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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.
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48
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Rodriguez-Concepcion M, Campos N, Lois LM, Maldonado C, Hoeffler JF, Grosdemange-Billiard C, Rohmer M, Boronat A: Genetic evidence of branching in the isoprenoid pathway for the production of isopentenyl diphosphate and dimethylallyl diphosphate in Escherichia coli. FEBS Lett 2000, 473:328-332.
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50
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Adam P, Hecht S, Eisenreich WG, Kaiser J, Grawet T, Arigoni D, Bacher A, Rohdich F: Biosynthesis of terpenes: studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase. Proc Natl Acad Sci USA 2002, 99:12108-12113.
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51
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Alticicek B, Duin EC, Reichenberg A, Hedderich R, Kollas AK, Hintz M, Wagner S, Wiesner J, Beck E, Jomaa H: LytB protein catalyses the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis. FEBS Lett 2002, 532:437-440.
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52
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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.
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Proc Natl Acad Sci USA
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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.
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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.
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Ohya N, Koyama T: Biosynthesis of natural rubber and other natural polyisoprenoides. In Biopolymers - Biology, Chemistry, Biotechnology, Applications, vol 2 (Polyisoprenoids), edn 1. Edited by Koyama T, Steinbüchel A. Weinheim: Wiley-VCH; 2001:73-109.
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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.
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Oppermann-Sanio FB, Steinbüchel A: Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production. Naturwissenschaften 2001, 89:11-22.
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Naturwissenschaften
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Biosynthesis of the cyanobacterial reserve polymer multi-Larginyl-poly-L-aspartic acid (cyanophycin) - Mechanism of the cyanophycin synthetase reaction studied with synthetic primers
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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.
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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.
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Steinbüchel A, Lütke-Eversloh T: Metabolic engineering and pathway construction for biotechnological production of relevant polyhydroxyalkanoates in microorganisms. Biochem Eng 2003, 3734:1-16.
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Biochem Eng
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Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acid inclusions
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Steinbüchel A, Aerts K, Babel W, Fölliner C, Liebergesell M, Madkour MH, Mayer F, Pieper-Fürst U, Pries A, Valentin HE: Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acid inclusions. Can J Microbiol 1995, 41(Suppl 1):94-105.
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Liebergesell, M.5
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68
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Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus
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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.
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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.
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Microbiology
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Linos A, Steinbüchel A: Biodegradation of natural and synthetic rubbers. In Biopolymers - Biology, Chemistry, Biotechnology, Applications, vol 2 (Polyisoprenoids), edn 1. Edited by Koyama T, Steinbüchel A. Weinheim: Wiley-VCH; 2001:321-359.
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