메뉴 건너뛰기




Volumn 181, Issue 5, 1999, Pages 1429-1435

Analysis of 4-phosphopantetheinylation of polyhydroxybutyrate synthase from Ralstonia eutropha: Generation of β-alanine auxotrophic Tn5 mutants and cloning of the panD gene region

Author keywords

[No Author keywords available]

Indexed keywords

BETA ALANINE; POLY(3 HYDROXYBUTYRIC ACID); SYNTHETASE;

EID: 0033049830     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.5.1429-1435.1999     Document Type: Article
Times cited : (28)

References (39)
  • 1
    • 0023749235 scopus 로고
    • Pseudomonas oleovorans as a source of poly(β-hydroxyalkanoates) for potential applications as biodegradable polyesters
    • Brandl, H., R. A. Gross, R. W. Lenz, and R. C. Fuller. 1988. Pseudomonas oleovorans as a source of poly(β-hydroxyalkanoates) for potential applications as biodegradable polyesters. Appl. Environ. Microbiol. 54:1977-1982.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1977-1982
    • Brandl, H.1    Gross, R.A.2    Lenz, R.W.3    Fuller, R.C.4
  • 2
    • 84954963239 scopus 로고
    • The metabolism of pantothenic acid
    • Brown, G. M. 1959. The metabolism of pantothenic acid. J. Biol. Chem. 234: 370-378.
    • (1959) J. Biol. Chem. , vol.234 , pp. 370-378
    • Brown, G.M.1
  • 3
    • 0018838186 scopus 로고
    • β-Alanine synthesis in Escherichia coli
    • Cronan, J. 1980. β-Alanine synthesis in Escherichia coli. J. Bacteriol. 141: 1291-1297.
    • (1980) J. Bacteriol. , vol.141 , pp. 1291-1297
    • Cronan, J.1
  • 4
    • 0020003603 scopus 로고
    • Genetic and biochemical analysis of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium
    • Cronan, J. E., Jr., K. J. Littel, and S. Jackowsky. 1982. Genetic and biochemical analysis of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 149:916-922.
    • (1982) J. Bacteriol. , vol.149 , pp. 916-922
    • Cronan J.E., Jr.1    Littel, K.J.2    Jackowsky, S.3
  • 5
    • 0014409414 scopus 로고
    • Acyl carrier protein. X. Acyl carrier protein synthetase
    • Elovson, J., and D. Vegelos. 1968. Acyl carrier protein. X. Acyl carrier protein synthetase. J. Biol. Chem. 243:3603-3611.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3603-3611
    • Elovson, J.1    Vegelos, D.2
  • 6
    • 0030738431 scopus 로고    scopus 로고
    • Enterobactin biosynthesis in Escherichia coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate
    • Gehring, A. M., K. A. Bradley, and C. T. Walsh. 1997. Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Biochemistry 36:8495-8503.
    • (1997) Biochemistry , vol.36 , pp. 8495-8503
    • Gehring, A.M.1    Bradley, K.A.2    Walsh, C.T.3
  • 7
    • 0027933456 scopus 로고
    • Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: Evidence for a required posttranslational modification for catalytic activity
    • Gerngross, T. U., K. D. Snell, O. P. Peoples, and A. J. Sinskey. 1994. Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity. Biochemistry 33:9311-9320.
    • (1994) Biochemistry , vol.33 , pp. 9311-9320
    • Gerngross, T.U.1    Snell, K.D.2    Peoples, O.P.3    Sinskey, A.J.4
  • 8
    • 0029130956 scopus 로고
    • The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli
    • Glavas, N. A., and P. D. Bragg. 1995. The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochim. Biophys. Acta 1231:297-303.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 297-303
    • Glavas, N.A.1    Bragg, P.D.2
  • 9
    • 0021111879 scopus 로고
    • Compilation and analysis of Escherichia coli promoter DNA sequences
    • Hawley, D. K., and W. R. McClure. 1983. Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res. 11:2237-2255.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 2237-2255
    • Hawley, D.K.1    McClure, W.R.2
  • 10
    • 0019812065 scopus 로고
    • Regulation of coenzyme A biosynthesis
    • Jackowski, S., and C. O. Rock. 1981. Regulation of coenzyme A biosynthesis. J. Bacteriol. 148:926-932.
    • (1981) J. Bacteriol. , vol.148 , pp. 926-932
    • Jackowski, S.1    Rock, C.O.2
  • 11
    • 0021186069 scopus 로고
    • Metabolism of 4′-phosphopantetheine in Escherichia coli
    • Jackowski, S., and C. O. Rock. 1984. Metabolism of 4′-phosphopantetheine in Escherichia coli. J. Bacteriol. 158:115-120.
    • (1984) J. Bacteriol. , vol.158 , pp. 115-120
    • Jackowski, S.1    Rock, C.O.2
  • 12
    • 0022626960 scopus 로고
    • Consequences of reduced intracellular coenzyme A content in Escherichia coli
    • Jackowski, S., and C. O. Rock. 1986. Consequences of reduced intracellular coenzyme A content in Escherichia coli. J. Bacteriol. 166:866-871.
    • (1986) J. Bacteriol. , vol.166 , pp. 866-871
    • Jackowski, S.1    Rock, C.O.2
  • 13
    • 0027405409 scopus 로고
    • Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme
    • Jones, C. E., J. M. Brook, D. Buck, C. Abell, and A. G. Smith. 1993. Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme. J. Bacteriol. 175:2125-2130.
    • (1993) J. Bacteriol. , vol.175 , pp. 2125-2130
    • Jones, C.E.1    Brook, J.M.2    Buck, D.3    Abell, C.4    Smith, A.G.5
  • 14
    • 0019904249 scopus 로고
    • Wide host range cloning vectors: A cosmid clone bank of an Agrobacterium Ti plasmid
    • Knauf, V. C., and E. W. Nester. 1982. Wide host range cloning vectors: a cosmid clone bank of an Agrobacterium Ti plasmid. Plasmid 8:4-54.
    • (1982) Plasmid , vol.8 , pp. 4-54
    • Knauf, V.C.1    Nester, E.W.2
  • 15
    • 0028793123 scopus 로고
    • Four new derivatives of the broad host range cloning vector pBBRIMCS, carrying different antibiotic resistence cassettes
    • Kovach, M. E. 1945. Four new derivatives of the broad host range cloning vector pBBRIMCS, carrying different antibiotic resistence cassettes. Gene 166:175-176.
    • (1945) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1
  • 17
    • 0028577728 scopus 로고
    • Targeting of the polyhydroxybutyrate biosynthetic pathway to the plastids of Arabidopsis thaliana results in high levels of polymer accumulation
    • Nawrath, C., Y. Poirier, and C. Somerville. 1994. Targeting of the polyhydroxybutyrate biosynthetic pathway to the plastids of Arabidopsis thaliana results in high levels of polymer accumulation. Proc. Natl. Acad. Sci. USA 91:12760-12764.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12760-12764
    • Nawrath, C.1    Poirier, Y.2    Somerville, C.3
  • 18
    • 0024466118 scopus 로고
    • Characterisation of recombinant thioesterase and acyl carrier protein domains of chicken acid synthase expressed in Escherichia coli
    • Pazirandeh, M., S. S. Chirala, W. H. Huang, and S. J. Wakil. 1989. Characterisation of recombinant thioesterase and acyl carrier protein domains of chicken acid synthase expressed in Escherichia coli. J. Biol. Chem. 264: 18195-18201.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18195-18201
    • Pazirandeh, M.1    Chirala, S.S.2    Huang, W.H.3    Wakil, S.J.4
  • 19
    • 0024445845 scopus 로고
    • Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Characterisation of the genes encoding β-ketothiolase and acetoacetyl-CoA reductase
    • Peoples, O. P., and A. J. Sinskey. 1989. Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Characterisation of the genes encoding β-ketothiolase and acetoacetyl-CoA reductase. J. Biol. Chem. 264: 15293-15297.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15293-15297
    • Peoples, O.P.1    Sinskey, A.J.2
  • 20
    • 0024425823 scopus 로고
    • Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes europhus H16. Identification and characterisation of the PHB polymerase gene (phaC)
    • Peoples, O. P., and A. J. Sinskey. 1989. Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes europhus H16. Identification and characterisation of the PHB polymerase gene (phaC) J. Biol. Chem. 264:15298-15303.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15298-15303
    • Peoples, O.P.1    Sinskey, A.J.2
  • 21
    • 0025863049 scopus 로고
    • Biosynthesis of Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF and analysis of covalent phosphopantetheine
    • Rusnak, F., M. Sakaitani, D. Drueckhammer, J. Reichert, and C. T. Walsh. 1991. Biosynthesis of Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF and analysis of covalent phosphopantetheine. Biochemistry 30:2916-2927.
    • (1991) Biochemistry , vol.30 , pp. 2916-2927
    • Rusnak, F.1    Sakaitani, M.2    Drueckhammer, D.3    Reichert, J.4    Walsh, C.T.5
  • 24
    • 0024248526 scopus 로고
    • Cloning of the Alcaligenes eutrophus genes for synthesis of poly-β-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli
    • Schubert, A., A. Steinbüchel, and H. G. Schlegel. 1988. Cloning of the Alcaligenes eutrophus genes for synthesis of poly-β-hydroxybutyric acid (PHB) and synthesis of PHB in Escherichia coli. J. Bacteriol. 170:283-294.
    • (1988) J. Bacteriol. , vol.170 , pp. 283-294
    • Schubert, A.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 25
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16 S ribosomal RNA: Complementary to nonsense triplets and ribosome binding sites
    • Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16 S ribosomal RNA: complementary to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71:1313-1342.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1313-1342
    • Shine, J.1    Dalgarno, L.2
  • 26
    • 0002433715 scopus 로고
    • Vector plasmids for in vivo and in vitro manipulations of Gram-negative bacteria
    • A. Pühler (ed.), Springer Verlag KG, Berlin, Germany
    • Simon, R., U. Priefer, and A. Pühler. 1983. Vector plasmids for in vivo and in vitro manipulations of Gram-negative bacteria, p. 98-106. In A. Pühler (ed.), Molecular genetics of the bacteria plant interaction. Springer Verlag KG, Berlin, Germany.
    • (1983) Molecular Genetics of the Bacteria Plant Interaction , pp. 98-106
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 27
    • 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. 1993. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Bio/Technology 1:784-791.
    • (1993) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 28
    • 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
    • in press
    • Spiekermann, P., B. H. A. Rehm, R. Kalscheuer, D. Baumeister, and A. Steinbüchel. 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., in press.
    • Arch. Microbiol.
    • Spiekermann, P.1    Rehm, B.H.A.2    Kalscheuer, R.3    Baumeister, D.4    Steinbüchel, A.5
  • 29
    • 0019997397 scopus 로고
    • Mutagenesis of Alcaligenes eutrophus by insertion of drug-resistence transposon Tn5
    • Srivastava, S., M. Urban, and B. Friedrich. 1982. Mutagenesis of Alcaligenes eutrophus by insertion of drug-resistence transposon Tn5. Arch. Microbiol. 131:203-207.
    • (1982) Arch. Microbiol. , vol.131 , pp. 203-207
    • Srivastava, S.1    Urban, M.2    Friedrich, B.3
  • 30
    • 0029018968 scopus 로고
    • Diversity of microbial polyhydroxyalkanoic acids
    • Steinbüchel, A., and H. E. Valentin. 1995. Diversity of microbial polyhydroxyalkanoic acids. FEMS Microbiol. Lett. 128:219-228.
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 219-228
    • Steinbüchel, A.1    Valentin, H.E.2
  • 32
  • 33
    • 0025002088 scopus 로고
    • Formation of polyesters consisting of medium-chain-length 3-hydroxyalkanoic acid from gluconate by Pseudomonas aeruginosa and other fluorescent pseudomonads
    • Timm, A., and A. Steinbüchel. 1990. Formation of polyesters consisting of medium-chain-length 3-hydroxyalkanoic acid from gluconate by Pseudomonas aeruginosa and other fluorescent pseudomonads. Appl. Environ. Microbiol. 56:3360-3367.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3360-3367
    • Timm, A.1    Steinbüchel, A.2
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0028078896 scopus 로고
    • Application of enzymatically synthesized short-chain-length hydroxy fatty acid coenzyme A thioesters for assay of polyhydroxyalkanoic acid synthases
    • Valentin, H. E., and A. Steinbüchel. 1994. Application of enzymatically synthesized short-chain-length hydroxy fatty acid coenzyme A thioesters for assay of polyhydroxyalkanoic acid synthases. Appl. Microbiol. Biotechnol. 40:699-709.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 699-709
    • Valentin, H.E.1    Steinbüchel, A.2
  • 36
    • 0016662195 scopus 로고
    • Ketopantoic acid and ketopantoyl lactone reductases
    • Wilken, D. R., H. L. King, Jr., and R. E. Dyar. 1975. Ketopantoic acid and ketopantoyl lactone reductases, J. Biol. Chem. 259:2311-2314.
    • (1975) J. Biol. Chem. , vol.259 , pp. 2311-2314
    • Wilken, D.R.1    King H.L., Jr.2    Dyar, R.E.3
  • 37
    • 0018696728 scopus 로고
    • Purification and properties of L-aspartate-1-decarboxylase, an enzyme that catalyzes the formation β-alanine in Escherichia coi
    • Williamson, J. M., and G. Brown. 1979. Purification and properties of L-aspartate-1-decarboxylase, an enzyme that catalyzes the formation β-alanine in Escherichia coi. J. Biol. Chem. 254:8074-8082.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8074-8082
    • Williamson, J.M.1    Brown, G.2
  • 39
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp8 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp8 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.