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Volumn 26, Issue 4, 2014, Pages 1619-1629

Evolution of acyl-ACP thioesterases and β-ketoacyl-ACP synthases revealed by protein-protein interactions

Author keywords

Acyl carrier protein; Algae; Bacteria; Chlamydomonas reinhardtii; Evolution; Fatty acid synthase

Indexed keywords


EID: 84905264609     PISSN: 09218971     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10811-013-0203-4     Document Type: Article
Times cited : (19)

References (63)
  • 2
    • 84862585031 scopus 로고    scopus 로고
    • Feedback regulation of plastidic acetyl-CoA carboxylase by 18:1-acyl carrier protein in Brassica napus
    • Andre C, Haslam RP, Shanklin J (2012) Feedback regulation of plastidic acetyl-CoA carboxylase by 18: 1-acyl carrier protein in Brassica napus. Proc Natl Acad Sci U S A 109: 10107-10112.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10107-10112
    • Andre, C.1    Haslam, R.P.2    Shanklin, J.3
  • 3
    • 66749108480 scopus 로고    scopus 로고
    • A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the α-proteobacterial mitochondrial ancestor
    • Atteia A, Adrait A, Brugière S, Tardif M, van Lis R, Deusch O, Dagan T, Kuhn L, Gontero B, Martin W (2009) A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the α-proteobacterial mitochondrial ancestor. Mol Biol Evol 26: 1533-1548.
    • (2009) Mol Biol Evol , vol.26 , pp. 1533-1548
    • Atteia, A.1    Adrait, A.2    Brugière, S.3    Tardif, M.4    van Lis, R.5    Deusch, O.6    Dagan, T.7    Kuhn, L.8    Gontero, B.9    Martin, W.10
  • 4
    • 84866354335 scopus 로고    scopus 로고
    • Manipulating fatty acid biosynthesis in microalgae for biofuel through protein-protein interactions
    • Blatti JL, Beld J, Behnke CA, Mendez M, Mayfield SP, Burkart MD (2012) Manipulating fatty acid biosynthesis in microalgae for biofuel through protein-protein interactions. PLoS ONE 7(9).
    • (2012) PLoS ONE , vol.7 , Issue.9
    • Blatti, J.L.1    Beld, J.2    Behnke, C.A.3    Mendez, M.4    Mayfield, S.P.5    Burkart, M.D.6
  • 5
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery
    • Campbell JW, Cronan JE (2001) Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery. Annu Rev Microbiol 55: 305-332.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan, J.E.2
  • 6
    • 77954011231 scopus 로고    scopus 로고
    • Thioesterases: a new perspective based on their primary and tertiary structures
    • Cantu DC, Chen Y, Reilly PJ (2010) Thioesterases: a new perspective based on their primary and tertiary structures. Protein Sci 19: 1281-1295.
    • (2010) Protein Sci , vol.19 , pp. 1281-1295
    • Cantu, D.C.1    Chen, Y.2    Reilly, P.J.3
  • 8
    • 84870193101 scopus 로고    scopus 로고
    • Structural classification and properties of ketoacyl reductases, hydroxyacyl dehydratases, and enoyl reductases
    • Cantu DC, Dai T, Beversdorf ZS, Reilly PJ (2012a) Structural classification and properties of ketoacyl reductases, hydroxyacyl dehydratases, and enoyl reductases. Protein Eng Des Sel 25: 803-811.
    • (2012) Protein Eng Des Sel , vol.25 , pp. 803-811
    • Cantu, D.C.1    Dai, T.2    Beversdorf, Z.S.3    Reilly, P.J.4
  • 9
    • 84860128454 scopus 로고    scopus 로고
    • Acyl carrier protein structural classification and normal mode analysis
    • Cantu DC, Forrester MJ, Charov K, Reilly PJ (2012b) Acyl carrier protein structural classification and normal mode analysis. Protein Sci 21: 655-666.
    • (2012) Protein Sci , vol.21 , pp. 655-666
    • Cantu, D.C.1    Forrester, M.J.2    Charov, K.3    Reilly, P.J.4
  • 11
    • 0027255719 scopus 로고
    • Escherichia coli thioesterase I, molecular cloning, and sequencing of the structural gene and identification as a periplasmic enzyme
    • Cho H, Cronan JE (1993) Escherichia coli thioesterase I, molecular cloning, and sequencing of the structural gene and identification as a periplasmic enzyme. J Biol Chem 268: 9238-9245.
    • (1993) J Biol Chem , vol.268 , pp. 9238-9245
    • Cho, H.1    Cronan, J.E.2
  • 12
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: an automated docking and discrimination method for the prediction of protein complexes
    • Comeau SR, Gatchell DW, Vajda S, Camacho CJ (2004) ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20: 45-50.
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 13
    • 84870042464 scopus 로고    scopus 로고
    • The structural role of the carrier protein-active controller or passive carrier
    • Crosby J, Crump MP (2012) The structural role of the carrier protein-active controller or passive carrier. Nat Prod Rep 29: 1111-1137.
    • (2012) Nat Prod Rep , vol.29 , pp. 1111-1137
    • Crosby, J.1    Crump, M.P.2
  • 14
    • 77955956793 scopus 로고    scopus 로고
    • Selectivity in a barren landscape: the P450BioIACP complex
    • Cryle MJ (2010) Selectivity in a barren landscape: the P450BioIACP complex. Biochem Soc Trans 38: 934.
    • (2010) Biochem Soc Trans , vol.38 , pp. 934
    • Cryle, M.J.1
  • 15
    • 0026056227 scopus 로고
    • Developmental induction, purification, and further characterization of 12:0-ACP thioesterase from immature cotyledons of Umbellularia californica
    • Davies HM, Anderson L, Fan C, Hawkins DJ (1991) Developmental induction, purification, and further characterization of 12: 0-ACP thioesterase from immature cotyledons of Umbellularia californica. Arch Biochem Biophys 290: 37-45.
    • (1991) Arch Biochem Biophys , vol.290 , pp. 37-45
    • Davies, H.M.1    Anderson, L.2    Fan, C.3    Hawkins, D.J.4
  • 16
    • 0035142840 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein
    • Davis MS, Cronan JE (2001) Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein. J Bacteriol 183: 1499-1503.
    • (2001) J Bacteriol , vol.183 , pp. 1499-1503
    • Davis, M.S.1    Cronan, J.E.2
  • 17
    • 34547131328 scopus 로고    scopus 로고
    • In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis
    • De Lay NR, Cronan JE (2007) In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. J Biol Chem 282: 20319-20328.
    • (2007) J Biol Chem , vol.282 , pp. 20319-20328
    • De Lay, N.R.1    Cronan, J.E.2
  • 18
    • 51249165796 scopus 로고
    • Characterization of two acyl-acyl carrier protein thioesterases from developing Cuphea seeds specific for medium-chain- and oleoyl-acyl carrier protein
    • Dörmann P, Spener F, Ohlrogge JB (1993) Characterization of two acyl-acyl carrier protein thioesterases from developing Cuphea seeds specific for medium-chain- and oleoyl-acyl carrier protein. Planta 189: 425-432.
    • (1993) Planta , vol.189 , pp. 425-432
    • Dörmann, P.1    Spener, F.2    Ohlrogge, J.B.3
  • 19
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 20
    • 70350376747 scopus 로고    scopus 로고
    • Escherichia coli unsaturated fatty acid synthesis: complex transcription of the FabA gene and in vivo identification of the essential reaction catalyzed by FabB
    • Feng Y, Cronan JE (2009) Escherichia coli unsaturated fatty acid synthesis: complex transcription of the FabA gene and in vivo identification of the essential reaction catalyzed by FabB. J Biol Chem 284: 29526-29535.
    • (2009) J Biol Chem , vol.284 , pp. 29526-29535
    • Feng, Y.1    Cronan, J.E.2
  • 21
    • 0037143585 scopus 로고    scopus 로고
    • Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity
    • Florova G, Kazanina G, Reynolds KA (2002) Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity. Biochemistry 41: 10462-10471.
    • (2002) Biochemistry , vol.41 , pp. 10462-10471
    • Florova, G.1    Kazanina, G.2    Reynolds, K.A.3
  • 22
    • 0025766849 scopus 로고
    • Transgenic expression of aminoglycoside adenine transferase in the chloroplast: a selectable marker for site-directed transformation of Chlamydomonas
    • Goldschmidt-Clermont M (1991) Transgenic expression of aminoglycoside adenine transferase in the chloroplast: a selectable marker for site-directed transformation of Chlamydomonas. Nucleic Acids Res 19: 4083-4089.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4083-4089
    • Goldschmidt-Clermont, M.1
  • 23
    • 83155184834 scopus 로고    scopus 로고
    • Characterization of a novel thioesterase (PtTE) from Phaeodactylum tricornutum
    • Gong Y, Guo X, Wan X, Liang Z, Jiang M (2011) Characterization of a novel thioesterase (PtTE) from Phaeodactylum tricornutum. J Basic Microbiol 51: 666-672.
    • (2011) J Basic Microbiol , vol.51 , pp. 666-672
    • Gong, Y.1    Guo, X.2    Wan, X.3    Liang, Z.4    Jiang, M.5
  • 24
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii
    • Gorman DS, Levine RP (1965) Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc Natl Acad Sci U S A 54: 1665-1669.
    • (1965) Proc Natl Acad Sci U S A , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 25
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Métoz F (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 26
    • 0025353421 scopus 로고
    • Escherichia coli β-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin
    • Guerra DJ, Browse JA (1990) Escherichia coli β-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin. Arch Biochem Biophys 280: 336-345.
    • (1990) Arch Biochem Biophys , vol.280 , pp. 336-345
    • Guerra, D.J.1    Browse, J.A.2
  • 27
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F (2001) MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17: 754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 28
    • 56549128655 scopus 로고    scopus 로고
    • Divergent evolution of the thiolase superfamily and chalcone synthase family
    • Jiang C, Kim SY, Suh DY (2008) Divergent evolution of the thiolase superfamily and chalcone synthase family. Mol Phylogenet Evol 49: 691-701.
    • (2008) Mol Phylogenet Evol , vol.49 , pp. 691-701
    • Jiang, C.1    Kim, S.Y.2    Suh, D.Y.3
  • 29
    • 81155158878 scopus 로고    scopus 로고
    • Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity
    • d oi: 10. 1186/1471-2091-12-44
    • Jing F, Cantu DC, Tvaruzkova J, Chipman JP, Nikolau BJ, Yandeau-Nelson MD, Reilly PJ (2011) Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity. BMC Biochem 12: 44 d oi: 10. 1186/1471-2091-12-44.
    • (2011) BMC Biochem , vol.12 , pp. 44
    • Jing, F.1    Cantu, D.C.2    Tvaruzkova, J.3    Chipman, J.P.4    Nikolau, B.J.5    Yandeau-Nelson, M.D.6    Reilly, P.J.7
  • 30
    • 0029257162 scopus 로고
    • Palmitoyl-acyl carrier protein (ACP) thioesterase and the evolutionary origin of plant acyl-ACP thioesterases
    • Jones A, Davies HM, Voelker TA (1995) Palmitoyl-acyl carrier protein (ACP) thioesterase and the evolutionary origin of plant acyl-ACP thioesterases. Plant Cell 7: 359-371.
    • (1995) Plant Cell , vol.7 , pp. 359-371
    • Jones, A.1    Davies, H.M.2    Voelker, T.A.3
  • 31
    • 76749121331 scopus 로고    scopus 로고
    • High level production of adrenic acid in Physcomitrella patens using the algae Pavlova sp. Δ5-elongase gene
    • Kaewsuwan S, Bunyapraphatsara N, Cove DJ, Quatrano RS, Chodok P (2010) High level production of adrenic acid in Physcomitrella patens using the algae Pavlova sp. Δ5-elongase gene. Bioresour Technol 101: 4081-4088.
    • (2010) Bioresour Technol , vol.101 , pp. 4081-4088
    • Kaewsuwan, S.1    Bunyapraphatsara, N.2    Cove, D.J.3    Quatrano, R.S.4    Chodok, P.5
  • 32
    • 78649822879 scopus 로고    scopus 로고
    • A one-shot solution to bacterial and fungal contamination in the green alga Chlamydomonas reinhardtii culture by using an antibiotic cocktail
    • Kan Y, Pan J (2010) A one-shot solution to bacterial and fungal contamination in the green alga Chlamydomonas reinhardtii culture by using an antibiotic cocktail. J Phycol 46: 1356-1358.
    • (2010) J Phycol , vol.46 , pp. 1356-1358
    • Kan, Y.1    Pan, J.2
  • 34
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research
    • Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, Toyonaga H, Mori H (2006) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12: 291-299.
    • (2006) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 37
    • 0032976397 scopus 로고    scopus 로고
    • Markov chain Monte Carlo algorithms for the Bayesian analysis of phylogenetic trees
    • Larget B, Simon DL (1999) Markov chain Monte Carlo algorithms for the Bayesian analysis of phylogenetic trees. Mol Biol Evol 16: 750-759.
    • (1999) Mol Biol Evol , vol.16 , pp. 750-759
    • Larget, B.1    Simon, D.L.2
  • 38
    • 79955565417 scopus 로고    scopus 로고
    • Fatty acid production in genetically modified cyanobacteria
    • Liu X, Sheng J, Curtiss III R (2011) Fatty acid production in genetically modified cyanobacteria. Proc Natl Acad Sci U S A 108: 6899-6904.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6899-6904
    • Liu, X.1    Sheng, J.2    Curtiss III, R.3
  • 39
    • 0038723702 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: Consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
    • Lo YC, Lin SC, Shaw JF, Liaw YC (2003) Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: Consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol 330: 539-551.
    • (2003) J Mol Biol , vol.330 , pp. 539-551
    • Lo, Y.C.1    Lin, S.C.2    Shaw, J.F.3    Liaw, Y.C.4
  • 40
    • 33749176747 scopus 로고
    • Fatty acid synthase-an example of protein evolution by gene fusion
    • McCarthy AD, Hardie DG (1984) Fatty acid synthase-an example of protein evolution by gene fusion. Trends Biochem Sci 9: 60-63.
    • (1984) Trends Biochem Sci , vol.9 , pp. 60-63
    • McCarthy, A.D.1    Hardie, D.G.2
  • 42
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: a novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 43
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2-Approximately maximum-likelihood trees for large alignments
    • Price MN, Dehal PS, Arkin AP (2010) FastTree 2-Approximately maximum-likelihood trees for large alignments. PLoS ONE 5(3).
    • (2010) PLoS ONE , vol.5 , Issue.3
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 44
  • 45
    • 78650557603 scopus 로고    scopus 로고
    • Genetic engineering of fatty acid chain length in Phaeodactylum tricornutum
    • Radakovits R, Eduafo PM, Posewitz MC (2011) Genetic engineering of fatty acid chain length in Phaeodactylum tricornutum. Metab Eng 13: 89-95.
    • (2011) Metab Eng , vol.13 , pp. 89-95
    • Radakovits, R.1    Eduafo, P.M.2    Posewitz, M.C.3
  • 46
    • 84905266106 scopus 로고    scopus 로고
    • Rambaut A (2009)http://tree. bio. ed. ac. uk/software/figtree/.
    • (2009)
    • Rambaut, A.1
  • 47
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 48
    • 0242285757 scopus 로고    scopus 로고
    • Plastid-derived type II fatty acid biosynthetic enzymes in chromists
    • Ryall K, Harper JT, Keeling PJ (2003) Plastid-derived type II fatty acid biosynthetic enzymes in chromists. Gene 313: 139-148.
    • (2003) Gene , vol.313 , pp. 139-148
    • Ryall, K.1    Harper, J.T.2    Keeling, P.J.3
  • 49
    • 0029107708 scopus 로고
    • Expression of the Escherichia coli FabA gene encoding beta-hydroxydecanoyl thioester dehydrase and transport to chloroplasts in transgenic tobacco
    • Saito K, Hamajima A, Ohkuma M, Murakoshi I, Ohmori S, Kawaguchi A, Teeri TH, Cronan Jnr JE (1995) Expression of the Escherichia coli FabA gene encoding beta-hydroxydecanoyl thioester dehydrase and transport to chloroplasts in transgenic tobacco. Transgenic Res 4: 60-69.
    • (1995) Transgenic Res , vol.4 , pp. 60-69
    • Saito, K.1    Hamajima, A.2    Ohkuma, M.3    Murakoshi, I.4    Ohmori, S.5    Kawaguchi, A.6    Teeri, T.H.7    Cronan Jr., J.E.8
  • 50
    • 0036647410 scopus 로고    scopus 로고
    • Characterization of substrate specificity of plant FatA and FatB acyl-ACP thioesterases
    • Salas JJ, Ohlrogge JB (2002) Characterization of substrate specificity of plant FatA and FatB acyl-ACP thioesterases. Arch Biochem Biophys 403: 25-34.
    • (2002) Arch Biochem Biophys , vol.403 , pp. 25-34
    • Salas, J.J.1    Ohlrogge, J.B.2
  • 51
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 52
    • 79954465584 scopus 로고    scopus 로고
    • Structural and functional analyses of a saturated acyl ACP thioesterase, type B from immature seed tissue of Jatropha curcas
    • Srikanta Dani KG, Hatti KS, Ravikumar P, Kush A (2011) Structural and functional analyses of a saturated acyl ACP thioesterase, type B from immature seed tissue of Jatropha curcas. Plant Biol 13: 453-461.
    • (2011) Plant Biol , vol.13 , pp. 453-461
    • Srikanta Dani, K.G.1    Hatti, K.S.2    Ravikumar, P.3    Kush, A.4
  • 53
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 55
    • 0036338519 scopus 로고    scopus 로고
    • Metabolic engineering of fatty acid biosynthesis in plants
    • Thelen JJ, Ohlrogge JB (2002) Metabolic engineering of fatty acid biosynthesis in plants. Metab Eng 4: 12-21.
    • (2002) Metab Eng , vol.4 , pp. 12-21
    • Thelen, J.J.1    Ohlrogge, J.B.2
  • 56
    • 0028149560 scopus 로고
    • Alteration of the specificity and regulation of fatty acid synthesis of Escherichia coli by expression of a plant medium-chain acyl-acyl carrier protein thioesterase
    • Voelker TA, Davies HM (1994) Alteration of the specificity and regulation of fatty acid synthesis of Escherichia coli by expression of a plant medium-chain acyl-acyl carrier protein thioesterase. J Bacteriol 176: 7320-7327.
    • (1994) J Bacteriol , vol.176 , pp. 7320-7327
    • Voelker, T.A.1    Davies, H.M.2
  • 57
    • 77950586384 scopus 로고    scopus 로고
    • Intein-mediated cyclization of bacterial acyl carrier protein stabilizes its folded conformation but does not abolish function
    • Volkmann G, Murphy PW, Rowland EE, Cronan JE Jr, Liu XQ, Blouin C, Byers DM (2010) Intein-mediated cyclization of bacterial acyl carrier protein stabilizes its folded conformation but does not abolish function. J Biol Chem 285: 8605-8614.
    • (2010) J Biol Chem , vol.285 , pp. 8605-8614
    • Volkmann, G.1    Murphy, P.W.2    Rowland, E.E.3    Cronan Jr., J.E.4    Liu, X.Q.5    Blouin, C.6    Byers, D.M.7
  • 58
    • 33846831427 scopus 로고    scopus 로고
    • Mechanism-based protein cross-linking probes to investigate carrier protein-mediated biosynthesis
    • Worthington AS, Rivera H, Torpey JW, Alexander MD, Burkart MD (2006) Mechanism-based protein cross-linking probes to investigate carrier protein-mediated biosynthesis. ACS Chem Biol 1: 687-691.
    • (2006) ACS Chem Biol , vol.1 , pp. 687-691
    • Worthington, A.S.1    Rivera, H.2    Torpey, J.W.3    Alexander, M.D.4    Burkart, M.D.5
  • 60
    • 80053319603 scopus 로고    scopus 로고
    • Characterization and analysis of the cotton cyclopropane fatty acid synthase family and their contribution to cyclopropane fatty acid synthesis
    • doi:10.1186/1471-2229-11-97
    • Yu XH, Rawat R, Shanklin J (2011) Characterization and analysis of the cotton cyclopropane fatty acid synthase family and their contribution to cyclopropane fatty acid synthesis. BMC Plant Biol 11: 97. doi: 10. 1186/1471-2229-11-97.
    • (2011) BMC Plant Biol , vol.11 , pp. 97
    • Yu, X.H.1    Rawat, R.2    Shanklin, J.3
  • 61
    • 0028871447 scopus 로고
    • Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering
    • Yuan L, Voelker TA, Hawkins DJ (1995) Modification of the substrate specificity of an acyl-acyl carrier protein thioesterase by protein engineering. Proc Natl Acad Sci U S A 92: 10639-10643.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10639-10643
    • Yuan, L.1    Voelker, T.A.2    Hawkins, D.J.3
  • 62
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinforma 9.
    • (2008) BMC Bioinforma 9
    • Zhang, Y.1
  • 63
    • 74949114946 scopus 로고    scopus 로고
    • The length of the bound fatty acid influences the dynamics of the acyl carrier protein and the stability of the thioester bond
    • Zornetzer GA, Tanem J, Fox BG, Markley JL (2010) The length of the bound fatty acid influences the dynamics of the acyl carrier protein and the stability of the thioester bond. Biochemistry 49/3: 470-477.
    • (2010) Biochemistry , vol.49 , Issue.3 , pp. 470-477
    • Zornetzer, G.A.1    Tanem, J.2    Fox, B.G.3    Markley, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.