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Volumn 189, Issue 22, 2007, Pages 8250-8256

Isolated poly(3-hydroxybutyrate) (PHB) granules are complex bacterial organelles catalyzing formation of PHB from acetyl coenzyme A (CoA) and degradation of PHB to acetyl-CoA

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYBUTYRYL ACETYL COENZYME A; ACETYL COENZYME A; BACTERIAL PROTEIN; POLY(3 HYDROXYBUTYRIC ACID); PROTEIN PHAZA1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 36549036251     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00752-07     Document Type: Article
Times cited : (95)

References (48)
  • 1
    • 26444456073 scopus 로고    scopus 로고
    • Properties of a novel intracellular poly(3-hydroxybutyrate) depolymerase with high specific activity (PhaZd) in Wautersia eutropha H16
    • Abe, T., T. Kobayashi, and T. Saito. 2005. Properties of a novel intracellular poly(3-hydroxybutyrate) depolymerase with high specific activity (PhaZd) in Wautersia eutropha H16. J. Bacteriol. 187:6982-6990.
    • (2005) J. Bacteriol , vol.187 , pp. 6982-6990
    • Abe, T.1    Kobayashi, T.2    Saito, T.3
  • 2
    • 33947538844 scopus 로고    scopus 로고
    • Biochemical evidence that phaZ gene encodes a specific intracellular medium chain length polyhydroxyalkanoate depolymerase in Pseudomonas putida KT2442: Characterization of a paradigmatic enzyme
    • de Eugenio, L. I., P. Garcia, J. M. Luengo, J. M. Sanz, J. S. Roman, J. L. Garcia, and M. A. Prieto. 2007. Biochemical evidence that phaZ gene encodes a specific intracellular medium chain length polyhydroxyalkanoate depolymerase in Pseudomonas putida KT2442: characterization of a paradigmatic enzyme. J. Biol. Chem. 282:4951-4962.
    • (2007) J. Biol. Chem , vol.282 , pp. 4951-4962
    • de Eugenio, L.I.1    Garcia, P.2    Luengo, J.M.3    Sanz, J.M.4    Roman, J.S.5    Garcia, J.L.6    Prieto, M.A.7
  • 3
    • 0025020367 scopus 로고
    • Cyclic nature of poly(3-hydroxyalkanoate) metabolism in Alcaligenes eutrophus
    • Doi, Y., A. Segawa, Y. Kawaguchi, and M. Kunioka. 1990. Cyclic nature of poly(3-hydroxyalkanoate) metabolism in Alcaligenes eutrophus. FEMS Microbiol. Lett. 55:165-169.
    • (1990) FEMS Microbiol. Lett , vol.55 , pp. 165-169
    • Doi, Y.1    Segawa, A.2    Kawaguchi, Y.3    Kunioka, M.4
  • 4
    • 0017145313 scopus 로고
    • Enzymatic synthesis of poly-beta-hydroxybutyrate in Zoogloea ramigera
    • Fukui, T., A. Yoshimoto, M. Matsumoto, S. Hosokawa, and T. Saito. 1976. Enzymatic synthesis of poly-beta-hydroxybutyrate in Zoogloea ramigera. Arch. Microbiol. 110:149-156.
    • (1976) Arch. Microbiol , vol.110 , pp. 149-156
    • Fukui, T.1    Yoshimoto, A.2    Matsumoto, M.3    Hosokawa, S.4    Saito, T.5
  • 5
    • 33748782753 scopus 로고    scopus 로고
    • Assay of poly(3-hydroxybutyrate) depolymerase activity and product determination
    • Gebauer, B., and D. Jendrossek. 2006. Assay of poly(3-hydroxybutyrate) depolymerase activity and product determination. Appl. Environ. Microbiol. 72:6094-6100.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 6094-6100
    • Gebauer, B.1    Jendrossek, D.2
  • 6
    • 0029049968 scopus 로고
    • Enzyme-catalyzed synthesis of poly[(R)-(-)-3-hydroxybutyrate]: Formation of macroscopic granules in vitro
    • Gerngross, T. U., and D. P. Martin. 1995. Enzyme-catalyzed synthesis of poly[(R)-(-)-3-hydroxybutyrate]: formation of macroscopic granules in vitro. Proc. Natl. Acad. Sci. USA 92:6279-6283.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6279-6283
    • Gerngross, T.U.1    Martin, D.P.2
  • 7
    • 0027297201 scopus 로고
    • Immunocytochemical analysis of poly-beta-hydroxybutyrate (PHB) synthase in Alcaligenes eutrophus H16: Localization of the synthase enzyme at the surface of PHB granules
    • Gerngross, T. U., P. Reilly, J. Stubbe, A. J. Sinskey, and O. P. Peoples. 1993. Immunocytochemical analysis of poly-beta-hydroxybutyrate (PHB) synthase in Alcaligenes eutrophus H16: localization of the synthase enzyme at the surface of PHB granules. J. Bacteriol. 175:5289-5293.
    • (1993) J. Bacteriol , vol.175 , pp. 5289-5293
    • Gerngross, T.U.1    Reilly, P.2    Stubbe, J.3    Sinskey, A.J.4    Peoples, O.P.5
  • 8
    • 0035965210 scopus 로고    scopus 로고
    • A new type of thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of short chain-length hydroxyalkanoic acids
    • Handrick, R., S. Reinhardt, M. L. Focarete, M. Scandola, G. Adamus, M. Kowalczuk, and D. Jendrossek. 2001. A new type of thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of short chain-length hydroxyalkanoic acids. J. Biol. Chem. 276:36215-36224.
    • (2001) J. Biol. Chem , vol.276 , pp. 36215-36224
    • Handrick, R.1    Reinhardt, S.2    Focarete, M.L.3    Scandola, M.4    Adamus, G.5    Kowalczuk, M.6    Jendrossek, D.7
  • 9
    • 0033814278 scopus 로고    scopus 로고
    • Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha
    • Handrick, R., S. Reinhardt, and D. Jendrossek. 2000. Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha. J. Bacteriol. 182:5916-5918.
    • (2000) J. Bacteriol , vol.182 , pp. 5916-5918
    • Handrick, R.1    Reinhardt, S.2    Jendrossek, D.3
  • 10
    • 1842473745 scopus 로고    scopus 로고
    • Unraveling the function of the Rhodospirillum rubrum activator of polyhydroxybutyrate (PHB) degradation: The activator is a PHB-granule-bound protein (phasin)
    • Handrick, R., S. Reinhardt, D. Schultheiss, T. Reichart, D. Schüler, V. Jendrossek, and D. Jendrossek. 2004. Unraveling the function of the Rhodospirillum rubrum activator of polyhydroxybutyrate (PHB) degradation: the activator is a PHB-granule-bound protein (phasin). J. Bacteriol. 186:2466-2475.
    • (2004) J. Bacteriol , vol.186 , pp. 2466-2475
    • Handrick, R.1    Reinhardt, S.2    Schultheiss, D.3    Reichart, T.4    Schüler, D.5    Jendrossek, V.6    Jendrossek, D.7
  • 11
    • 36549081427 scopus 로고    scopus 로고
    • Jendrossek, D. 2002. Extracellular polyhydroxyalkanoate depolymerases: the key enzymes of PHA degradation, p. 41-83. In Y. Doi and A. Steinbüchel (ed.), Biopolymers, 3b. Polyesters II. Wiley-VCH, Weinheim, Germany.
    • Jendrossek, D. 2002. Extracellular polyhydroxyalkanoate depolymerases: the key enzymes of PHA degradation, p. 41-83. In Y. Doi and A. Steinbüchel (ed.), Biopolymers, vol. 3b. Polyesters II. Wiley-VCH, Weinheim, Germany.
  • 12
    • 34247609332 scopus 로고    scopus 로고
    • Peculiarities of PHA granule preparation and PHA depolymerase activity determination
    • Jendrossek, D. 2007. Peculiarities of PHA granule preparation and PHA depolymerase activity determination. Appl. Microbiol. Biotechnol. 74:1186-1196.
    • (2007) Appl. Microbiol. Biotechnol , vol.74 , pp. 1186-1196
    • Jendrossek, D.1
  • 13
    • 0036406855 scopus 로고    scopus 로고
    • Microbial degradation of polyhydroxyalkanoates
    • Jendrossek, D., and R. Handrick. 2002. Microbial degradation of polyhydroxyalkanoates. Annu. Rev. Microbiol. 56:403-432.
    • (2002) Annu. Rev. Microbiol , vol.56 , pp. 403-432
    • Jendrossek, D.1    Handrick, R.2
  • 14
    • 33846404159 scopus 로고    scopus 로고
    • PHB granules at the early stages of formation are localized close to the cytoplasmic membrane in Caryophanon latum
    • Jendrossek, D., O. Selchow, and M. Hoppert. 2007. PHB granules at the early stages of formation are localized close to the cytoplasmic membrane in Caryophanon latum. Appl. Environ Microbiol. 73:586-593.
    • (2007) Appl. Environ Microbiol , vol.73 , pp. 586-593
    • Jendrossek, D.1    Selchow, O.2    Hoppert, M.3
  • 15
    • 0346752504 scopus 로고    scopus 로고
    • Catalytic triad of intracellular poly(3-hydroxybutyrate) depolymerase (PhaZ1) in Ralstonia eutropha H16
    • Kobayashi, T., and T. Saito. 2003. Catalytic triad of intracellular poly(3-hydroxybutyrate) depolymerase (PhaZ1) in Ralstonia eutropha H16. J. Biosci. Bioeng. 96:487-492.
    • (2003) J. Biosci. Bioeng , vol.96 , pp. 487-492
    • Kobayashi, T.1    Saito, T.2
  • 16
    • 0038285546 scopus 로고    scopus 로고
    • Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase
    • Kobayashi, T., M. Shiraki, T. Abe, A. Sugiyama, and T. Saito. 2003. Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase. J. Bacteriol. 185:3485-3490.
    • (2003) J. Bacteriol , vol.185 , pp. 3485-3490
    • Kobayashi, T.1    Shiraki, M.2    Abe, T.3    Sugiyama, A.4    Saito, T.5
  • 17
    • 22544433446 scopus 로고    scopus 로고
    • Novel intracellular 3-hydroxybutyrate-oligomer hydrolase in Wautersia eutropha H16
    • Kobayashi, T., K. Uchino, T. Abe, Y. Yamazaki, and T. Saito. 2005. Novel intracellular 3-hydroxybutyrate-oligomer hydrolase in Wautersia eutropha H16. J. Bacteriol. 187:5129-5135.
    • (2005) J. Bacteriol , vol.187 , pp. 5129-5135
    • Kobayashi, T.1    Uchino, K.2    Abe, T.3    Yamazaki, Y.4    Saito, T.5
  • 18
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., P. H. Elzer, D. S. Hill, G. T. Robertson, M. A. Farris, R. M. Roop II, and K. M. Peterson. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop II, R.M.6    Peterson, K.M.7
  • 19
    • 33847254447 scopus 로고    scopus 로고
    • Studies on the influence of phasins on accumulation and degradation of PHB and nanostructure of PHB granules in Ralstonia eutropha H16
    • Kuchta, K., L. Chi, H. Fuchs, M. Pötter, and A. Steinbüchel. 2007. Studies on the influence of phasins on accumulation and degradation of PHB and nanostructure of PHB granules in Ralstonia eutropha H16. Biomacromolecules 8:657-662.
    • (2007) Biomacromolecules , vol.8 , pp. 657-662
    • Kuchta, K.1    Chi, L.2    Fuchs, H.3    Pötter, M.4    Steinbüchel, A.5
  • 20
    • 27644482690 scopus 로고    scopus 로고
    • Transcriptional analysis of Ralstonia eutropha genes related to poly-(R)-3-hydroxybutyrate homeostasis during batch fermentation
    • Lawrence, A. G., J. Schoenheit, A. He, J. Tian, P. Liu, J. Stubbe, and A. J. Sinskey. 2005. Transcriptional analysis of Ralstonia eutropha genes related to poly-(R)-3-hydroxybutyrate homeostasis during batch fermentation. Appl. Microbiol. Biotechnol. 68:663-672.
    • (2005) Appl. Microbiol. Biotechnol , vol.68 , pp. 663-672
    • Lawrence, A.G.1    Schoenheit, J.2    He, A.3    Tian, J.4    Liu, P.5    Stubbe, J.6    Sinskey, A.J.7
  • 21
    • 0027032280 scopus 로고
    • Isolation and identification of granule-associated proteins relevant for poly(3-hydroxyalkanoic acid) biosynthesis in Chromatium vinosum D
    • Liebergesell, M., B. Schmidt, and A. Steinbüchel. 1992. Isolation and identification of granule-associated proteins relevant for poly(3-hydroxyalkanoic acid) biosynthesis in Chromatium vinosum D. FEMS Microbiol. Lett. 78:227-232.
    • (1992) FEMS Microbiol. Lett , vol.78 , pp. 227-232
    • Liebergesell, M.1    Schmidt, B.2    Steinbüchel, A.3
  • 22
    • 0030432445 scopus 로고    scopus 로고
    • Electron microscopic observations on the macromolecular organization of the boundary layer of bacterial PHA inclusion bodies
    • Mayer, F., M. H. Madkour, U. Pieper-Fürst, R. Wieczorek, M. Liebergesell, and A. Steinbüchel. 1996. Electron microscopic observations on the macromolecular organization of the boundary layer of bacterial PHA inclusion bodies. J. Gen. Microbiol. 42:445-455.
    • (1996) J. Gen. Microbiol , vol.42 , pp. 445-455
    • Mayer, F.1    Madkour, M.H.2    Pieper-Fürst, U.3    Wieczorek, R.4    Liebergesell, M.5    Steinbüchel, A.6
  • 23
    • 78651166101 scopus 로고
    • Depolymerization of poly-beta-hydroxybutyrate by intracellular enzyme system
    • Merrick, J. M., and M. Doudoroff. 1964. Depolymerization of poly-beta-hydroxybutyrate by intracellular enzyme system. J. Bacteriol. 88:60-71.
    • (1964) J. Bacteriol , vol.88 , pp. 60-71
    • Merrick, J.M.1    Doudoroff, M.2
  • 24
    • 0001630584 scopus 로고
    • Morphological changes in poly-beta-hydroxybutyrate granules associated with decreased susceptibility to enzymatic hydrolysis
    • Merrick, J. M., D. G. Lundgren, and R. M. Pfister. 1965. Morphological changes in poly-beta-hydroxybutyrate granules associated with decreased susceptibility to enzymatic hydrolysis. J. Bacteriol. 89:234-239.
    • (1965) J. Bacteriol , vol.89 , pp. 234-239
    • Merrick, J.M.1    Lundgren, D.G.2    Pfister, R.M.3
  • 25
    • 20444498924 scopus 로고    scopus 로고
    • In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases
    • Peters, V., and B. H. Rehm. 2005. In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases. FEMS Microbiol. Lett. 248:93-100.
    • (2005) FEMS Microbiol. Lett , vol.248 , pp. 93-100
    • Peters, V.1    Rehm, B.H.2
  • 27
    • 0036667428 scopus 로고    scopus 로고
    • Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16
    • Pötter, M., M. H. Madkour, F. Mayer, and A. Steinbüchel. 2002. Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16. Microbiology 148:2413-2426.
    • (2002) Microbiology , vol.148 , pp. 2413-2426
    • Pötter, M.1    Madkour, M.H.2    Mayer, F.3    Steinbüchel, A.4
  • 28
    • 15844385953 scopus 로고    scopus 로고
    • Influence of homologous phasins (PhaP) on PHA accumulation and regulation of their expression by the transcriptional repressor PhaR in Ralstonia eutropha H16
    • Pötter, M., H. Müller, and A. Steinbüchel. 2005. Influence of homologous phasins (PhaP) on PHA accumulation and regulation of their expression by the transcriptional repressor PhaR in Ralstonia eutropha H16. Microbiology 151:825-833.
    • (2005) Microbiology , vol.151 , pp. 825-833
    • Pötter, M.1    Müller, H.2    Steinbüchel, A.3
  • 29
    • 4344627575 scopus 로고    scopus 로고
    • The complex structure of polyhydroxybutyrate (PHB) granules: Four orthologous and paralogous phasins occur in Ralstonia eutropha
    • Pötter, M., H. Müller, F. Reinecke, R. Wieczorek, F. Fricke, B. Bowien, B. Friedrich, and A. Steinbüchel. 2004. The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha. Microbiology 150:2301-2311.
    • (2004) Microbiology , vol.150 , pp. 2301-2311
    • Pötter, M.1    Müller, H.2    Reinecke, F.3    Wieczorek, R.4    Fricke, F.5    Bowien, B.6    Friedrich, B.7    Steinbüchel, A.8
  • 30
    • 33847332519 scopus 로고    scopus 로고
    • Biogenesis and structure of polyhydroxyalkanoate granules
    • J. M. Shively ed, Springer Verlag, Berlin, Germany
    • Pötter, M., and A. Steinbüchel. 2006. Biogenesis and structure of polyhydroxyalkanoate granules, p. 109-136. In J. M. Shively (ed.), Inclusions in prokaryotes, vol. 1. Springer Verlag, Berlin, Germany.
    • (2006) Inclusions in prokaryotes , vol.1 , pp. 109-136
    • Pötter, M.1    Steinbüchel, A.2
  • 31
    • 16344375052 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate) granule-associated proteins: Impacts on poly(3-hydroxybutyrate) synthesis and degradation
    • Pötter, M., and A. Steinbüchel. 2005. Poly(3-hydroxybutyrate) granule-associated proteins: impacts on poly(3-hydroxybutyrate) synthesis and degradation. Biomacromolecules 6:552-560.
    • (2005) Biomacromolecules , vol.6 , pp. 552-560
    • Pötter, M.1    Steinbüchel, A.2
  • 32
    • 0035190694 scopus 로고    scopus 로고
    • Cloning of an intracellular poly[D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product
    • Saegusa, H., M. Shiraki, C. Kanai, and T. Saito. 2001. Cloning of an intracellular poly[D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product. J. Bacteriol. 183:94-100.
    • (2001) J. Bacteriol , vol.183 , pp. 94-100
    • Saegusa, H.1    Shiraki, M.2    Kanai, C.3    Saito, T.4
  • 33
    • 0036379752 scopus 로고    scopus 로고
    • Cloning of an intracellular D(-)-3-hydroxybutyrate-oligomer hydrolase gene from Ralstonia eutropha H16 and identification of the active site serine residue by site-directed mutagenesis
    • Saegusa, H., M. Shiraki, and T. Saito. 2002. Cloning of an intracellular D(-)-3-hydroxybutyrate-oligomer hydrolase gene from Ralstonia eutropha H16 and identification of the active site serine residue by site-directed mutagenesis. J. Biosci. Bioeng. 94:106-112.
    • (2002) J. Biosci. Bioeng , vol.94 , pp. 106-112
    • Saegusa, H.1    Shiraki, M.2    Saito, T.3
  • 34
    • 36549089091 scopus 로고    scopus 로고
    • Saito, T., and T. Kobayashi. 2002. Intracellular degradation of PHAs, p. 23-40. In Y. Doi and A. Steinbüchel (ed.), Biopolymers, 3b. Polyesters II. Wiley-VCH, Weinheim, Germany.
    • Saito, T., and T. Kobayashi. 2002. Intracellular degradation of PHAs, p. 23-40. In Y. Doi and A. Steinbüchel (ed.), Biopolymers, vol. 3b. Polyesters II. Wiley-VCH, Weinheim, Germany.
  • 35
    • 0024248526 scopus 로고
    • Cloning of the Alcaligenes eutrophus genes for synthesis of poly-beta- hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli
    • Schubert, P., A. Steinbuchel, and H. G. Schlegel. 1988. Cloning of the Alcaligenes eutrophus genes for synthesis of poly-beta- hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli. J. Bacteriol. 170:5837-5847.
    • (1988) J. Bacteriol , vol.170 , pp. 5837-5847
    • Schubert, P.1    Steinbuchel, A.2    Schlegel, H.G.3
  • 36
    • 0021027842 scopus 로고
    • A broad host-range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host-range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Biotechnology 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 37
    • 0033037037 scopus 로고    scopus 로고
    • A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds
    • Spiekermann, P., B. H. Rehm, R. Kalscheuer, D. Baumeister, and A. Steinbüchel. 1999. A sensitive, viable-colony staining method using Nile red for direct screening of bacteria that accumulate polyhydroxyalkanoic acids and other lipid storage compounds. Arch. Microbiol. 171:73-80.
    • (1999) Arch. Microbiol , vol.171 , pp. 73-80
    • Spiekermann, P.1    Rehm, B.H.2    Kalscheuer, R.3    Baumeister, D.4    Steinbüchel, A.5
  • 39
    • 0035234192 scopus 로고    scopus 로고
    • Biochemical and molecular basis of microbial synthesis of polyhydroxyalkanoates in microorganisms
    • Steinbüchel, A., and S. Hein. 2001. Biochemical and molecular basis of microbial synthesis of polyhydroxyalkanoates in microorganisms. Adv. Biochem. Eng. Biotechnol. 71:81.
    • (2001) Adv. Biochem. Eng. Biotechnol , vol.71 , pp. 81
    • Steinbüchel, A.1    Hein, S.2
  • 41
    • 0142059593 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate (PHA) homeostasis: The role of PHA synthase
    • Stubbe, J., and J. Tian. 2003. Polyhydroxyalkanoate (PHA) homeostasis: the role of PHA synthase. Nat. Prod. Rep. 20:445-457.
    • (2003) Nat. Prod. Rep , vol.20 , pp. 445-457
    • Stubbe, J.1    Tian, J.2
  • 42
    • 22244459223 scopus 로고    scopus 로고
    • Nontemplate-dependent polymerization processes: Polyhydroxyalkanoate synthases as a paradigm
    • Stubbe, J., J. Tian, A. He, A. J. Sinskey, A. G. Lawrence, and P. Liu. 2005. Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm. Annu. Rev. Biochem. 74:433-480.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 433-480
    • Stubbe, J.1    Tian, J.2    He, A.3    Sinskey, A.J.4    Lawrence, A.G.5    Liu, P.6
  • 43
    • 0029006910 scopus 로고
    • Turnover of poly(3-hydroxybutyrate) (PHB) and its influence on the molecular mass of the polymer accumulated by Alcaligenes eutrophus during batch culture
    • Taidi, B., D. Mansfield, and A. J. Anderson. 1995. Turnover of poly(3-hydroxybutyrate) (PHB) and its influence on the molecular mass of the polymer accumulated by Alcaligenes eutrophus during batch culture. FEMS Microbiol. Lett. 129:201-206.
    • (1995) FEMS Microbiol. Lett , vol.129 , pp. 201-206
    • Taidi, B.1    Mansfield, D.2    Anderson, A.J.3
  • 44
    • 33646347413 scopus 로고    scopus 로고
    • Thiolysis of poly(3- hydroxybutyrate) with polyhydroxyalkanoate synthase from Ralstonia eutropha
    • Uchino, K., and T. Saito. 2006. Thiolysis of poly(3- hydroxybutyrate) with polyhydroxyalkanoate synthase from Ralstonia eutropha. J. Biochem. (Tokyo) 139:615-621.
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 615-621
    • Uchino, K.1    Saito, T.2
  • 45
    • 0343930745 scopus 로고    scopus 로고
    • Occurrence of polyhydroxyalkanoic acid granule-associated proteins related to the Alcaligenes eutrophus H16 GA24 protein in other bacteria
    • Wieczorek, R., A. Steinbüchel, and B. Schmidt. 1996. Occurrence of polyhydroxyalkanoic acid granule-associated proteins related to the Alcaligenes eutrophus H16 GA24 protein in other bacteria. FEMS Microbiol. Lett. 135:23-30.
    • (1996) FEMS Microbiol. Lett , vol.135 , pp. 23-30
    • Wieczorek, R.1    Steinbüchel, A.2    Schmidt, B.3
  • 46
    • 0034977798 scopus 로고    scopus 로고
    • Accumulation of the PhaP phasin of Ralstonia eutropha is dependent on production of polyhydroxybutyrate in cells
    • York, G. M., B. H. Junker, J. A. Stubbe, and A. J. Sinskey. 2001. Accumulation of the PhaP phasin of Ralstonia eutropha is dependent on production of polyhydroxybutyrate in cells. J. Bacteriol. 183:4217-4226.
    • (2001) J. Bacteriol , vol.183 , pp. 4217-4226
    • York, G.M.1    Junker, B.H.2    Stubbe, J.A.3    Sinskey, A.J.4
  • 47
    • 0037701554 scopus 로고    scopus 로고
    • Ralstonia eutropha H16 encodes two and possibly three intracellular poly[D-(-)-3-hydroxybutyrate] depolymerase genes
    • York, G. M., J. Lupberger, J. Tian, A. G. Lawrence, J. Stubbe, and A. J. Sinskey. 2003. Ralstonia eutropha H16 encodes two and possibly three intracellular poly[D-(-)-3-hydroxybutyrate] depolymerase genes. J. Bacteriol. 185:3788-3794.
    • (2003) J. Bacteriol , vol.185 , pp. 3788-3794
    • York, G.M.1    Lupberger, J.2    Tian, J.3    Lawrence, A.G.4    Stubbe, J.5    Sinskey, A.J.6
  • 48
    • 0036136119 scopus 로고    scopus 로고
    • The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production
    • York, G. M., J. Stubbe, and A. J. Sinskey. 2002. The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production. J. Bacteriol. 184:59-66.
    • (2002) J. Bacteriol , vol.184 , pp. 59-66
    • York, G.M.1    Stubbe, J.2    Sinskey, A.J.3


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