메뉴 건너뛰기




Volumn 6, Issue 3, 2003, Pages 261-270

Production of rubber-like polymers by microorganisms

Author keywords

[No Author keywords available]

Indexed keywords

1,4 POLYISOPRENE; BIOPOLYMER; CARBON; DIMETHYLALLYLTRANSFERASE; ELASTOMER; ISOMERASE; ISOPRENE; ISOPRENOID; METHYLERYTHRITOL PHOSPHATE; MEVALONIC ACID; MICROBIAL ENZYME; PHOSPHATE; POLYESTER; POLYHYDROXYALKANOIC ACID; POLYMER; RUBBER; THIOESTER; UNCLASSIFIED DRUG;

EID: 0037927755     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(03)00061-4     Document Type: Review
Times cited : (61)

References (72)
  • 5
    • 0034045387 scopus 로고    scopus 로고
    • Microstructure of purified rubber particles
    • Wood DF, Cornish K: Microstructure of purified rubber particles. Int J Plant Sci 2000, 161:435-445.
    • (2000) Int J Plant Sci , vol.161 , pp. 435-445
    • Wood, D.F.1    Cornish, K.2
  • 6
    • 0033902401 scopus 로고    scopus 로고
    • A simplified protocol for micropropagation of guayule (Parthenium argentatum, Gray)
    • Castillon J, Cornish K: A simplified protocol for micropropagation of guayule (Parthenium argentatum, Gray). In Vitro Cell Dev Biol Plant 2000, 36:215-219.
    • (2000) In Vitro Cell Dev Biol Plant , vol.36 , pp. 215-219
    • Castillon, J.1    Cornish, K.2
  • 7
    • 0032903712 scopus 로고    scopus 로고
    • Regulation of initiation and polymer molecular weight of cis-1,4-polyisoprene synthesized in vitro by particles isolated from P. argentatum (Gray)
    • Castillon J, Cornish K: Regulation of initiation and polymer molecular weight of cis-1,4-polyisoprene synthesized in vitro by particles isolated from P. argentatum (Gray). Phytochemistry 2000, 51:43-51.
    • (2000) Phytochemistry , vol.51 , pp. 43-51
    • Castillon, J.1    Cornish, K.2
  • 10
    • 0347241168 scopus 로고    scopus 로고
    • Perspectives for biotechnological production and utilization of biopolymers: Metabolic engineering of polyhydroxyalkanoate biosynthesis pathways as a successful example
    • Steinbüchel A: Perspectives for biotechnological production and utilization of biopolymers: metabolic engineering of polyhydroxyalkanoate biosynthesis pathways as a successful example. Macromol Biosci 2001, 1:1-24.
    • (2001) Macromol Biosci , vol.1 , pp. 1-24
    • Steinbüchel, A.1
  • 13
    • 0020526779 scopus 로고
    • Characterization of intracellular inclusions formed by Pseudomonas oleovorans during growth on octane
    • De Smet MJ, Eggink G, Witholt B, Kingma J, Wynberg H: Characterization of intracellular inclusions formed by Pseudomonas oleovorans during growth on octane. J Bacteriol 1983, 154:870-878.
    • (1983) J Bacteriol , vol.154 , pp. 870-878
    • De Smet, M.J.1    Eggink, G.2    Witholt, B.3    Kingma, J.4    Wynberg, H.5
  • 18
    • 0031845468 scopus 로고    scopus 로고
    • Radiation crosslinking of a bacterial medium-chain-length poly(hydroxyalkanoate) elastomer from tallow
    • Ashby RD, Cromwick AM, Foglia TA: Radiation crosslinking of a bacterial medium-chain-length poly(hydroxyalkanoate) elastomer from tallow. Int J Biol Macromol 1998, 23:61-72.
    • (1998) Int J Biol Macromol , vol.23 , pp. 61-72
    • Ashby, R.D.1    Cromwick, A.M.2    Foglia, T.A.3
  • 19
    • 0034726424 scopus 로고    scopus 로고
    • Viscoelastic properties of linseed oil-based medium chain length poly(hydroxyalkanoate) films: Effects of epoxidation and curing
    • Ashby RD, Foglia TA, Solaiman DKY, Liu CK, Nunez A, Eggink G: Viscoelastic properties of linseed oil-based medium chain length poly(hydroxyalkanoate) films: effects of epoxidation and curing. Int J Biol Macromol 2000, 27:355-361.
    • (2000) Int J Biol Macromol , vol.27 , pp. 355-361
    • Ashby, R.D.1    Foglia, T.A.2    Solaiman, D.K.Y.3    Liu, C.K.4    Nunez, A.5    Eggink, G.6
  • 20
    • 0034892795 scopus 로고    scopus 로고
    • Free radical crosslinking of unsaturated bacterial polyesters obtained from soybean oily acids
    • Hazer B, Demirel SI, Borcakli M, Eroglu MS, Cakmak M, Erman B: Free radical crosslinking of unsaturated bacterial polyesters obtained from soybean oily acids. Polym Bulletin 2001, 46:389-394.
    • (2001) Polym Bulletin , vol.46 , pp. 389-394
    • Hazer, B.1    Demirel, S.I.2    Borcakli, M.3    Eroglu, M.S.4    Cakmak, M.5    Erman, B.6
  • 21
  • 22
    • 0028498777 scopus 로고
    • Chemical modification of bacterial elastomers. 2. Sulfur vulcanization
    • Gagnon KD, Lenz RW, Farris RJ, Fuller RC: Chemical modification of bacterial elastomers. 2. Sulfur vulcanization. Polymer 1994, 35:4368-4375.
    • (1994) Polymer , vol.35 , pp. 4368-4375
    • Gagnon, K.D.1    Lenz, R.W.2    Farris, R.J.3    Fuller, R.C.4
  • 23
    • 0031357979 scopus 로고    scopus 로고
    • Poly(3-hydroxyalkanoate)s produced by Pseudomonas oleovorans grown by feeding nonanoic and 10-undecenoic acids in sequence
    • Kim YB, Rhee YH, Lenz RW: Poly(3-hydroxyalkanoate)s produced by Pseudomonas oleovorans grown by feeding nonanoic and 10-undecenoic acids in sequence. Polym J 1997, 29:894-898.
    • (1997) Polym J , vol.29 , pp. 894-898
    • Kim, Y.B.1    Rhee, Y.H.2    Lenz, R.W.3
  • 26
    • 0001075820 scopus 로고    scopus 로고
    • Crosslinking of microbial copolyesters with pendant epoxide groups by diamine
    • Lee MY, Cha SY, Park WH: Crosslinking of microbial copolyesters with pendant epoxide groups by diamine. Polymer 1999, 40:3787-3793.
    • (1999) Polymer , vol.40 , pp. 3787-3793
    • Lee, M.Y.1    Cha, S.Y.2    Park, W.H.3
  • 27
    • 0000092876 scopus 로고
    • Characterization and enzymatic degradation of a cross-linked bacterial polyester
    • Scherer TM, Fuller RC, Lenz RW: Characterization and enzymatic degradation of a cross-linked bacterial polyester. J Environ Polym Degrad 1994, 2:263-269.
    • (1994) J Environ Polym Degrad , vol.2 , pp. 263-269
    • Scherer, T.M.1    Fuller, R.C.2    Lenz, R.W.3
  • 28
    • 0036858637 scopus 로고    scopus 로고
    • Chemical modification of chlorinated microbial polyesters
    • Arkin AH, Hazer B: Chemical modification of chlorinated microbial polyesters. Biomacromolecules 2002, 3:1327-1335.
    • (2002) Biomacromolecules , vol.3 , pp. 1327-1335
    • Arkin, A.H.1    Hazer, B.2
  • 29
    • 0043236872 scopus 로고    scopus 로고
    • A biodegradable rubber from bacteria, poly(hydroxyalkanoate) from pseudomonads
    • De Koning G, Witholt B: A biodegradable rubber from bacteria, poly(hydroxyalkanoate) from pseudomonads. Mat Sci Eng C 1996, 4:121-124.
    • (1996) Mat Sci Eng C , vol.4 , pp. 121-124
    • De Koning, G.1    Witholt, B.2
  • 30
    • 0035155574 scopus 로고    scopus 로고
    • Identification of a new class of biopolymer: Bacterial synthesis of a sulfur-containing polymer with thioester linkages
    • Lütke-Eversloh T, Bergander K, Luftmann H, Steinbüchel A: Identification of a new class of biopolymer: bacterial synthesis of a sulfur-containing polymer with thioester linkages. Microbiology 2001, 147:11-19. This paper describes a novel class of biopolymer, the 8th chemical class, which has been referred to as the polythioesters. Biosynthesis of polythioesters was in Ralstonia eutropha catalysed by the unspecific polyhydroxyalkanoate synthase of this bacterium from 3-mercaptopropionyl-CoA, which was formed if the cells were cultivated with mercaptopropionic acid or thiodipropionic acid as carbon sources.
    • (2001) Microbiology , vol.147 , pp. 11-19
    • Lütke-Eversloh, T.1    Bergander, K.2    Luftmann, H.3    Steinbüchel, A.4
  • 32
    • 0028946084 scopus 로고
    • Phylogenetic identificafion and in situ detection of individual microbial cells without cultivation
    • Amann RI, Ludwig W, Schleifer KH: Phylogenetic identificafion and in situ detection of individual microbial cells without cultivation. Microbiol Rev 1995, 59: 143-169.
    • (1995) Microbiol Rev , vol.59 , pp. 143-169
    • Amann, R.I.1    Ludwig, W.2    Schleifer, K.H.3
  • 33
    • 0037010721 scopus 로고    scopus 로고
    • Metagenome - A challenging source of enzyme discovery
    • Lorenz P, Schleper C: Metagenome - a challenging source of enzyme discovery. J Mol Catal B - Enzymatic 2002, 19:13-19.
    • (2002) J Mol Catal B - Enzymatic , vol.19 , pp. 13-19
    • Lorenz, P.1    Schleper, C.2
  • 34
    • 84946810674 scopus 로고    scopus 로고
    • Biosynthetic routes to the building blocks of isoprenoids
    • Edited by Koyama T, Steinbüchel A. Weinheim: Wiley-VCH
    • Rohmer M, Seemann M, Grosdemange-Billiard C: Biosynthetic routes to the building blocks of isoprenoids. In Biopolymers Biology, Chemistry, Biotechnology, Applications, vol 2 (Polyisoprenoids), edn 1. Edited by Koyama T, Steinbüchel A. Weinheim: Wiley-VCH; 2001:49-72. This paper provides an excellent overview of the current state of the two pathways yielding isopentenyl diphosphate and dimethylallyl diphosphate and the implications of the existence of two different pathways for isoprenoid precursors and their distribution in various organisms.
    • (2001) Biopolymers Biology, Chemistry, Biotechnology, Applications, Vol 2 (Polyisoprenoids), Edn 1 , vol.2 , pp. 49-72
    • Rohmer, M.1    Seemann, M.2    Grosdemange-Billiard, C.3
  • 35
    • 0033513375 scopus 로고    scopus 로고
    • The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants
    • Lichtenthaler HK: The 1-deoxy-D-xylulose-5-phosphate pathway of isoprenoid biosynthesis in plants. Annu Rev Plant Physiol Plant Molec Biol 1999, 50:47-65.
    • (1999) Annu Rev Plant Physiol Plant Molec Biol , vol.50 , pp. 47-65
    • Lichtenthaler, H.K.1
  • 36
    • 0032558613 scopus 로고    scopus 로고
    • Fosmidomycin, a specific inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in the nonmevalonate pathway for terpenoid biosynthesis
    • Kuzuyama T, Shimizu T, Takahashi S, Seeto H: Fosmidomycin, a specific inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase in the nonmevalonate pathway for terpenoid biosynthesis. Tetrahedron Lett 1998, 39:7913-7916.
    • (1998) Tetrahedron Lett , vol.39 , pp. 7913-7916
    • Kuzuyama, T.1    Shimizu, T.2    Takahashi, S.3    Seeto, H.4
  • 38
    • 0034666627 scopus 로고    scopus 로고
    • Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: An approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa
    • Altincicek B, Hintz M, Sanderbrand S, Wiesner J, Beck E, Jomaa H: Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa. FEMS Microbiol Lett 2000, 190:329-333.
    • (2000) FEMS Microbiol Lett , vol.190 , pp. 329-333
    • Altincicek, B.1    Hintz, M.2    Sanderbrand, S.3    Wiesner, J.4    Beck, E.5    Jomaa, H.6
  • 39
    • 0037064471 scopus 로고    scopus 로고
    • Enzymatic synthesis of 1-deoxysugar-phosphates using E. coli 1-deoxy-D-xylulose 5-phosphate synthase
    • Querol J, Grosdemange-Billiard C, Rohmer M, Boronat A, Imperial S: Enzymatic synthesis of 1-deoxysugar-phosphates using E. coli 1-deoxy-D-xylulose 5-phosphate synthase. Tetrahedron Lett 2002, 43:8265-8268.
    • (2002) Tetrahedron Lett , vol.43 , pp. 8265-8268
    • Querol, J.1    Grosdemange-Billiard, C.2    Rohmer, M.3    Boronat, A.4    Imperial, S.5
  • 40
    • 0036379275 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis via the methylerythritol phosphate pathway - Mechanistic investigations of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase
    • Hoeffler JF, Tritsch D, Grosdemange-Billiard C, Rohmer M: Isoprenoid biosynthesis via the methylerythritol phosphate pathway - mechanistic investigations of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase. Eur J Biochem 2002, 269:4446-4457.
    • (2002) Eur J Biochem , vol.269 , pp. 4446-4457
    • Hoeffler, J.F.1    Tritsch, D.2    Grosdemange-Billiard, C.3    Rohmer, M.4
  • 41
    • 0034953307 scopus 로고    scopus 로고
    • Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis
    • Richard SB, Bowmann ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP: Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis. Nat Struct Biol 2001, 8:641-648. This paper provides the three-dimensional structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase. This is the first three-dimensional structure of an enzyme involved in isopentenyl diphosphate biosynthesis via the methylerythritol phosphate pathway.
    • (2001) Nat Struct Biol , vol.8 , pp. 641-648
    • Richard, S.B.1    Bowmann, M.E.2    Kwiatkowski, W.3    Kang, I.4    Chow, C.5    Lillo, A.M.6    Cane, D.E.7    Noel, J.P.8
  • 42
    • 0034655829 scopus 로고    scopus 로고
    • Studies on the nonmevalonate pathway: Conversion of 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol kinase
    • Kuzuyama T, Takagi M, Kaneda K, Watanabe H, Dairi T, Seto H: Studies on the nonmevalonate pathway: conversion of 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol kinase. Tetrahedron Lett 2000, 41:2925-2928.
    • (2000) Tetrahedron Lett , vol.41 , pp. 2925-2928
    • Kuzuyama, T.1    Takagi, M.2    Kaneda, K.3    Watanabe, H.4    Dairi, T.5    Seto, H.6
  • 45
    • 0037185506 scopus 로고    scopus 로고
    • Isopreniod biosynthesis in Escherichia coli via the methylerythritol phosphate pathway: Accumulation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate in a gcpE deficient mutant of Escherichia coli
    • Seemann M, Campos N, Rodriguez-Concepcion M, Hoeffler JF, Grosdemange-Billiard C, Boronat A, Rohmer M: Isopreniod biosynthesis in Escherichia coli via the methylerythritol phosphate pathway: accumulation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate in a gcpE deficient mutant of Escherichia coli. Tetrahedron Lett 2002, 43:775-778.
    • (2002) Tetrahedron Lett , vol.43 , pp. 775-778
    • Seemann, M.1    Campos, N.2    Rodriguez-Concepcion, M.3    Hoeffler, J.F.4    Grosdemange-Billiard, C.5    Boronat, A.6    Rohmer, M.7
  • 46
    • 0037127472 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in Escherichia coli via the methylerythritol phosphate pathway: Enzymatic conversion of methylerythritol cyclodiphosphate into a phosphorylated derivative of (E)-2-methylbut-2-ene-1,4-diol
    • Seemann M, Campos N, Rodriguez-Concepcion M, Ibanez E, Duvold T, Tritsch D, Boronat A, Rohmer M: Isoprenoid biosynthesis in Escherichia coli via the methylerythritol phosphate pathway: enzymatic conversion of methylerythritol cyclodiphosphate into a phosphorylated derivative of (E)-2-methylbut-2-ene-1,4-diol. Tetrahedron Lett 2002, 43:1413-1415. This paper clearly reveals the reaction catalysed by the last but one enzyme in the sequence of the methylerythritol phosphate pathway.
    • (2002) Tetrahedron Lett , vol.43 , pp. 1413-1415
    • Seemann, M.1    Campos, N.2    Rodriguez-Concepcion, M.3    Ibanez, E.4    Duvold, T.5    Tritsch, D.6    Boronat, A.7    Rohmer, M.8
  • 47
    • 2242429820 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis through the methylerythritol phosphate pathway: The (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein
    • Seemann M, Bui BTS, Wolff M, Tritsch D, Campos N, Boronat A, Marquet A, Rohmer M: Isoprenoid biosynthesis through the methylerythritol phosphate pathway: The (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein. Angew Chemie Int Ed 2002, 41:4337-4339.
    • (2002) Angew Chemie Int Ed , vol.41 , pp. 4337-4339
    • Seemann, M.1    Bui, B.T.S.2    Wolff, M.3    Tritsch, D.4    Campos, N.5    Boronat, A.6    Marquet, A.7    Rohmer, M.8
  • 48
  • 49
    • 0036714123 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in higher plants and in Escherichia coli: On the branching in the methylerythritol phosphate pathway and the independent biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate
    • Hoeffler JF, Hemmerlin A, Grosdemange-Billiard C, Bach TJ, Rohmer M: Isoprenoid biosynthesis in higher plants and in Escherichia coli: on the branching in the methylerythritol phosphate pathway and the independent biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate. Biochem J 2002, 366:573-583.
    • (2002) Biochem J , vol.366 , pp. 573-583
    • Hoeffler, J.F.1    Hemmerlin, A.2    Grosdemange-Billiard, C.3    Bach, T.J.4    Rohmer, M.5
  • 52
    • 0037452578 scopus 로고    scopus 로고
    • The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: Studies on the mechanisms of the reactions catalysed by IspG and IspH protein
    • Rohdich F, Zepeck F, Adam P, Hecht S, Kaiser J, Laupitz R, Grawert T, Amslinger S, Eisenreich W, Bacher A et al.: The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalysed by IspG and IspH protein. Proc Natl Acad Sci USA 2003, 100:1586-1591. This paper provides the most advanced biochemical characterisation of the two enzymes catalysing the last and the last but one reactions of the methylerythritol phosphate pathway. The products of the reactions catalysed by these two enzymes and the molar ratio of the two products resulting from catalysis of the last enzyme, the reductase, were determined. The paper provides evidence that the last but one enzyme, the synthase, requires auxiliary proteins.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1586-1591
    • Rohdich, F.1    Zepeck, F.2    Adam, P.3    Hecht, S.4    Kaiser, J.5    Laupitz, R.6    Grawert, T.7    Amslinger, S.8    Eisenreich, W.9    Bacher, A.10
  • 53
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang PH, Ko TP, Wang AHJ: Structure, mechanism and function of prenyltransferases. Eur J Biochem 2002, 269:3339-3354. This paper provides an excellent and up-to-date overview on the three classes of prenyltransferases, their molecular structures and biochemical reaction mechanisms.
    • (2002) Eur J Biochem , vol.269 , pp. 3339-3354
    • Liang, P.H.1    Ko, T.P.2    Wang, A.H.J.3
  • 54
    • 0037322820 scopus 로고    scopus 로고
    • Molecular analysis of cis-prenyl chain elongating enzymes
    • Kharel Y, Koyama T: Molecular analysis of cis-prenyl chain elongating enzymes. Nat Prod Rep 2003, 30:111-118. This paper provides an excellent and up-to-date overview of cis-isoprenyl pyrophosphate synthases with emphasis on the molecular structures and catalytic mechanisms. It also discusses, in detail, the aspect of carbonchain-length determination.
    • (2003) Nat Prod Rep , vol.30 , pp. 111-118
    • Kharel, Y.1    Koyama, T.2
  • 56
    • 0035832806 scopus 로고    scopus 로고
    • Similarities and differences in rubber biochemistry among plant species
    • Cornish K: Similarities and differences in rubber biochemistry among plant species. Phytochemistry 2001, 57:1123-1134. This paper describes the in vitro dependencies of rubber-molecule initiation and biosynthesis rate of rubber synthases of the three plants Hevea brasiliensis, Parthenium argentatum and Ficus elastica and of the molecular weight of the synthesised rubber from the substrate concentrations and the isopentenyl diphosphate to farnesyl diphosphate ratio.
    • (2001) Phytochemistry , vol.57 , pp. 1123-1134
    • Cornish, K.1
  • 57
    • 0034674654 scopus 로고    scopus 로고
    • Molecular cloning, expression and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana
    • Oh SK, Han KH, Ryu SB, Kang H: Molecular cloning, expression and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. J Biol Chem 2000, 275:18482-18488.
    • (2000) J Biol Chem , vol.275 , pp. 18482-18488
    • Oh, S.K.1    Han, K.H.2    Ryu, S.B.3    Kang, H.4
  • 58
    • 0034578097 scopus 로고    scopus 로고
    • Rubber molecular weight regulation, in vitro, in plant species that produce high and low molecular weights in vivo
    • Cornish K, Castillon J, Scott DJ: Rubber molecular weight regulation, in vitro, in plant species that produce high and low molecular weights in vivo. Biomacromolecules 2000, 1:633-641.
    • (2000) Biomacromolecules , vol.1 , pp. 633-641
    • Cornish, K.1    Castillon, J.2    Scott, D.J.3
  • 59
    • 0000199891 scopus 로고    scopus 로고
    • Isolation, characterisation and functional analysis of a novel cDNA clone encoding a small rubber particle protein from Hevea brasiliensis
    • Oh SK, Kang H, Shin DH, Yang J, Chow KS, Yeang HY, Wagner B, Breiteneder H, Han KH: Isolation, characterisation and functional analysis of a novel cDNA clone encoding a small rubber particle protein from Hevea brasiliensis. J Biol Chem 1999, 274:17132-17138.
    • (1999) J Biol Chem , vol.274 , pp. 17132-17138
    • Oh, S.K.1    Kang, H.2    Shin, D.H.3    Yang, J.4    Chow, K.S.5    Yeang, H.Y.6    Wagner, B.7    Breiteneder, H.8    Han, K.H.9
  • 60
    • 0038450995 scopus 로고    scopus 로고
    • PHA synthase from Chromatium vinosum: Cysteine 149 is involved in covalent catalysis
    • Müh U, Sinskey AJ, Kirby DP, Lane WS, Stubbe JA: PHA synthase from Chromatium vinosum: cysteine 149 is involved in covalent catalysis. Biochemistry 1999, 38:826-837.
    • (1999) Biochemistry , vol.38 , pp. 826-837
    • Müh, U.1    Sinskey, A.J.2    Kirby, D.P.3    Lane, W.S.4    Stubbe, J.A.5
  • 61
    • 0036164128 scopus 로고    scopus 로고
    • Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production
    • Oppermann-Sanio FB, Steinbüchel A: Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production. Naturwissenschaften 2001, 89:11-22.
    • (2001) Naturwissenschaften , vol.89 , pp. 11-22
    • Oppermann-Sanio, F.B.1    Steinbüchel, A.2
  • 62
    • 0033850973 scopus 로고    scopus 로고
    • Biosynthesis of the cyanobacterial reserve polymer multi-Larginyl-poly-L-aspartic acid (cyanophycin) - Mechanism of the cyanophycin synthetase reaction studied with synthetic primers
    • Berg H, Ziegler K, Piotukh K, Baier K, Lockau W, Volkmer-Engert R: Biosynthesis of the cyanobacterial reserve polymer multi-Larginyl-poly-L-aspartic acid (cyanophycin) - mechanism of the cyanophycin synthetase reaction studied with synthetic primers. Eur J Biochem 2000, 267:5561-5570.
    • (2000) Eur J Biochem , vol.267 , pp. 5561-5570
    • Berg, H.1    Ziegler, K.2    Piotukh, K.3    Baier, K.4    Lockau, W.5    Volkmer-Engert, R.6
  • 63
    • 0033969362 scopus 로고    scopus 로고
    • Cloning and characterization of the Yarrowia lipolytica squalene synthase (SQS1) gene and functional complementation of the Saccharomyces cerevisiae erg9 mutation
    • Merkulov S, van Assema F, Springer J, del Carmen AF, Mooibroek H: Cloning and characterization of the Yarrowia lipolytica squalene synthase (SQS1) gene and functional complementation of the Saccharomyces cerevisiae erg9 mutation. Yeast 2000, 16:197-206.
    • (2000) Yeast , vol.16 , pp. 197-206
    • Merkulov, S.1    Van Assema, F.2    Springer, J.3    Del Carmen, A.F.4    Mooibroek, H.5
  • 64
    • 0038468696 scopus 로고    scopus 로고
    • Metabolic engineering and pathway construction for biotechnological production of relevant polyhydroxyalkanoates in microorganisms
    • Steinbüchel A, Lütke-Eversloh T: Metabolic engineering and pathway construction for biotechnological production of relevant polyhydroxyalkanoates in microorganisms. Biochem Eng 2003, 3734:1-16.
    • (2003) Biochem Eng , vol.3734 , pp. 1-16
    • Steinbüchel, A.1    Lütke-Eversloh, T.2
  • 65
    • 0038806615 scopus 로고    scopus 로고
    • Biosynthetic routes diverting from intermediates of isoprenoid biosynthesis to related products of the metabolism
    • Edited by Koyama T, Steinbüchel A. Weinheim: Wiley-VCH
    • Zhang YW, Koyama T: Biosynthetic routes diverting from intermediates of isoprenoid biosynthesis to related products of the metabolism. In Biopolymers - Biology, Chemistry, Biotechnology, Applications, vol 2 (Polyisoprenolds), edn 1. Edited by Koyama T, Steinbüchel A. Weinheim: Wiley-VCH; 2001:111-142.
    • (2001) Biopolymers - Biology, Chemistry, Biotechnology, Applications, Vol 2 (Polyisoprenolds), Edn 1 , vol.2 , pp. 111-142
    • Zhang, Y.W.1    Koyama, T.2
  • 68
    • 0029039870 scopus 로고
    • Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus
    • Wieczorek R, Pries A, Steinbüchel A, Mayer F: Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus. J Bacteriol 1995, 177:2425-2435.
    • (1995) J Bacteriol , vol.177 , pp. 2425-2435
    • Wieczorek, R.1    Pries, A.2    Steinbüchel, A.3    Mayer, F.4
  • 70
    • 0037151074 scopus 로고    scopus 로고
    • A novel group of oleosins is present inside the pollen of Arabidopsis
    • Kim HU, Hsieh K, Ratnayake C, Huang AHC: A novel group of oleosins is present inside the pollen of Arabidopsis. J Biol Chem 2002, 277:22677-22684.
    • (2002) J Biol Chem , vol.277 , pp. 22677-22684
    • Kim, H.U.1    Hsieh, K.2    Ratnayake, C.3    Huang, A.H.C.4
  • 71
    • 0036667428 scopus 로고    scopus 로고
    • Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16
    • Pötter M, Madkour MH, Mayer F, Steinbüchel A: Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16. Microbiology 2002, 148:2413-2426. This paper proposes an interesting model for the regulation of expression of the major phasin PhaP1 from Ralstonia eutropha by the regulator protein PhaR, which binds to polyhydroxyalkanoate granules as well as to the upstream phaP1 and phaR regions. The conclusions drawn in this paper were based on their own molecular studies and on investigations carried out in the laboratories of AJ Sinskey and T Yamane.
    • (2002) Microbiology , vol.148 , pp. 2413-2426
    • Pötter, M.1    Madkour, M.H.2    Mayer, F.3    Steinbüchel, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.