메뉴 건너뛰기




Volumn 142, Issue 6, 1996, Pages 1459-1468

Molecular characterization of a chromosomal region involved in the oxidation of acetyl-CoA to glyoxylate in the isocitrate-lyase-negative methylotroph Methylobacterium extorquens AM1

Author keywords

Acetyl CoA oxidation; C1 and C2 metabolism; Isocitrate lyase negative methylotrophs; Methylobacterium extorquens; Serine cycle

Indexed keywords

ACETYL COENZYME A; ALCOHOL DEHYDROGENASE; CARBOXYLASE; CATALASE; COBAMAMIDE; GLYCOLIC ACID; GLYOXYLIC ACID; ISOCITRATE LYASE; ISOMERASE; MUTASE; OXIDOREDUCTASE;

EID: 0029955349     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-6-1459     Document Type: Article
Times cited : (41)

References (57)
  • 2
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R. F., Jr & Seizer, W. (1952). A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195, 133-140.
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beers Jr., R.F.1    Seizer, W.2
  • 5
    • 0025720743 scopus 로고
    • The isolation, cloning and identification of a vegetative catalase gene from Bacillus subtilis
    • Bol, D. K. & Yasbin, R. E. (1991). The isolation, cloning and identification of a vegetative catalase gene from Bacillus subtilis. Gene 109, 31-37.
    • (1991) Gene , vol.109 , pp. 31-37
    • Bol, D.K.1    Yasbin, R.E.2
  • 6
    • 0028216615 scopus 로고
    • Genetic organization of the mau gene cluster in Methylobacterisim extorquens AM1: Complete nucleotide sequence and generation and characteristics of mau mutants
    • Chistoserdov, A. Y, Chistoserdova, L. V., McIntire, W. S. & Lidstrom, M. E. (1994). Genetic organization of the mau gene cluster in Methylobacterisim extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants. J Bacteriol 176, 4052-4065.
    • (1994) J Bacteriol , vol.176 , pp. 4052-4065
    • Chistoserdov, A.Y.1    Chistoserdova, L.V.2    McIntire, W.S.3    Lidstrom, M.E.4
  • 7
    • 0025838326 scopus 로고
    • Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1
    • Chistoserdova, L. V. & Lidstrom, M. E. (1991). Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1. J Bacteriol 173, 7228-7232.
    • (1991) J Bacteriol , vol.173 , pp. 7228-7232
    • Chistoserdova, L.V.1    Lidstrom, M.E.2
  • 8
    • 0026524498 scopus 로고
    • Cloning, mutagenesis, and physiological effect of a hydroxypyruvate reductase gene from Methylobacterium extorquens AM1
    • Chistoserdova, L. & Lidstrom, M. E. (1992). Cloning, mutagenesis, and physiological effect of a hydroxypyruvate reductase gene from Methylobacterium extorquens AM1. J Bacteriol 174, 71-77.
    • (1992) J Bacteriol , vol.174 , pp. 71-77
    • Chistoserdova, L.1    Lidstrom, M.E.2
  • 9
    • 0028215037 scopus 로고
    • Genetics of the serine cycle in Methylobacterium extorquens AM1: Identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA
    • Chistoserdova, L. V. & Lidstrom, M. E. (1994a). Genetics of the serine cycle in Methylobacterium extorquens AM1: identification of sgaA and mtdA and sequences of sgaA, hprA, and mtdA. J Bacteriol 176, 1957-1968.
    • (1994) J Bacteriol , vol.176 , pp. 1957-1968
    • Chistoserdova, L.V.1    Lidstrom, M.E.2
  • 10
    • 0028172819 scopus 로고
    • Genetics of the serine cycle in M. extorquens AM1: Cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase
    • Chistoserdova, L. V. & Lidstrom, M. E. (1994b). Genetics of the serine cycle in M. extorquens AM1: cloning, sequence, mutation, and physiological effect of glyA, the gene for serine hydroxymethyltransferase. J Bacteriol 176, 6759-6763.
    • (1994) J Bacteriol , vol.176 , pp. 6759-6763
    • Chistoserdova, L.V.1    Lidstrom, M.E.2
  • 12
    • 0026754531 scopus 로고
    • Analysis of the Escherichia coli genome - DNA sequence of the region from 84.5 to 86.5 minutes
    • Daniels, D. L., Plunket, G., III, Burland, V. D. & Blattner F. R. (1992). Analysis of the Escherichia coli genome - DNA sequence of the region from 84.5 to 86.5 minutes. Science 257, 771-778.
    • (1992) Science , vol.257 , pp. 771-778
    • Daniels, D.L.1    Plunket III, G.2    Burland, V.D.3    Blattner, F.R.4
  • 14
    • 0022000283 scopus 로고
    • Plasmids related to the broad host range vector, pRK290, useful for gene cloning and monitoring gene expression
    • Ditta, G., Schmidhauser, T., Yakobson, F., Lu, P., Liang, X., Finlay, D., Guiney, D. & Helinski, D. (1985). Plasmids related to the broad host range vector, pRK290, useful for gene cloning and monitoring gene expression. Plasmid 13, 149-153.
    • (1985) Plasmid , vol.13 , pp. 149-153
    • Ditta, G.1    Schmidhauser, T.2    Yakobson, F.3    Lu, P.4    Liang, X.5    Finlay, D.6    Guiney, D.7    Helinski, D.8
  • 15
    • 0015608445 scopus 로고
    • 1 compounds, ethanol and β-hydroxybutyrate
    • 1 compounds, ethanol and β-hydroxybutyrate. Biochem J 132, 797-801.
    • (1973) Biochem J , vol.132 , pp. 797-801
    • Dunstan, P.M.1    Anthony, C.2
  • 16
    • 0015349090 scopus 로고
    • 2 compounds. The involvement of glycollate in the metabolism of ethanol and of acetate by Pseudomonas AM1
    • 2 compounds. The involvement of glycollate in the metabolism of ethanol and of acetate by Pseudomonas AM1. Biochem J 128, 99-106.
    • (1972) Biochem J , vol.128 , pp. 99-106
    • Dunstan, P.M.1    Anthony, C.2    Drabble, W.T.3
  • 18
    • 0022546251 scopus 로고
    • The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii
    • Francalanci, F., Davis, N. K., Fuller, J. Q., Murfitt, D. & Leadlay, P. F. (1986). The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii. Biochem J 236, 489-494.
    • (1986) Biochem J , vol.236 , pp. 489-494
    • Francalanci, F.1    Davis, N.K.2    Fuller, J.Q.3    Murfitt, D.4    Leadlay, P.F.5
  • 20
    • 0026781514 scopus 로고
    • Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis
    • Godon, J.-J., Chopin, M.-C. & Ehrlich, S. D. (1992). Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis. J Bacteriol 174, 6580-6589.
    • (1992) J Bacteriol , vol.174 , pp. 6580-6589
    • Godon, J.-J.1    Chopin, M.-C.2    Ehrlich, S.D.3
  • 22
    • 0023189082 scopus 로고
    • Comparison of the cis-acting control regions of two coordinately controlled genes involved in ethanol utilization in Aspergillus nidulans
    • Gwynne, D. I., Buxton, F. P., Sibley, S., Davies, R. W., Lockington, R. A., Scazzocchio, C & Sealy-Lewis, H. M. (1987). Comparison of the cis-acting control regions of two coordinately controlled genes involved in ethanol utilization in Aspergillus nidulans. Gene 51, 205-216.
    • (1987) Gene , vol.51 , pp. 205-216
    • Gwynne, D.I.1    Buxton, F.P.2    Sibley, S.3    Davies, R.W.4    Lockington, R.A.5    Scazzocchio, C.6    Sealy-Lewis, H.M.7
  • 23
    • 0000011010 scopus 로고
    • Methanol assimilation by Hyphoraicrobiurti spp
    • Harder, W., Attwood, M. & Quayle, J. R. (1973). Methanol assimilation by Hyphoraicrobiurti spp. J Gen Micrabiol 78, 155-163.
    • (1973) J Gen Micrabiol , vol.78 , pp. 155-163
    • Harder, W.1    Attwood, M.2    Quayle, J.R.3
  • 24
    • 0024287984 scopus 로고
    • Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coll
    • Heilmann, H. J., Magert, H. J. & Gassen, H. G. (1988). Identification and isolation of glucose dehydrogenase genes of Bacillus megaterium M1286 and their expression in Escherichia coll. Eur J Biochem 174, 485-490.
    • (1988) Eur J Biochem , vol.174 , pp. 485-490
    • Heilmann, H.J.1    Magert, H.J.2    Gassen, H.G.3
  • 25
    • 0024618232 scopus 로고
    • Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction
    • Jansen, R., Kalousek, F., Fenton, W. A., Rosenberg, L. E. & Ledley, F. D. (1989). Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. Genomics 4, 198-205.
    • (1989) Genomics , vol.4 , pp. 198-205
    • Jansen, R.1    Kalousek, F.2    Fenton, W.A.3    Rosenberg, L.E.4    Ledley, F.D.5
  • 26
    • 0017724572 scopus 로고
    • A new spectrophotometric assay for protein in cell extracts
    • Kalb, V. F. & Bernlohr R. W. (1977). A new spectrophotometric assay for protein in cell extracts. Anal Biochem 82, 362-371.
    • (1977) Anal Biochem , vol.82 , pp. 362-371
    • Kalb, V.F.1    Bernlohr, R.W.2
  • 27
    • 0026719344 scopus 로고
    • Isolation and characterization of a cDNA from Cuphea lanceolata encoding a β-ketoacyl-ACP reductase
    • Klein, B., Pawlovski, K., Horicke-Grandpierre, C., Schell, J. & Topfer, R. (1992): Isolation and characterization of a cDNA from Cuphea lanceolata encoding a β-ketoacyl-ACP reductase. Mol Gen Genet 233, 122-128.
    • (1992) Mol Gen Genet , vol.233 , pp. 122-128
    • Klein, B.1    Pawlovski, K.2    Horicke-Grandpierre, C.3    Schell, J.4    Topfer, R.5
  • 29
    • 0342453448 scopus 로고
    • Isolation of cDNA clones coding for the α and β chains of human propionyl-Co a carboxylase: Chromosomal assignments and DNA polymorphisms associated with pccA and pccB genes
    • Lamhonwah, A.-M., Barankiewicz, T. J., Willard, H. F., Mahuran, D. J., Quan, F. & Gravel, R. A. (1986). Isolation of cDNA clones coding for the α and β chains of human propionyl-Co A carboxylase: chromosomal assignments and DNA polymorphisms associated with pccA and pccB genes. Proc Natl Acad Sci USA 83, 4864-4868.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4864-4868
    • Lamhonwah, A.-M.1    Barankiewicz, T.J.2    Willard, H.F.3    Mahuran, D.J.4    Quan, F.5    Gravel, R.A.6
  • 30
    • 0022447232 scopus 로고
    • Characterization of the developrnentally regulated Bacillus subtilis glucose dehydrogenase gene
    • Lampel, K., Uratani, B., Chaudhry, G., Ramaley, R. & Rudikoff, S. (1986). Characterization of the developrnentally regulated Bacillus subtilis glucose dehydrogenase gene. J Bacteriol 166, 238-243.
    • (1986) J Bacteriol , vol.166 , pp. 238-243
    • Lampel, K.1    Uratani, B.2    Chaudhry, G.3    Ramaley, R.4    Rudikoff, S.5
  • 32
    • 0014105807 scopus 로고
    • Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe
    • Megnet, R. (1967). Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe. Arch Biochem Biophys 121, 194-201.
    • (1967) Arch Biochem Biophys , vol.121 , pp. 194-201
    • Megnet, R.1
  • 33
    • 0021431375 scopus 로고
    • Hybridization of nucleic acids immobilized on solid supports
    • Meinkoth, J. & Wahl, G. (1984). Hybridization of nucleic acids immobilized on solid supports. Anal Biochem 138, 267-284.
    • (1984) Anal Biochem , vol.138 , pp. 267-284
    • Meinkoth, J.1    Wahl, G.2
  • 35
    • 0025294383 scopus 로고
    • cDNA and deduced amino acid sequence of Drosophila catalase
    • Orr, E. C., Bewley, G. C. & Orr, W. C. (1990). cDNA and deduced amino acid sequence of Drosophila catalase. Nucleic Acids Res 18, 3663.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3663
    • Orr, E.C.1    Bewley, G.C.2    Orr, W.C.3
  • 36
    • 0001031422 scopus 로고
    • 1 compounds: Isolation and characterization of Pseudomonas AM1
    • 1 compounds: isolation and characterization of Pseudomonas AM1. Biochem J 81, 465-469.
    • (1961) Biochem J , vol.81 , pp. 465-469
    • Peel, D.1    Quayle, J.R.2
  • 37
    • 0024633628 scopus 로고
    • Fine structure analysis of the Zoogloea ramigera phbA-phbB locus encoding β-ketothiolase and acetoacetyl-CoA reductase
    • Peoples, O. P. & Sinskey, A. J. (1989). Fine structure analysis of the Zoogloea ramigera phbA-phbB locus encoding β-ketothiolase and acetoacetyl-CoA reductase. Nucleotide sequence of phbB. Mol Microbiol 3, 349-357.
    • (1989) Nucleotide Sequence of PhbB. Mol Microbiol , vol.3 , pp. 349-357
    • Peoples, O.P.1    Sinskey, A.J.2
  • 38
    • 0020529722 scopus 로고
    • Nucleotide sequence of the yeast alcohol dehydrogenase II gene
    • Russell, D. W., Smith, M., Williamson, V. M. & Young, E. T. (1983). Nucleotide sequence of the yeast alcohol dehydrogenase II gene. J Biol Chem 258, 2674-2682
    • (1983) J Biol Chem , vol.258 , pp. 2674-2682
    • Russell, D.W.1    Smith, M.2    Williamson, V.M.3    Young, E.T.4
  • 39
    • 0020663608 scopus 로고
    • The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharomyces pombe
    • Russell, P. & Hall, B. D. (1983). The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharomyces pombe. J Biol Chem 258, 143-149.
    • (1983) J Biol Chem , vol.258 , pp. 143-149
    • Russell, P.1    Hall, B.D.2
  • 40
    • 0019365279 scopus 로고
    • A general method for site-directed mutagenesis in procaryotes
    • Ruvkun, G. B. & Ausubel, J. R. (1981). A general method for site-directed mutagenesis in procaryotes. Nature 289, 85-88.
    • (1981) Nature , vol.289 , pp. 85-88
    • Ruvkun, G.B.1    Ausubel, J.R.2
  • 41
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H. & Miura, K.-I. (1963). Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72, 619-629.
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.-I.2
  • 42
    • 0015138225 scopus 로고
    • Mutants of Pseudomonas AM1 that require glycollate or glyoxylate for growth on methanol and ethanol
    • Salem, A. R. & Quayle, J. R. (1971). Mutants of Pseudomonas AM1 that require glycollate or glyoxylate for growth on methanol and ethanol. Biochem J 124, 74P.
    • (1971) Biochem J , vol.124
    • Salem, A.R.1    Quayle, J.R.2
  • 43
    • 0015836680 scopus 로고
    • The metabolism of lactate and pyruvate by Pseudomonas AM1
    • Salem, A. R., Wagner, C., Hacking, A. J. & Quayle, J. R. (1973). The metabolism of lactate and pyruvate by Pseudomonas AM1. J Gen Microbiol 76, 375-388.
    • (1973) J Gen Microbiol , vol.76 , pp. 375-388
    • Salem, A.R.1    Wagner, C.2    Hacking, A.J.3    Quayle, J.R.4
  • 44
    • 0025425353 scopus 로고
    • The alcohol dehydrogenase system in the yeast, Kluyveromyces lactis
    • Saliola, M., Shuster, J. R. & Falcone, C. (1990). The alcohol dehydrogenase system in the yeast, Kluyveromyces lactis. Yeast 6, 193-204.
    • (1990) Yeast , vol.6 , pp. 193-204
    • Saliola, M.1    Shuster, J.R.2    Falcone, C.3
  • 46
    • 0001440833 scopus 로고
    • 12 in a methanol-utilizing bacterium, Protaminobacter ruber
    • Edited by R. L. Crawford & R. S. Hanson. Washington, DC: American Society for Microbiology
    • 1 Compounds, pp. 113-117. Edited by R. L. Crawford & R. S. Hanson. Washington, DC: American Society for Microbiology.
    • (1984) 1 Compounds , pp. 113-117
    • Shimizu, S.1    Ueda, S.2    Sato, K.3
  • 47
    • 0002433715 scopus 로고
    • Vector plasmids for in vivo manipulations of Gram-negative bacteria
    • Edited by A. Puhler. Berlin: Springer-Verlag
    • Simon, R., Priefer, U. & Puhler, A. (1983). Vector plasmids for in vivo manipulations of Gram-negative bacteria. In: Molecular Genetics of the Bacteria-Plant Interactions, pp. 98-106. Edited by A. Puhler. Berlin: Springer-Verlag.
    • (1983) Molecular Genetics of the Bacteria-Plant Interactions , pp. 98-106
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 48
    • 0026589576 scopus 로고
    • Molecular cloning of higher plant 3-oxoacyl (acyl carrier protein) reductase. Sequence identities with the nodG gene product of the nitrogen-fixing soil bacterium Rhizobium meliloti
    • Slabas, A. R., Chase, D., Nishida, I., Murata, N., Sidebottom, C., Safford, R., Sheldon, P. S., Kekwick, R. G. O., Hardie, D. G. & Mackintosh, R. W. (1992). Molecular cloning of higher plant 3-oxoacyl (acyl carrier protein) reductase. Sequence identities with the nodG gene product of the nitrogen-fixing soil bacterium Rhizobium meliloti. Biochem J 283, 321-326.
    • (1992) Biochem J , vol.283 , pp. 321-326
    • Slabas, A.R.1    Chase, D.2    Nishida, I.3    Murata, N.4    Sidebottom, C.5    Safford, R.6    Sheldon, P.S.7    Kekwick, R.G.O.8    Hardie, D.G.9    Mackintosh, R.W.10
  • 49
    • 8944232389 scopus 로고
    • Complementation analysis of mutants defective in the conversion of acetyl-CoA to glyoxylate in Methylobacterium extorquens AM1
    • Warwick, England
    • 1 Compounds, B54. Warwick, England
    • (1992) 1 Compounds
    • Smith, L.M.1    Goodwin, P.M.2
  • 51
    • 0011488675 scopus 로고
    • Characterization and complementation of mutants of Methylobaeterium AM1 which are defective in C-1 assimilation
    • Stone, S. & Goodwin, P. M. (1989). Characterization and complementation of mutants of Methylobaeterium AM1 which are defective in C-1 assimilation. J Gen Microbiol 135, 227-235.
    • (1989) J Gen Microbiol , vol.135 , pp. 227-235
    • Stone, S.1    Goodwin, P.M.2
  • 52
    • 0027181983 scopus 로고
    • 2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle
    • 2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur J Biochem 215, 633-643.
    • (1993) Eur J Biochem , vol.215 , pp. 633-643
    • Strauss, G.1    Fuchs, G.2
  • 53
    • 0025020587 scopus 로고
    • 16S ribosomal RNA sequence analysis for determination of phylogenetic relationship among methylotrophs
    • Tsuji, K., Tsien, H. C., Hanson, R. S., DePalma, S. R., Scholtz, R. & LaRoche, S. (1990). 16S ribosomal RNA sequence analysis for determination of phylogenetic relationship among methylotrophs. J Gen Microbiol 136, 1-10.
    • (1990) J Gen Microbiol , vol.136 , pp. 1-10
    • Tsuji, K.1    Tsien, H.C.2    Hanson, R.S.3    DePalma, S.R.4    Scholtz, R.5    LaRoche, S.6
  • 54
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J. & Messing, J. (1982). The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19, 259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 55
    • 0019293885 scopus 로고
    • An absolute method for protein determination based on difference in absorbance at 235 and 280 nm
    • Whitaker, J. R. & Granum, P. E. (1980). An absolute method for protein determination based on difference in absorbance at 235 and 280 nm. Anal Biochem 109, 156-159.
    • (1980) Anal Biochem , vol.109 , pp. 156-159
    • Whitaker, J.R.1    Granum, P.E.2
  • 56
    • 0025162802 scopus 로고
    • Primary structure and activity of mouse methylmalonyl-CoA mutase
    • Wilkemeyer, M. F., Crane, A. M. & Ledley, F. D. (1990). Primary structure and activity of mouse methylmalonyl-CoA mutase. Biochem J 271, 449-455.
    • (1990) Biochem J , vol.271 , pp. 449-455
    • Wilkemeyer, M.F.1    Crane, A.M.2    Ledley, F.D.3
  • 57
    • 0022226921 scopus 로고
    • Isolation and DNA sequence of adb3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae
    • Young, E. T. & Pilgrim, P. (1985). Isolation and DNA sequence of adb3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Mol Cell Biol 11, 3024-3034.
    • (1985) Mol Cell Biol , vol.11 , pp. 3024-3034
    • Young, E.T.1    Pilgrim, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.