메뉴 건너뛰기




Volumn 188, Issue 24, 2006, Pages 8551-8559

Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp.

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; COENZYME A; FATTY ACID; HYDRACRYLIC ACID; MALONYL COENZYME A; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; RECOMBINANT ENZYME; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RNA;

EID: 33845383207     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00987-06     Document Type: Article
Times cited : (77)

References (35)
  • 1
    • 0019888537 scopus 로고
    • Evidence for two functional gal promotors in intact Escherichia coli
    • Aiba, H., S. Adhya, and B. de Crombrugghe. 1981. Evidence for two functional gal promotors in intact Escherichia coli. J. Biol. Chem. 256:11905-11910.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11905-11910
    • Aiba, H.1    Adhya, S.2    De Crombrugghe, B.3
  • 3
    • 0018894188 scopus 로고
    • Affinity labeling of the Escherichia coli aspartate-beta-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue
    • Biellmann, J. F., P. Eid, and C. Hirth. 1980. Affinity labeling of the Escherichia coli aspartate-beta-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue. Eur. J. Biochem. 104:65-69.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 65-69
    • Biellmann, J.F.1    Eid, P.2    Hirth, C.3
  • 4
    • 16644389785 scopus 로고    scopus 로고
    • Critical catalytic functional groups in the mechanism of aspartate-β-semialdehyde dehydrogenase
    • Blanco, J., R. A. Moore, C. R. Faehnle, and R. E. Viola. 2004. Critical catalytic functional groups in the mechanism of aspartate-β-semialdehyde dehydrogenase. Acta Crystallogr. Sect. D Biol. Crystallogr. 60:1808-1815.
    • (2004) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.60 , pp. 1808-1815
    • Blanco, J.1    Moore, R.A.2    Faehnle, C.R.3    Viola, R.E.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 7
    • 0037310470 scopus 로고    scopus 로고
    • Characterization of a bifunctional archaeal acyl coenzyme A carboxylase
    • Chaukrut, S., H. Arai, M. Ishii, and Y. Igarashi. 2003. Characterization of a bifunctional archaeal acyl coenzyme A carboxylase. J. Bacteriol. 185:938-947.
    • (2003) J. Bacteriol. , vol.185 , pp. 938-947
    • Chaukrut, S.1    Arai, H.2    Ishii, M.3    Igarashi, Y.4
  • 8
    • 33645220015 scopus 로고    scopus 로고
    • Metabolic enzymes that bind RNA: Yet another level of cellular regulatory network?
    • Ciesla, J. 2006. Metabolic enzymes that bind RNA: yet another level of cellular regulatory network? Acta Biochim. Pol. 53:11-32.
    • (2006) Acta Biochim. Pol. , vol.53 , pp. 11-32
    • Ciesla, J.1
  • 9
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 10
    • 0027293771 scopus 로고
    • Retrobiosynthetic analysis of carbon dioxide fixation in the phototrophic eubacterium Chloroflexus aurantiacus
    • Eisenreich, W., G. Strauss, U. Werz, G. Fuchs, and A. Bacher. 1993. Retrobiosynthetic analysis of carbon dioxide fixation in the phototrophic eubacterium Chloroflexus aurantiacus. Eur. J. Biochem. 215:619-632.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 619-632
    • Eisenreich, W.1    Strauss, G.2    Werz, U.3    Fuchs, G.4    Bacher, A.5
  • 11
    • 2242454128 scopus 로고    scopus 로고
    • Dehydrogenases from all three domains of life cleave RNA
    • Evguenieva-Hackenberg, E., E. Schiltz, and G. Klug. 2002. Dehydrogenases from all three domains of life cleave RNA. J. Biol. Chem. 277:46145-46150.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46145-46150
    • Evguenieva-Hackenberg, E.1    Schiltz, E.2    Klug, G.3
  • 12
    • 27144518797 scopus 로고    scopus 로고
    • A new branch in the family: Structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii
    • Faehnle, C. R., J. F. Ohren, and R. E. Viola. 2005. A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii. J. Mol. Biol. 353:1055-1068.
    • (2005) J. Mol. Biol. , vol.353 , pp. 1055-1068
    • Faehnle, C.R.1    Ohren, J.F.2    Viola, R.E.3
  • 13
    • 33645239888 scopus 로고    scopus 로고
    • Properties of succinyl-coenzyme A: L-malate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus
    • Friedmann, S., A. Steindorf, B. E. Alber, and G. Fuchs. 2006. Properties of succinyl-coenzyme A: L-malate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188:2646-2655.
    • (2006) J. Bacteriol. , vol.188 , pp. 2646-2655
    • Friedmann, S.1    Steindorf, A.2    Alber, B.E.3    Fuchs, G.4
  • 14
    • 14644445240 scopus 로고    scopus 로고
    • Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene
    • Fuhrmann, M., A. Hausherr, L. Ferbitz, T. Schodl, M. Heitzer, and P. Hegemann. 2004. Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene. Plant Mol. Biol. 55:869-881.
    • (2004) Plant Mol. Biol. , vol.55 , pp. 869-881
    • Fuhrmann, M.1    Hausherr, A.2    Ferbitz, L.3    Schodl, T.4    Heitzer, M.5    Hegemann, P.6
  • 18
    • 0022517262 scopus 로고
    • 2 fixation in Chloroflexus aurantiacus
    • 2 fixation in Chloroflexus aurantiacus. Arch. Microbiol. 145:173-180.
    • (1986) Arch. Microbiol. , vol.145 , pp. 173-180
    • Holo, H.1    Sirevåg, R.2
  • 19
  • 20
    • 0001960079 scopus 로고
    • Metallosphaera sedula gen. and sp. nov. represents a new genus of aerobic, metal-mobilizing, thermoacidophilic archaebacteria
    • Huber, G., C. Spinnler, A. Gambacorta, and K. O. Stetter. 1989. Metallosphaera sedula gen. and sp. nov. represents a new genus of aerobic, metal-mobilizing, thermoacidophilic archaebacteria. Syst. Appl. Microbiol. 12:38-47.
    • (1989) Syst. Appl. Microbiol. , vol.12 , pp. 38-47
    • Huber, G.1    Spinnler, C.2    Gambacorta, A.3    Stetter, K.O.4
  • 23
    • 0037294946 scopus 로고    scopus 로고
    • Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Carboxylating enzyme in the 3-hydroxypropionate cycle for autotrophic carbon fixation
    • Hügler, M., R. S. Krieger, M. Jahn, and G. Fuchs. 2003. Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Carboxylating enzyme in the 3-hydroxypropionate cycle for autotrophic carbon fixation. Eur. J. Biochem. 270:736-744.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 736-744
    • Hügler, M.1    Krieger, R.S.2    Jahn, M.3    Fuchs, G.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0033057627 scopus 로고    scopus 로고
    • Presence of acetyl coenzyme A (CoA) carboxylase and propionyl-CoA carboxylase in autotrophic Crenarchaeota and indication for operation of a 3-hydroxypropionate cycle in autotrophic carbon fixation
    • Menendez, C., Z. Bauer, H. Huber, N. Gad'on, K.-O. Stetter, and G. Fuchs. 1999. Presence of acetyl coenzyme A (CoA) carboxylase and propionyl-CoA carboxylase in autotrophic Crenarchaeota and indication for operation of a 3-hydroxypropionate cycle in autotrophic carbon fixation. J. Bacteriol. 181:1088-1098.
    • (1999) J. Bacteriol. , vol.181 , pp. 1088-1098
    • Menendez, C.1    Bauer, Z.2    Huber, H.3    Gad'on, N.4    Stetter, K.-O.5    Fuchs, G.6
  • 27
    • 0002833868 scopus 로고
    • Acidophilic, mineral-oxidizing bacteria: The utilization of carbon dioxide with particular reference to autotrophy in Sulfolobus
    • M. S. Da Costa, J. C. Duarte, and R. A. D. Williams (ed.). Elsevier, London, United Kingdom
    • Norris, P., A. Nixon, and A. Hart. 1989. Acidophilic, mineral-oxidizing bacteria: the utilization of carbon dioxide with particular reference to autotrophy in Sulfolobus, p. 24-43. In M. S. Da Costa, J. C. Duarte, and R. A. D. Williams (ed.), Microbiology of extreme environments and its potential for biotechnology. Elsevier, London, United Kingdom.
    • (1989) Microbiology of Extreme Environments and Its Potential for Biotechnology , pp. 24-43
    • Norris, P.1    Nixon, A.2    Hart, A.3
  • 29
    • 77049139172 scopus 로고
    • The role of sulfhydryl groups in the activity of D-glyceraldehyde-3- phosphate dehydrogenase
    • Segal, H. L., and P. D. Boyer. 1953. The role of sulfhydryl groups in the activity of D-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 1953:265-281.
    • (1953) J. Biol. Chem. , vol.1953 , pp. 265-281
    • Segal, H.L.1    Boyer, P.D.2
  • 30
    • 0026611716 scopus 로고
    • 2 fixation pathways in the sulfur-reducing archaebacterium Thermoproteus neutrophilus and in the phototrophic eubacterium Chloroflexus aurantiacus
    • 2 fixation pathways in the sulfur-reducing archaebacterium Thermoproteus neutrophilus and in the phototrophic eubacterium Chloroflexus aurantiacus. Eur. J. Biochem. 205:853-866.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 853-866
    • Strauss, G.1    Eisenreich, W.2    Bacher, A.3    Fuchs, G.4
  • 31
    • 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
  • 32
    • 0036484726 scopus 로고    scopus 로고
    • Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs, Japan
    • Suzuki, T., T. Iwasaki, T. Uzawa, K. Hara, N. Nemoto, T. Kon, T. Ueki, A. Yamagishi, and T. Oshima. 2002. Sulfolobus tokodaii sp. nov. (f. Sulfolobus sp. strain 7), a new member of the genus Sulfolobus isolated from Beppu Hot Springs, Japan. Extremophiles 6:39-44.
    • (2002) Extremophiles , vol.6 , pp. 39-44
    • Suzuki, T.1    Iwasaki, T.2    Uzawa, T.3    Hara, K.4    Nemoto, N.5    Kon, T.6    Ueki, T.7    Yamagishi, A.8    Oshima, T.9
  • 33
    • 0023851702 scopus 로고
    • Identification of the cysteine residue in the active site of horse liver mitochondrial aldehyde dehydrogenase
    • Tu, G. C., and H. Weiner. 1988. Identification of the cysteine residue in the active site of horse liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 263:1212-1217.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1212-1217
    • Tu, G.C.1    Weiner, H.2
  • 34
    • 0034860917 scopus 로고    scopus 로고
    • The central enzymes of the aspartate family of amino acid biosynthesis
    • Viola, R. E. 2001. The central enzymes of the aspartate family of amino acid biosynthesis. Acc. Chem. Res. 34:339-349.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 339-349
    • Viola, R.E.1
  • 35
    • 0024466714 scopus 로고
    • A one-step, low-background Coomassie staining procedure for polyacrylamide gels
    • Zehr, B. D., T. J. Savin, and R. E. Hall. 1989. A one-step, low-background Coomassie staining procedure for polyacrylamide gels. Anal. Biochem. 182:157-159.
    • (1989) Anal. Biochem. , vol.182 , pp. 157-159
    • Zehr, B.D.1    Savin, T.J.2    Hall, R.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.