classification, prediction, and verification of the regioselectivity of fungal polyketide synthase product template domains. J Biol Chem 285:22762-71
    • (2010) J Biol Chem , vol.285 , pp. 22762-22771
    • Li, Y.1    Xu, W.2    Tang, Y.3
  • 80
    • 84863304168 scopus 로고    scopus 로고
    • Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis
    • Liew CW, Nilsson M, Chen MW, et al. (2012). Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis. J Biol Chem 287:23203-15
    • (2012) J Biol Chem , vol.287 , pp. 23203-23215
    • Liew, C.W.1    Nilsson, M.2    Chen, M.W.3
  • 81
    • 78349306683 scopus 로고    scopus 로고
    • Induced-fit upon ligand binding revealed by crystal structures of the hot-dog fold thioesterase in dynemicin biosynthesis
    • Liew CW, Sharff A, Kotaka M, et al. (2010). Induced-fit upon ligand binding revealed by crystal structures of the hot-dog fold thioesterase in dynemicin biosynthesis. J Mol Biol 404:291-306
    • (2010) J Mol Biol , vol.404 , pp. 291-306
    • Liew, C.W.1    Sharff, A.2    Kotaka, M.3
  • 82
    • 79957950813 scopus 로고    scopus 로고
    • Solution structures of the acyl carrier protein domain from the highly reducing type i iterative polyketide synthase CalE8
    • Lim J, Kong R, Murugan E, et al. (2011). Solution structures of the acyl carrier protein domain from the highly reducing type I iterative polyketide synthase CalE8. PLoS One 6:e20549
    • (2011) PLoS One , vol.6
    • Lim, J.1    Kong, R.2    Murugan, E.3
  • 83
    • 0037435553 scopus 로고    scopus 로고
    • Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases
    • Liou GF, Lau J, Cane DE, et al. (2003). Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases. Biochemistry 42:200-7
    • (2003) Biochemistry , vol.42 , pp. 200-207
    • Liou, G.F.1    Lau, J.2    Cane, D.E.3
  • 84
    • 82255181183 scopus 로고    scopus 로고
    • Structural basis for phosphopantetheinyl carrier domain interactions in the terminal module of nonribosomal peptide synthetases
    • Liu Y, Zheng T, Bruner SD. (2011). Structural basis for phosphopantetheinyl carrier domain interactions in the terminal module of nonribosomal peptide synthetases. Chem Biol 18:1482-8
    • (2011) Chem Biol , vol.18 , pp. 1482-1488
    • Liu, Y.1    Zheng, T.2    Bruner, S.D.3
  • 85
    • 70350493673 scopus 로고    scopus 로고
    • Complete reconstitution of a highly reducing iterative polyketide synthase
    • Ma SM, Li JW, Choi JW, et al. (2009). Complete reconstitution of a highly reducing iterative polyketide synthase. Science 326:589-92
    • (2009) Science , vol.326 , pp. 589-592
    • Schuler, M.A.M.1    Li, J.W.2    Choi, J.W.3
  • 86
    • 38349000749 scopus 로고    scopus 로고
    • Redirecting the cyclization steps of fungal polyketide synthase
    • Ma SM, Zhan J, Xie X, et al. (2008). Redirecting the cyclization steps of fungal polyketide synthase. J Am Chem Soc 130:38-9
    • (2008) J Am Chem Soc , vol.130 , pp. 38-39
    • Schuler, M.A.M.1    Zhan, J.2    Xie, X.3
  • 87
    • 33644697200 scopus 로고    scopus 로고
    • Architecture of mammalian fatty acid synthase at 4.5 A resolution
    • Maier T, Jenni S, Ban N. (2006). Architecture of mammalian fatty acid synthase at 4.5 A resolution. Science 311:1258-62
    • (2006) Science , vol.311 , pp. 1258-1262
    • Maier, T.1    Jenni, S.2    Ban, N.3
  • 88
    • 51149098989 scopus 로고    scopus 로고
    • The crystal structure of a mammalian fatty acid synthase
    • Maier T, Leibundgut M, Ban N. (2008). The crystal structure of a mammalian fatty acid synthase. Science 321:1315-22
    • (2008) Science , vol.321 , pp. 1315-1322
    • Maier, T.1    Leibundgut, M.2    Ban, N.3
  • 89
    • 0033515090 scopus 로고    scopus 로고
    • Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel ''unnatural'' natural products
    • McDaniel R, Thamchaipenet A, Gustafsson C, et al. (1999). Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel ''unnatural'' natural products. Proc Nat Acad Sci USA 96:1846-51
    • (1999) Proc Nat Acad Sci USA , vol.96 , pp. 1846-1851
    • McDaniel, R.1    Thamchaipenet, A.2    Gustafsson, C.3
  • 90
    • 68949159560 scopus 로고    scopus 로고
    • The chemical biology of modular biosynthetic enzymes
    • Meier JL, Burkart MD. (2009). The chemical biology of modular biosynthetic enzymes. Chem Soc Rev 38:2012-45
    • (2009) Chem Soc Rev , vol.38 , pp. 2012-2045
    • Meier, J.L.1    Burkart, M.D.2
  • 91
    • 77955418050 scopus 로고    scopus 로고
    • A mechanism based protein crosslinker for acyl carrier protein dehydratases
    • Meier JL, Haushalter RW, Burkart MD. (2010). A mechanism based protein crosslinker for acyl carrier protein dehydratases. Bioorg Med Chem Lett 20:4936-9
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 4936-4939
    • Meier, J.L.1    Haushalter, R.W.2    Burkart, M.D.3
  • 92
    • 0033525885 scopus 로고    scopus 로고
    • Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacylacyl carrier protein synthase
    • Moche M, Schneider G, Edwards P, et al. (1999). Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacylacyl carrier protein synthase. J Biol Chem 274:6031-34
    • (1999) J Biol Chem , vol.274 , pp. 6031-6034
    • Moche, M.1    Schneider, G.2    Edwards, P.3
  • 93
    • 84858308226 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the 30 years from
    • 1981 to 2010
    • Newman DJ, Cragg GM. (2012). Natural products as sources of new drugs over the 30 years from 1981 to 2010. J Nat Prod 75:311-35
    • (2012) J Nat Prod , vol.75 , pp. 311-335
    • Newman, D.J.1    Cragg, G.M.2
  • 94
    • 38949203821 scopus 로고    scopus 로고
    • Exploiting the mosaic structure of trans-acyltransferase polyketide synthases for natural product discovery and pathway dissection
    • Nguyen T, Ishida K, Jenke-Kodama H, et al. (2008). Exploiting the mosaic structure of trans-acyltransferase polyketide synthases for natural product discovery and pathway dissection. Nat Biotechnol 26:225-33
    • (2008) Nat Biotechnol , vol.26 , pp. 225-233
    • Nguyen, T.1    Ishida, K.2    Jenke-Kodama, H.3
  • 95
    • 0036375898 scopus 로고    scopus 로고
    • Medium-chain dehydrogenases/ reductases (MDR). Family characterizations including genome comparisons and active site modeling
    • Nordling E, Jornvall H, Persson B. (2002). Medium-chain dehydrogenases/ reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269:4267-76
    • (2002) Eur J Biochem , vol.269 , pp. 4267-4276
    • Nordling, E.1    Jornvall, H.2    Persson, B.3
  • 96
    • 0035085234 scopus 로고    scopus 로고
    • Structures of beta-ketoacyl-acyl carrier protein synthase i complexed with fatty acids elucidate its catalytic machinery
    • Olsen JG, Kadziola A, von Wettstein-Knowles P, et al. (2001). Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Structure 9:233-43
    • (2001) Structure , vol.9 , pp. 233-243
    • Olsen, J.G.1    Kadziola, A.2    Von Wettstein-Knowles, P.3
  • 97
    • 4344675456 scopus 로고    scopus 로고
    • Targeting modular polyketide synthases with iteratively acting acyltransferases from metagenomes of uncultured bacterial consortia
    • Piel J, Hui DQ, Fusetani N, et al. (2004). Targeting modular polyketide synthases with iteratively acting acyltransferases from metagenomes of uncultured bacterial consortia. Environ Microbiol 6:921-7
    • (2004) Environ Microbiol , vol.6 , pp. 921-927
    • Piel, J.1    Hui, D.Q.2    Fusetani, N.3
  • 98
    • 38049136859 scopus 로고    scopus 로고
    • A mammalian type i fatty acid synthase acyl carrier protein domain does not sequester acyl chains
    • Ploskon E, Arthur CJ, Evans SE, et al. (2008). A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains. J Biol Chem 283:518-28
    • (2008) J Biol Chem , vol.283 , pp. 518-528
    • Ploskon, E.1    Arthur, C.J.2    Evans, S.E.3
  • 99
    • 0038154085 scopus 로고    scopus 로고
    • The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae
    • Price AC, Rock CO, White SW. (2003). The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae. J Bacteriol 185:4136-43
    • (2003) J Bacteriol , vol.185 , pp. 4136-4143
    • Price, A.C.1    Rock, C.O.2    White, S.W.3
  • 100
    • 0035980230 scopus 로고    scopus 로고
    • Structure of beta-ketoacyl- [acyl carrier protein] reductase from Escherichia coli: Negative cooperativity and its structural basis
    • Price AC, Zhang YM, Rock CO, et al. (2001). Structure of beta-ketoacyl- [acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. Biochemistry 40:12772-81
    • (2001) Biochemistry , vol.40 , pp. 12772-12781
    • Price, A.C.1    Zhang, Y.M.2    Rock, C.O.3
  • 101
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri LE, Weinreb PH, Lei M, et al. (1998). Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37:1585-95
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3
  • 102
    • 0035845638 scopus 로고    scopus 로고
    • Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro
    • Rangan VS, Joshi AK, Smith S. (2001). Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 40:10792-9
    • (2001) Biochemistry , vol.40 , pp. 10792-10799
    • Rangan, V.S.1    Joshi, A.K.2    Smith, S.3
  • 103
    • 0030911617 scopus 로고    scopus 로고
    • Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA: acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue
    • Rangan VS, Smith S. (1997). Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. J Biol Chem 272:11975-8
    • (1997) J Biol Chem , vol.272 , pp. 11975-11978
    • Rangan, V.S.1    Smith, S.2
  • 104
    • 0041317602 scopus 로고    scopus 로고
    • The type i rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs
    • Reed MAC, Schweizer M, Szafranska AE, et al. (2003). The type I rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs. Org Biomol Chem 1:463-71
    • (2003) Org Biomol Chem , vol.1 , pp. 463-471
    • Mac, R.1    Schweizer, M.2    Szafranska, A.E.3
  • 105
    • 0035951074 scopus 로고    scopus 로고
    • Alteration of the substrate specificity of a modular polyketide synthase acyltransferase domain through site-specific mutations
    • Reeves CD, Murli S, Ashley GW, et al. (2001). Alteration of the substrate specificity of a modular polyketide synthase acyltransferase domain through site-specific mutations. Biochemistry 40:15464-70
    • (2001) Biochemistry , vol.40 , pp. 15464-15470
    • Reeves, C.D.1    Murli, S.2    Ashley, G.W.3
  • 106
    • 0036277954 scopus 로고    scopus 로고
    • X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site
    • Roujeinikova A, Baldock C, Simon WJ, et al. (2002). X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Structure 10:825-35
    • (2002) Structure , vol.10 , pp. 825-835
    • Roujeinikova, A.1    Baldock, C.2    Simon, W.J.3
  • 107
    • 0015719741 scopus 로고
    • The isolation and general properties of Escherichia coli malonyl coenzyme A-acyl carrier protein transacylase
    • Ruch FE, Vagelos PR. (1973). The isolation and general properties of Escherichia coli malonyl coenzyme A-acyl carrier protein transacylase. J Biol Chem 248:8086-94
    • (1973) J Biol Chem , vol.248 , pp. 8086-8094
    • Ruch, F.E.1    Vagelos, P.R.2
  • 108
    • 77955313358 scopus 로고    scopus 로고
    • Biochemical and structural characterization of the tautomycetin thioesterase: Analysis of a stereoselective polyketide hydrolase
    • Scaglione JB, Akey DL, Sullivan R, et al. (2010). Biochemical and structural characterization of the tautomycetin thioesterase: analysis of a stereoselective polyketide hydrolase. Angew Chem Int Ed Engl 49:5726-30
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 5726-5730
    • Scaglione, J.B.1    Akey, D.L.2    Sullivan, R.3
  • 109
    • 0029061966 scopus 로고
    • The Escherichia coli malonyl-coa-acyl carrier protein transacylase at 1.5-angstrom resolution - Crystal structure of a fatty acid synthase component
    • Serre L, Verbree EC, Dauter Z, et al. (1995). The Escherichia coli malonyl-coa-acyl carrier protein transacylase at 1.5-angstrom resolution - crystal structure of a fatty acid synthase component. J Biol Chem 270:12961-4
    • (1995) J Biol Chem , vol.270 , pp. 12961-12964
    • Serre, L.1    Verbree, E.C.2    Dauter, Z.3
  • 110
    • 33744954170 scopus 로고    scopus 로고
    • Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs
    • Sharma AK, Sharma SK, Surolia A, et al. (2006). Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs. Biochemistry 45:6904-16
    • (2006) Biochemistry , vol.45 , pp. 6904-6916
    • Sharma, A.K.1    Sharma, S.K.2    Surolia, A.3
  • 111
    • 34247853435 scopus 로고    scopus 로고
    • The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates
    • Sharma KK, Boddy CN. (2007). The thioesterase domain from the pimaricin and erythromycin biosynthetic pathways can catalyze hydrolysis of simple thioester substrates. Bioorg Med Chem Lett 17:3034-7
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 3034-3037
    • Sharma, K.K.1    Boddy, C.N.2
  • 112
    • 0037398774 scopus 로고    scopus 로고
    • Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms
    • Shen B. (2003). Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms. Curr Opin Chem Biol 7:285-95
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 285-295
    • Shen, B.1
  • 113
    • 0037816242 scopus 로고    scopus 로고
    • Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: Implication for NADPH and substrate recognition
    • Shimomura Y, Kakuta Y, Fukuyama K. (2003). Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition. J Bacteriol 185:4211-18
    • (2003) J Bacteriol , vol.185 , pp. 4211-4218
    • Shimomura, Y.1    Kakuta, Y.2    Fukuyama, K.3
  • 114
    • 26944480788 scopus 로고    scopus 로고
    • Molecular basis of Celmer's rules: Stereochemistry of catalysis by isolated ketoreductase domains from modular polyketide synthases
    • Siskos AP, Baerga-Ortiz A, Bali S, et al. (2005). Molecular basis of Celmer's rules: stereochemistry of catalysis by isolated ketoreductase domains from modular polyketide synthases. Chem Biol 12:1145-53
    • (2005) Chem Biol , vol.12 , pp. 1145-1153
    • Siskos, A.P.1    Baerga-Ortiz, A.2    Bali, S.3
  • 115
    • 51149101636 scopus 로고    scopus 로고
    • Biochemistry: An enzyme assembly line
    • Smith JL, Sherman DH. (2008). Biochemistry: an enzyme assembly line. Science 321:1304-5
    • (2008) Science , vol.321 , pp. 1304-1305
    • Smith, J.L.1    Sherman, D.H.2
  • 116
    • 34848843433 scopus 로고    scopus 로고
    • The type i fatty acid and polyketide synthases: A tale of two megasynthases
    • Smith S, Tsai SC. (2007). The type I fatty acid and polyketide synthases: a tale of two megasynthases. Nat Prod Rep 24:1041-72
    • (2007) Nat Prod Rep , vol.24 , pp. 1041-1072
    • Smith, S.1    Tsai, S.C.2
  • 117
    • 0037411269 scopus 로고    scopus 로고
    • Structural and functional organization of the animal fatty acid synthase
    • Smith S, Witkowski A, Joshi AK. (2003). Structural and functional organization of the animal fatty acid synthase. Prog Lipid Res 42:289-317
    • (2003) Prog Lipid Res , vol.42 , pp. 289-317
    • Smith, S.1    Witkowski, A.2    Joshi, A.K.3
  • 118
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • Staunton J, Weissman KJ. (2001). Polyketide biosynthesis: a millennium review. Nat Prod Rep 18:380-416
    • (2001) Nat Prod Rep , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 119
    • 34447516335 scopus 로고    scopus 로고
    • Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase
    • Tang Y, Chen AY, Kim CY, et al. (2007). Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase. Chem Biol 14:931-43
    • (2007) Chem Biol , vol.14 , pp. 931-943
    • Tang, Y.1    Chen, A.Y.2    Kim, C.Y.3
  • 120
    • 33746776204 scopus 로고    scopus 로고
    • The 2.7-angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase
    • Tang Y, Kim CY, Mathews II, et al. (2006). The 2.7-angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase. Proc Nat Acad Sci USA 103:11124-9
    • (2006) Proc Nat Acad Sci USA , vol.103 , pp. 11124-11129
    • Tang, Y.1    Kim, C.Y.2    Mathews, I.I.3
  • 121
    • 19344369476 scopus 로고    scopus 로고
    • Engineered biosynthesis of regioselectively modified aromatic polyketides using bimodular polyketide synthases
    • Tang Y, Lee TS, Khosla C. (2004). Engineered biosynthesis of regioselectively modified aromatic polyketides using bimodular polyketide synthases. PLoS Biol 2:227-38
    • (2004) PLoS Biol , vol.2 , pp. 227-238
    • Tang, Y.1    Lee, T.S.2    Khosla, C.3
  • 122
    • 0142135988 scopus 로고    scopus 로고
    • Polyketide chain length control by chain length factor
    • Tang Y, Tsai SC, Khosla C. (2003). Polyketide chain length control by chain length factor. J Am Chem Soc 125:12708-9
    • (2003) J Am Chem Soc , vol.125 , pp. 12708-12709
    • Tang, Y.1    Tsai, S.C.2    Khosla, C.3
  • 123
    • 77955446661 scopus 로고    scopus 로고
    • Insights into protein- protein and enzyme-substrate interactions in modular polyketide synthases
    • Tran L, Broadhurst RW, Tosin M, et al. (2010). Insights into protein- protein and enzyme-substrate interactions in modular polyketide synthases. Chem Biol 17:705-16
    • (2010) Chem Biol , vol.17 , pp. 705-716
    • Tran, L.1    Broadhurst, R.W.2    Tosin, M.3
  • 124
    • 44049097046 scopus 로고    scopus 로고
    • Covalent linkage mediates communication between ACP and TE domains in modular polyketide synthases
    • Tran L, Tosin M, Spencer JB, et al. (2008). Covalent linkage mediates communication between ACP and TE domains in modular polyketide synthases. ChemBioChem 9:905-15
    • (2008) ChemBioChem , vol.9 , pp. 905-915
    • Tran, L.1    Tosin, M.2    Spencer, J.B.3
  • 125
    • 64349124980 scopus 로고    scopus 로고
    • Structural enzymology of polyketide synthases
    • Tsai SC, Ames BD. (2009). Structural enzymology of polyketide synthases. Methods Enzymol 459:17-47
    • (2009) Methods Enzymol , vol.459 , pp. 17-47
    • Tsai, S.C.1    Ames, B.D.2
  • 126
    • 0037159232 scopus 로고    scopus 로고
    • Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases
    • Tsai SC, Lu HX, Cane DE, et al. (2002). Insights into channel architecture and substrate specificity from crystal structures of two macrocycle-forming thioesterases of modular polyketide synthases. Biochemistry 41:12598-606
    • (2002) Biochemistry , vol.41 , pp. 12598-12606
    • Tsai, S.C.1    Lu, H.X.2    Cane, D.E.3
  • 127
    • 0035909913 scopus 로고    scopus 로고
    • Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel
    • Tsai SC, Miercke LJ, Krucinski J, et al. (2001). Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel. Proc Nat Acad Sci USA 98:14808-13
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 14808-14813
    • Tsai, S.C.1    Miercke, L.J.2    Krucinski, J.3
  • 128
    • 0035957047 scopus 로고    scopus 로고
    • Selective protein-protein interactions direct channeling of intermediates between polyketide synthase modules
    • Tsuji SY, Cane DE, Khosla C. (2001). Selective protein-protein interactions direct channeling of intermediates between polyketide synthase modules. Biochemistry 40:2326-31
    • (2001) Biochemistry , vol.40 , pp. 2326-2331
    • Tsuji, S.Y.1    Cane, D.E.2    Khosla, C.3
  • 129
    • 69249111810 scopus 로고    scopus 로고
    • Structural insights into the acyl intermediates of the Plasmodium falciparum fatty acid synthesis pathway: The mechanism of expansion of the acyl carrier protein core
    • Upadhyay SK, Misra A, Srivastava R, et al. (2009). Structural insights into the acyl intermediates of the Plasmodium falciparum fatty acid synthesis pathway: the mechanism of expansion of the acyl carrier protein core. J Biol Chem 284:22390-400
    • (2009) J Biol Chem , vol.284 , pp. 22390-22400
    • Upadhyay, S.K.1    Misra, A.2    Srivastava, R.3
  • 130
    • 73249121219 scopus 로고    scopus 로고
    • The biochemical basis for stereochemical control in polyketide biosynthesis
    • Valenzano CR, Lawson RJ, Chen AY, et al. (2009). The biochemical basis for stereochemical control in polyketide biosynthesis. J Am Chem Soc 131:18501-11
    • (2009) J Am Chem Soc , vol.131 , pp. 18501-18511
    • Valenzano, C.R.1    Lawson, R.J.2    Chen, A.Y.3
  • 131
    • 77958502924 scopus 로고    scopus 로고
    • Stereospecificity of the dehydratase domain of the erythromycin polyketide synthase
    • Valenzano CR, You YO, Garg A, et al. (2010). Stereospecificity of the dehydratase domain of the erythromycin polyketide synthase. J Am Chem Soc 132:14697-9
    • (2010) J Am Chem Soc , vol.132 , pp. 14697-14699
    • Valenzano, C.R.1    You, Y.O.2    Garg, A.3
  • 132
    • 38949083855 scopus 로고    scopus 로고
    • The chemical versatility of natural-product assembly lines
    • Walsh CT. (2008). The chemical versatility of natural-product assembly lines. Acc Chem Res 41:4-10
    • (2008) Acc Chem Res , vol.41 , pp. 4-10
    • Walsh, C.T.1
  • 133
    • 67650066485 scopus 로고    scopus 로고
    • A thioesterase from an iterative fungal polyketide synthase shows macrocyclization and cross coupling activity and may play a role in controlling iterative cycling through product offloading
    • Wang M, Zhou H, Wirz M, et al. (2009). A thioesterase from an iterative fungal polyketide synthase shows macrocyclization and cross coupling activity and may play a role in controlling iterative cycling through product offloading. Biochemistry 48:6288-90
    • (2009) Biochemistry , vol.48 , pp. 6288-6290
    • Wang, M.1    Zhou, H.2    Wirz, M.3
  • 134
    • 84864212659 scopus 로고    scopus 로고
    • Parameterization of solvent-protein interaction and its use on NMR protein structure determination
    • Wang Y, Schwieters CD, Tjandra N. (2012). Parameterization of solvent-protein interaction and its use on NMR protein structure determination. J Magn Reson 221:76-84
    • (2012) J Magn Reson , vol.221 , pp. 76-84
    • Wang, Y.1    Schwieters, C.D.2    Tjandra, N.3
  • 135
    • 0142149140 scopus 로고    scopus 로고
    • Understanding substrate specificity of polyketide synthase modules by generating hybrid multimodular synthases
    • Watanabe K, Wang CC, Boddy CN, et al. (2003). Understanding substrate specificity of polyketide synthase modules by generating hybrid multimodular synthases. J Biol Chem 278:42020-6
    • (2003) J Biol Chem , vol.278 , pp. 42020-42026
    • Watanabe, K.1    Wang, C.C.2    Boddy, C.N.3
  • 136
    • 77949377752 scopus 로고    scopus 로고
    • Solution structure of an acyl carrier protein domain from a fungal type i polyketide synthase
    • Wattana-amorn P, Williams C, Ploskon E, et al. (2010). Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase. Biochemistry 49:2186-93
    • (2010) Biochemistry , vol.49 , pp. 2186-2193
    • Wattana-Amorn, P.1    Williams, C.2    Ploskon, E.3
  • 137
    • 64049111007 scopus 로고    scopus 로고
    • Introduction to polyketide biosynthesis. Complex enzymes in microbial natural product
    • Weissman KJ. (2009). Introduction to polyketide biosynthesis. Complex enzymes in microbial natural product. Biosynthesis Part B: Polyketides Aminocoumarins Carbohydrates 459:3-16
    • (2009) Biosynthesis Part B: Polyketides Aminocoumarins Carbohydrates , vol.459 , pp. 3-16
    • Weissman, K.J.1
  • 138
    • 33745200262 scopus 로고    scopus 로고
    • Evidence for a protein- protein interaction motif on an acyl carrier protein domain from a modular polyketide synthase
    • Weissman KJ, Hong H, Popovic B, et al. (2006). Evidence for a protein- protein interaction motif on an acyl carrier protein domain from a modular polyketide synthase. Chem Biol 13:625-36
    • (2006) Chem Biol , vol.13 , pp. 625-636
    • Weissman, K.J.1    Hong, H.2    Popovic, B.3
  • 139
    • 44049083124 scopus 로고    scopus 로고
    • Protein-protein interactions in multienzyme megasynthetases
    • Weissman KJ, Muller R. (2008). Protein-protein interactions in multienzyme megasynthetases. ChemBioChem 9:826-48
    • (2008) ChemBioChem , vol.9 , pp. 826-848
    • Weissman, K.J.1    Muller, R.2
  • 140
    • 0032486328 scopus 로고    scopus 로고
    • The thioesterase of the erythromycin-producing polyketide synthase: Influence of acyl chain structure on the mode of release of substrate analogues from the acyl enzyme intermediates
    • Weissman KJ, Smith CJ, Hanefeld U, et al. (1998). The thioesterase of the erythromycin-producing polyketide synthase: influence of acyl chain structure on the mode of release of substrate analogues from the acyl enzyme intermediates. Angew Chem Int Edn 37:1437-40
    • (1998) Angew Chem Int Edn , vol.37 , pp. 1437-1440
    • Weissman, K.J.1    Smith, C.J.2    Hanefeld, U.3
  • 141
    • 83455210375 scopus 로고    scopus 로고
    • Beyond ethylmalonyl-CoA: The functional role of crotonyl-CoA carboxylase/reductase homologs in expanding polyketide diversity
    • Wilson MC, Moore BS. (2012). Beyond ethylmalonyl-CoA: the functional role of crotonyl-CoA carboxylase/reductase homologs in expanding polyketide diversity. Nat Prod Rep 29:72-86
    • (2012) Nat Prod Rep , vol.29 , pp. 72-86
    • Wilson, M.C.1    Moore, B.S.2
  • 142
    • 10644281452 scopus 로고    scopus 로고
    • Head-to-head coiled arrangement of the subunits of the animal fatty acid synthase
    • Witkowski A, Ghosal A, Joshi AK, et al. (2004). Head-to-head coiled arrangement of the subunits of the animal fatty acid synthase. Chem Biol 11:1667-76
    • (2004) Chem Biol , vol.11 , pp. 1667-1676
    • Witkowski, A.1    Ghosal, A.2    Joshi, A.K.3
  • 143
    • 0029816829 scopus 로고    scopus 로고
    • Fatty acid synthase: In vitro complementation of inactive mutants
    • Witkowski A, Joshi A, Smith S. (1996). Fatty acid synthase: in vitro complementation of inactive mutants. Biochemistry 35:10569-75
    • (1996) Biochemistry , vol.35 , pp. 10569-10575
    • Witkowski, A.1    Joshi, A.2    Smith, S.3
  • 144
    • 0033597208 scopus 로고    scopus 로고
    • Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit - Reevaluation of the side-by-side, antiparallel subunit model
    • Witkowski A, Joshi AK, Rangan VS, et al. (1999). Dibromopropanone cross-linking of the phosphopantetheine and active-site cysteine thiols of the animal fatty acid synthase can occur both inter- and intrasubunit - reevaluation of the side-by-side, antiparallel subunit model. J Biol Chem 274:11557-63
    • (1999) J Biol Chem , vol.274 , pp. 11557-11563
    • Witkowski, A.1    Joshi, A.K.2    Rangan, V.S.3
  • 145
    • 73449134857 scopus 로고    scopus 로고
    • Protein-protein recognition between acyltransferases and acyl carrier proteins in multimodular polyketide synthases
    • Wong FT, Chen AY, Cane DE, et al. (2010). Protein-protein recognition between acyltransferases and acyl carrier proteins in multimodular polyketide synthases. Biochemistry 49:95-102
    • (2010) Biochemistry , vol.49 , pp. 95-102
    • Wong, F.T.1    Chen, A.Y.2    Cane, D.E.3
  • 146
    • 79960812401 scopus 로고    scopus 로고
    • Structure and mechanism of the trans-acting acyltransferase from the disorazole synthase
    • Wong FT, Jin X, Mathews II, et al. (2011). Structure and mechanism of the trans-acting acyltransferase from the disorazole synthase. Biochemistry 50:6539-48
    • (2011) Biochemistry , vol.50 , pp. 6539-6548
    • Wong, F.T.1    Jin, X.2    Mathews, I.I.3
  • 147
    • 33645699855 scopus 로고    scopus 로고
    • One-pot chemoenzymatic synthesis of reporter-modified proteins
    • Worthington AS, Burkart MD. (2006). One-pot chemoenzymatic synthesis of reporter-modified proteins. Org Biomol Chem 4:44-6
    • (2006) Org Biomol Chem , vol.4 , pp. 44-46
    • Worthington, A.S.1    Burkart, M.D.2
  • 148
    • 77950314719 scopus 로고    scopus 로고
    • Mechanism-based crosslinking as a gauge for functional interaction of modular synthases
    • Worthington AS, Porter DF, Burkart MD. (2010). Mechanism-based crosslinking as a gauge for functional interaction of modular synthases. Org Biomol Chem 8:1769-72
    • (2010) Org Biomol Chem , vol.8 , pp. 1769-1772
    • Worthington, A.S.1    Porter, D.F.2    Burkart, M.D.3
  • 149
    • 33846831427 scopus 로고    scopus 로고
    • Mechanism-based protein cross-linking probes to investigate carrier protein-mediated biosynthesis
    • Worthington AS, Rivera H, Torpey JW, et al. (2006). Mechanism-based protein cross-linking probes to investigate carrier protein-mediated biosynthesis. ACS Chem Biol 1:687-91
    • (2006) ACS Chem Biol , vol.1 , pp. 687-691
    • Worthington, A.S.1    Rivera, H.2    Torpey, J.W.3
  • 150
    • 0037117747 scopus 로고    scopus 로고
    • Quantitative analysis of the relative contributions of donor acyl carrier proteins, acceptor ketosynthases, and linker regions to intermodular transfer of intermediates in hybrid polyketide synthases
    • Wu N, Cane DE, Khosla C. (2002). Quantitative analysis of the relative contributions of donor acyl carrier proteins, acceptor ketosynthases, and linker regions to intermodular transfer of intermediates in hybrid polyketide synthases. Biochemistry 41:5056-66
    • (2002) Biochemistry , vol.41 , pp. 5056-5066
    • Wu, N.1    Cane, D.E.2    Khosla, C.3
  • 151
    • 0034809381 scopus 로고    scopus 로고
    • Assessing the balance between protein-protein interactions and enzyme-substrate interactions in the channeling of intermediates between polyketide synthase modules
    • Wu N, Tsuji SY, Cane DE, et al. (2001). Assessing the balance between protein-protein interactions and enzyme-substrate interactions in the channeling of intermediates between polyketide synthase modules. J Am Chem Soc 123:6465-74
    • (2001) J Am Chem Soc , vol.123 , pp. 6465-6474
    • Wu, N.1    Tsuji, S.Y.2    Cane, D.E.3
  • 152
    • 67650537065 scopus 로고    scopus 로고
    • Acyltransferase mediated polyketide release from a fungal megasynthase
    • Xie X, Meehan MJ, Xu W, et al. (2009). Acyltransferase mediated polyketide release from a fungal megasynthase. J Am Chem Soc 131:8388-9
    • (2009) J Am Chem Soc , vol.131 , pp. 8388-8389
    • Xie, X.1    Meehan, M.J.2    Xu, W.3
  • 153
    • 0037466331 scopus 로고    scopus 로고
    • Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases
    • Yadav G, Gokhale RS, Mohanty D. (2003). Computational approach for prediction of domain organization and substrate specificity of modular polyketide synthases. J Mol Biol 328:335-63
    • (2003) J Mol Biol , vol.328 , pp. 335-363
    • Yadav, G.1    Gokhale, R.S.2    Mohanty, D.3
  • 154
    • 0035907466 scopus 로고    scopus 로고
    • Erythromycin biosynthesis the 4-pro-S hydride of NADPH is utilized for ketoreduction by both module 5 and module 6 of the 6-deoxyerythronolide B synthase
    • Yin YF, Gokhale R, Khosla C, et al. (2001). Erythromycin biosynthesis. The 4-pro-S hydride of NADPH is utilized for ketoreduction by both module 5 and module 6 of the 6-deoxyerythronolide B synthase. Bioorg Med Chem Lett 11:1477-9
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 1477-1479
    • Yin, Y.F.1    Gokhale, R.2    Khosla, C.3
  • 155
    • 34249803594 scopus 로고    scopus 로고
    • Malonyl-CoA: Acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein
    • Zhang L, Liu W, Xiao J, et al. (2007). Malonyl-CoA: acyl carrier protein transacylase from Helicobacter pylori: crystal structure and its interaction with acyl carrier protein. Protein Sci 16:1184-92
    • (2007) Protein Sci , vol.16 , pp. 1184-1192
    • Zhang, L.1    Liu, W.2    Xiao, J.3
  • 156
    • 0035896547 scopus 로고    scopus 로고
    • Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III
    • Zhang YM, Rao MS, Heath RJ, et al. (2001). Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III. J Biol Chem 276:8231-8
    • (2001) J Biol Chem , vol.276 , pp. 8231-8238
    • Zhang, Y.M.1    Rao, M.S.2    Heath, R.J.3
  • 157
    • 0346101746 scopus 로고    scopus 로고
    • Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction
    • Zhang YM, Wu B, Zheng J, et al. (2003). Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction. J Biol Chem 278:52935-43
    • (2003) J Biol Chem , vol.278 , pp. 52935-52943
    • Zhang, Y.M.1    Wu, B.2    Zheng, J.3
  • 158
    • 77953799129 scopus 로고    scopus 로고
    • Oxazolomycin Biosynthesis in Streptomyces Albus JA3453 Featuring An ''acyltransferase-less'' type i polyketide synthase that incorporates two distinct extender units
    • Zhao C, Coughlin JM, Ju J, et al. (2010). Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an ''acyltransferase-less'' type I polyketide synthase that incorporates two distinct extender units. J Biol Chem 285:20097-108
    • (2010) J Biol Chem , vol.285 , pp. 20097-20108
    • Zhao, C.1    Coughlin, J.M.2    Ju, J.3
  • 159
    • 84862879901 scopus 로고    scopus 로고
    • Divergence of multimodular polyketide synthases revealed by a didomain structure
    • Zheng J, Gay DC, Demeler B, et al. (2012). Divergence of multimodular polyketide synthases revealed by a didomain structure. Nat Chem Biol 8:615-21
    • (2012) Nat Chem Biol , vol.8 , pp. 615-621
    • Zheng, J.1    Gay, D.C.2    Demeler, B.3
  • 160
    • 79958713315 scopus 로고    scopus 로고
    • Structural and functional analysis of C2-type ketoreductases from modular polyketide synthases
    • Zheng J, Keatinge-Clay AT. (2011). Structural and functional analysis of C2-type ketoreductases from modular polyketide synthases. J Mol Biol 410:105-17
    • (2011) J Mol Biol , vol.410 , pp. 105-117
    • Zheng, J.1    Keatinge-Clay, A.T.2
  • 161
    • 77955477986 scopus 로고    scopus 로고
    • Structural and functional analysis of A-type ketoreductases from the amphotericin modular polyketide synthase
    • Zheng J, Taylor CA, Piasecki SK, et al. (2010). Structural and functional analysis of A-type ketoreductases from the amphotericin modular polyketide synthase. Structure 18:913-22
    • (2010) Structure , vol.18 , pp. 913-922
    • Zheng, J.1    Taylor, C.A.2    Piasecki, S.K.3
  • 162
    • 84862777743 scopus 로고    scopus 로고
    • A fungal ketoreductase domain that displays substrate-dependent stereospecificity
    • Zhou H, Gao ZZ, Qiao KJ, et al. (2012). A fungal ketoreductase domain that displays substrate-dependent stereospecificity. Nat Chem Biol 8:331-3
    • (2012) Nat Chem Biol , vol.8 , pp. 331-333
    • Zhou, H.1    Gao, Z.Z.2    Qiao, K.J.3
  • 163
    • 44049091848 scopus 로고    scopus 로고
    • A polyketide macrolactone synthase from the filamentous fungus Gibberella zeae
    • Zhou H, Zhan J, Watanabe K, et al. (2008). A polyketide macrolactone synthase from the filamentous fungus Gibberella zeae. Proc Nat Acad Sci USA 105:6249-54
    • (2008) Proc Nat Acad Sci USA , vol.105 , pp. 6249-6254
    • Zhou, H.1    Zhan, J.2    Watanabe, K.3
  • 164
    • 33846057025 scopus 로고    scopus 로고
    • Production of dihydroisocoumarins in Fusarium verticillioides by swapping ketosynthase domain of the fungal iterative polyketide synthase Fum1p with that of lovastatin diketide synthase
    • Zhu X, Yu F, Li XC, et al. (2007). Production of dihydroisocoumarins in Fusarium verticillioides by swapping ketosynthase domain of the fungal iterative polyketide synthase Fum1p with that of lovastatin diketide synthase. J Am Chem Soc 129:36-7
    • (2007) J Am Chem Soc , vol.129 , pp. 36-37
    • Zhu, X.1    Yu, F.2    Li, X.C.3
  • 165
    • 33645968397 scopus 로고    scopus 로고
    • Solution structures of spinach acyl carrier protein with decanoate and stearate
    • Zornetzer GA, Fox BG, Markley JL. (2006). Solution structures of spinach acyl carrier protein with decanoate and stearate. Biochemistry 45:5217-27
    • (2006) Biochemistry , vol.45 , pp. 5217-5227
    • Zornetzer, G.A.1    Fox, B.G.2    Markley, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.