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Volumn 80, Issue 1, 2014, Pages 166-176

Novel characteristics of succinate coenzyme a (succinate-coa) ligases: Conversion of malate to malyl-coa and coa-thioester formation of succinate analogues in vitro

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION PATHWAYS; EVOLUTIONARY ORIGIN; GENETIC COMPLEMENTATION; HEXAHISTIDINE TAG; PHYSIOLOGICAL SUBSTRATE; PURIFICATION PROTOCOL; STRUCTURAL COMPARISON; SUBSTRATE SPECIFICITY;

EID: 84891066366     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03075-13     Document Type: Article
Times cited : (21)

References (58)
  • 1
    • 77956906489 scopus 로고
    • Succinyl-CoA synthetase
    • In Boyer PD (ed), The enzymes. Academic Press, Inc., New York, NY
    • Bridger WA. 1974. Succinyl-CoA synthetase, p 581-606. In Boyer PD (ed), The enzymes. Academic Press, Inc., New York, NY.
    • (1974) , pp. 581-606
    • Bridger, W.A.1
  • 2
    • 0010982557 scopus 로고
    • Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme
    • Kaufman S. 1955. Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme. J. Biol. Chem. 216:153-164.
    • (1955) J. Biol. Chem. , vol.216 , pp. 153-164
    • Kaufman, S.1
  • 3
    • 0015211405 scopus 로고
    • Evidence for two types of subunits in succinyl coenzyme A synthetase
    • Bridger WA. 1971. Evidence for two types of subunits in succinyl coenzyme A synthetase. Biochem. Biophys. Res. Commun. 42:948-954. http://dx.doi.org/10.1016/0006-291X(71)90522-5.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 948-954
    • Bridger, W.A.1
  • 4
    • 0023055735 scopus 로고
    • Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli
    • Wolodko WT, Kay CM, Bridger WA. 1986. Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli. Biochemistry 25:5420-5425. http://dx.doi.org/10.1021/bi00367a012.
    • (1986) Biochemistry , vol.25 , pp. 5420-5425
    • Wolodko, W.T.1    Kay, C.M.2    Bridger, W.A.3
  • 5
    • 27644511971 scopus 로고    scopus 로고
    • Identification and characterisation of the alpha and beta subunits of succinyl CoA ligase of tomato
    • Studart-Guimaraes C, Gibon Y, Frankel N, Wood CC, Zanor MI, Fernie AR, Carrari F. 2005. Identification and characterisation of the alpha and beta subunits of succinyl CoA ligase of tomato. Plant Mol. Biol. 59:781-791. http://dx.doi.org/10.1007/s11103-005-1004-1.
    • (2005) Plant Mol. Biol. , vol.59 , pp. 781-791
    • Studart-Guimaraes, C.1    Gibon, Y.2    Frankel, N.3    Wood, C.C.4    Zanor, M.I.5    Fernie, A.R.6    Carrari, F.7
  • 6
    • 0033151780 scopus 로고    scopus 로고
    • Probing the nucleotide-binding site of Escherichia coli succinyl- CoA synthetase
    • Joyce MA, Fraser ME, Brownie ER, James MN, Bridger WA, Wolodko WT. 1999. Probing the nucleotide-binding site of Escherichia coli succinyl- CoA synthetase. Biochemistry 38:7273-7283. http://dx.doi.org/10.1021/bi990527s.
    • (1999) Biochemistry , vol.38 , pp. 7273-7283
    • Joyce, M.A.1    Fraser, M.E.2    Brownie, E.R.3    James, M.N.4    Bridger, W.A.5    Wolodko, W.T.6
  • 7
    • 0025977083 scopus 로고
    • Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase
    • Majumdar R, Guest JR, Bridger WA. 1991. Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase. Biochim. Biophys. Acta 1076:86-90. http://dx.doi.org/10.1016/0167-4838(91)90223-M.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 86-90
    • Majumdar, R.1    Guest, J.R.2    Bridger, W.A.3
  • 8
    • 0016719638 scopus 로고
    • Catalysis of a step of the overall reaction by the alpha subunit of Escherichia coli succinyl-coenzyme A synthetase
    • Pearson PH, Bridger WA. 1975. Catalysis of a step of the overall reaction by the alpha subunit of Escherichia coli succinyl-coenzyme A synthetase. J. Biol. Chem. 250:8524-8529.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8524-8529
    • Pearson, P.H.1    Bridger, W.A.2
  • 9
    • 0028276977 scopus 로고
    • The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution
    • Wolodko WT, Fraser ME, James MN, Bridger WA. 1994. The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-Å resolution. J. Biol. Chem. 269:10883-10890.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10883-10890
    • Wolodko, W.T.1    Fraser, M.E.2    James, M.N.3    Bridger, W.A.4
  • 10
    • 0023003018 scopus 로고
    • Distinct physiological roles of animal succinate thiokinases. Association of guanine nucleotide-linked succinate thiokinase with ketone body utilization
    • Jenkins TM, Weitzman PD. 1986. Distinct physiological roles of animal succinate thiokinases. Association of guanine nucleotide-linked succinate thiokinase with ketone body utilization. FEBS Lett. 205:215-218.
    • (1986) FEBS Lett. , vol.205 , pp. 215-218
    • Jenkins, T.M.1    Weitzman, P.D.2
  • 11
    • 0033614003 scopus 로고    scopus 로고
    • A detailed structural description of Escherichia coli succinyl-CoA synthetase
    • Fraser ME, James MN, Bridger WA, Wolodko JWT. 1999. A detailed structural description of Escherichia coli succinyl-CoA synthetase. J. Mol. Biol. 285:1633-1653. http://dx.doi.org/10.1006/jmbi.1998.2324.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1633-1653
    • Fraser, M.E.1    James, M.N.2    Bridger, W.A.3    Wolodko, J.W.T.4
  • 12
    • 0021356895 scopus 로고
    • Crystallization of succinyl- CoA synthetase from Escherichia coli
    • Wolodko WT, James MN, Bridger WA. 1984. Crystallization of succinyl- CoA synthetase from Escherichia coli. J. Biol. Chem. 259:5316-5320.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5316-5320
    • Wolodko, W.T.1    James, M.N.2    Bridger, W.A.3
  • 13
    • 0029923401 scopus 로고    scopus 로고
    • Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation
    • Birney M, Um HD, Klein C. 1996. Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation. J. Bacteriol. 178:2883-2889.
    • (1996) J. Bacteriol. , vol.178 , pp. 2883-2889
    • Birney, M.1    Um, H.D.2    Klein, C.3
  • 14
    • 0033975881 scopus 로고    scopus 로고
    • Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad specificity for nucleoside triphosphate (NTP) synthesis modulates specificity for NTP synthesis by the 12-kilodalton form of nucleoside diphosphate kinase
    • Kapatral V, Bina X, Chakrabarty AM. 2000. Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad specificity for nucleoside triphosphate (NTP) synthesis modulates specificity for NTP synthesis by the 12-kilodalton form of nucleoside diphosphate kinase. J. Bacteriol. 182: 1333-1339. http://dx.doi.org/10.1128/JB.182.5.1333-1339.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 1333-1339
    • Kapatral, V.1    Bina, X.2    Chakrabarty, A.M.3
  • 15
    • 0015501795 scopus 로고
    • Nucleotide specificity of Escherichia coli succinic thiokinase. Succinyl coenzyme A-stimulated nucleoside diphosphate kinase activity of the enzyme
    • Murakami K, Mitchell T, Nishimura JS. 1972. Nucleotide specificity of Escherichia coli succinic thiokinase. Succinyl coenzyme A-stimulated nucleoside diphosphate kinase activity of the enzyme. J. Biol. Chem. 247: 6247-6252.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6247-6252
    • Murakami, K.1    Mitchell, T.2    Nishimura, J.S.3
  • 16
    • 0021836849 scopus 로고
    • Fatty acids bound to unilamellar lipid vesicles as substrates for microsomal acyl-CoA ligase
    • Noy N, Zakim D. 1985. Fatty acids bound to unilamellar lipid vesicles as substrates for microsomal acyl-CoA ligase. Biochemistry 24:3521-3525. http://dx.doi.org/10.1021/bi00335a020.
    • (1985) Biochemistry , vol.24 , pp. 3521-3525
    • Noy, N.1    Zakim, D.2
  • 17
    • 26444522209 scopus 로고    scopus 로고
    • AMP-forming acetyl-CoA synthetase from the extremely halophilic archaeon Haloarcula marismortui: purification, identification and expression of the encoding gene, and phylogenetic affiliation
    • Bräsen C, Schönheit P. 2005. AMP-forming acetyl-CoA synthetase from the extremely halophilic archaeon Haloarcula marismortui: purification, identification and expression of the encoding gene, and phylogenetic affiliation. Extremophiles 9:355-365. http://dx.doi.org/10.1007/s00792-005-0449-0.
    • (2005) Extremophiles , vol.9 , pp. 355-365
    • Bräsen, C.1    Schönheit, P.2
  • 18
    • 0029794709 scopus 로고    scopus 로고
    • Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus
    • Mai X, Adams MW. 1996. Purification and characterization of two reversible and ADP-dependent acetyl coenzyme A synthetases from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 178:5897- 5903.
    • (1996) J. Bacteriol. , vol.178
    • Mai, X.1    Adams, M.W.2
  • 19
    • 0347355514 scopus 로고    scopus 로고
    • Propionyl-coenzyme A synthetases of Ralstonia solanacearum and Salmonella choleraesuis display atypical kinetics
    • Rajashekhara E, Watanabe K. 2004. Propionyl-coenzyme A synthetases of Ralstonia solanacearum and Salmonella choleraesuis display atypical kinetics. FEBS Lett. 556:143-147. http://dx.doi.org/10.1016/S0014-5793(03)01394-2.
    • (2004) FEBS Lett. , vol.556 , pp. 143-147
    • Rajashekhara, E.1    Watanabe, K.2
  • 20
    • 0019772583 scopus 로고
    • Butyryl-CoA synthetase of Pseudomonas aeruginosa-purification and characterization
    • Shimizu S, Inoue K, Tani Y, Yamada H. 1981. Butyryl-CoA synthetase of Pseudomonas aeruginosa-purification and characterization. Biochem. Biophys. Res. Commun. 103:1231-1237. http://dx.doi.org/10.1016/0006-291X(81)90254-0.
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 1231-1237
    • Shimizu, S.1    Inoue, K.2    Tani, Y.3    Yamada, H.4
  • 21
    • 34848840085 scopus 로고    scopus 로고
    • A novel ADP-forming succinyl-CoA synthetase in Thermococcus kodakaraensis structurally related to the archaeal nucleoside diphosphate-forming acetyl-CoA synthetases
    • Shikata K, Fukui T, Atomi H, Imanaka T. 2007. A novel ADP-forming succinyl-CoA synthetase in Thermococcus kodakaraensis structurally related to the archaeal nucleoside diphosphate-forming acetyl-CoA synthetases. J. Biol. Chem. 282:26963-26970. http://dx.doi.org/10.1074/jbc.M702694200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26963-26970
    • Shikata, K.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 22
    • 0013651376 scopus 로고
    • The metabolism of itaconic acid by liver mitochondria
    • Adler J, Wang SF, Lardy HA. 1957. The metabolism of itaconic acid by liver mitochondria. J. Biol. Chem. 229:865-879.
    • (1957) J. Biol. Chem. , vol.229 , pp. 865-879
    • Adler, J.1    Wang, S.F.2    Lardy, H.A.3
  • 23
    • 0344544759 scopus 로고
    • The utilization of aconate and itaconate by Micrococcus sp
    • Cooper RA, Itiaba K, Kornberg HL. 1965. The utilization of aconate and itaconate by Micrococcus sp. Biochem. J. 94:25-31.
    • (1965) Biochem. J. , vol.94 , pp. 25-31
    • Cooper, R.A.1    Itiaba, K.2    Kornberg, H.L.3
  • 24
    • 0013672915 scopus 로고
    • Studies on itaconate metabolism, I. Itaconyl-CoA synthesizing reaction in cell-free extract
    • Nagai J. 1963. Studies on itaconate metabolism, I. Itaconyl-CoA synthesizing reaction in cell-free extract. J. Biochem. 53:181-187.
    • (1963) J. Biochem. , vol.53 , pp. 181-187
    • Nagai, J.1
  • 25
    • 0142093990 scopus 로고    scopus 로고
    • Novel precursor substrates for polythioesters (PTE) and limits of PTE biosynthesis in Ralstonia eutropha
    • Lütke-Eversloh T, Steinbüchel A. 2003. Novel precursor substrates for polythioesters (PTE) and limits of PTE biosynthesis in Ralstonia eutropha. FEMS Microbiol. Lett. 221:191-196. http://dx.doi.org/10.1016/S0378-1097(03)00185-X.
    • (2003) FEMS Microbiol. Lett. , vol.221 , pp. 191-196
    • Lütke-Eversloh, T.1    Steinbüchel, A.2
  • 26
    • 79958026080 scopus 로고    scopus 로고
    • Novel reaction of succinyl coenzyme A (succinyl-CoA) synthetase: activation of 3-sulfinopropionate to 3-sulfinopropionyl-CoA in Advenella mimigardefordensis strain DPN7T during degradation of 3,3=-dithiodipropionic acid
    • Schürmann M, Wübbeler JH, Grote J, Steinbüchel A. 2011. Novel reaction of succinyl coenzyme A (succinyl-CoA) synthetase: activation of 3-sulfinopropionate to 3-sulfinopropionyl-CoA in Advenella mimigardefordensis strain DPN7T during degradation of 3,3=-dithiodipropionic acid. J. Bacteriol. 193:3078-3089. http://dx.doi.org/10.1128/JB.00049-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 3078-3089
    • Schürmann, M.1    Wübbeler, J.H.2    Grote, J.3    Steinbüchel, A.4
  • 27
    • 77950645166 scopus 로고    scopus 로고
    • Biodegradation of the xenobiotic organic disulphide 4,4=-dithiodibutyric acid by Rhodococcus erythropolis strain MI2 and comparison with the microbial utilization of 3,3=-dithiodipropionic acid and 3,3=-thiodipropionic acid
    • Wübbeler JH, Bruland N, Wozniczka M, Steinbüchel A. 2010. Biodegradation of the xenobiotic organic disulphide 4,4=-dithiodibutyric acid by Rhodococcus erythropolis strain MI2 and comparison with the microbial utilization of 3,3=-dithiodipropionic acid and 3,3=-thiodipropionic acid. Microbiology 156:1221-1233. http://dx.doi.org/10.1099/mic.0.036178-0.
    • (2010) Microbiology , vol.156 , pp. 1221-1233
    • Wübbeler, J.H.1    Bruland, N.2    Wozniczka, M.3    Steinbüchel, A.4
  • 28
    • 84861124182 scopus 로고    scopus 로고
    • Employing a recombinant strain of Advenella mimigardefordensis for biotechnical production of homopolythioesters from 3,3=-dithiodipropionic acid
    • Xia Y, Wübbeler JH, Qi Q, Steinbüchel A. 2012. Employing a recombinant strain of Advenella mimigardefordensis for biotechnical production of homopolythioesters from 3,3=-dithiodipropionic acid. Appl. Environ. Microbiol. 78:3286-3297. http://dx.doi.org/10.1128/AEM.00007-12.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 3286-3297
    • Xia, Y.1    Wübbeler, J.H.2    Qi, Q.3    Steinbüchel, A.4
  • 29
    • 46949090171 scopus 로고    scopus 로고
    • Novel pathway for catabolism of the organic sulfur compound 3,3=- dithiodipropionic acid via 3-mercaptopropionic acid and 3-sulfinoproppionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7
    • Wübbeler JH, Bruland N, Kretschmer K, Steinbüchel A. 2008. Novel pathway for catabolism of the organic sulfur compound 3,3=- dithiodipropionic acid via 3-mercaptopropionic acid and 3-sulfinoproppionic acid to propionyl-coenzyme A by the aerobic bacterium Tetrathiobacter mimigardefordensis strain DPN7. Appl. Environ. Microbiol. 74: 4028-4035. http://dx.doi.org/10.1128/AEM.00422-08.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 4028-4035
    • Wübbeler, J.H.1    Bruland, N.2    Kretschmer, K.3    Steinbüchel, A.4
  • 30
    • 33745302842 scopus 로고    scopus 로고
    • Tetrathiobacter mimigardefordensis sp. nov., isolated from compost, a betaproteobacterium capable of utilizing the organic disulfide. 3,3=-dithiodipropionic acid
    • Wübbeler JH, Lütke-Eversloh T, Van Trappen S, Vandamme P, Steinbüchel A. 2006. Tetrathiobacter mimigardefordensis sp. nov., isolated from compost, a betaproteobacterium capable of utilizing the organic disulfide 3,3=-dithiodipropionic acid. Int. J. Syst. Evol. Microbiol. 56:1305-1310. http://dx.doi.org/10.1099/ijs.0.64126-0.
    • (2006) Int. J. Syst. Evol. Microbiol , vol.56 , pp. 1305-1310
    • Wübbeler, J.H.1    Lütke-Eversloh, T.2    Van Trappen, S.3    Vandamme, P.4    Steinbüchel, A.5
  • 31
    • 78149413196 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenases of Advenella mimigardefordensis and Ralstonia eutropha catalyze cleavage of 3,3=-dithiodipropionic acid into 3-mercaptopropionic acid
    • Wübbeler JH, Raberg M, Brandt U, Steinbüchel A. 2010. Dihydrolipoamide dehydrogenases of Advenella mimigardefordensis and Ralstonia eutropha catalyze cleavage of 3,3=-dithiodipropionic acid into 3-mercaptopropionic acid. Appl. Environ. Microbiol. 76:7023-7028. http://dx.doi.org/10.1128/AEM.01706-10.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 7023-7028
    • Wübbeler, J.H.1    Raberg, M.2    Brandt, U.3    Steinbüchel, A.4
  • 32
    • 0022397910 scopus 로고
    • Primary structure of the succinyl- CoA synthetase of Escherichia coli
    • Buck D, Spencer ME, Guest JR. 1985. Primary structure of the succinyl- CoA synthetase of Escherichia coli. Biochemistry 24:6245-6252. http://dx.doi.org/10.1021/bi00343a031.
    • (1985) Biochemistry , vol.24 , pp. 6245-6252
    • Buck, D.1    Spencer, M.E.2    Guest, J.R.3
  • 33
    • 0034635193 scopus 로고    scopus 로고
    • ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by X-ray crystallography
    • Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT. 2000. ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by X-ray crystallography. Biochemistry 39:17-25. http://dx.doi.org/10.1021/bi991696f.
    • (2000) Biochemistry , vol.39 , pp. 17-25
    • Joyce, M.A.1    Fraser, M.E.2    James, M.N.3    Bridger, W.A.4    Wolodko, W.T.5
  • 35
    • 34250969714 scopus 로고
    • A submersion method for culture of hydrogen-oxidizing bacteria: growth physiological studies
    • Schlegel HG, Kaltwasser H, Gottschalk G. 1961. A submersion method for culture of hydrogen-oxidizing bacteria: growth physiological studies. Arch. Mikrobiol. 38:209-222. http://dx.doi.org/10.1007/BF00422356.
    • (1961) Arch. Mikrobiol. , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 36
    • 0003903343 scopus 로고
    • Molecular cloning: a laboratory manual
    • 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 37
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW. 2005. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41:207-234. http://dx.doi.org/10.1016/j.pep.2005.01.016.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 38
    • 0015947282 scopus 로고
    • Enzymatic and chemical synthesis of 3-sulfinopropionic acid, an analog of succinic acid
    • Jollès-Bergeret B. 1974. Enzymatic and chemical synthesis of 3-sulfinopropionic acid, an analog of succinic acid. Eur. J. Biochem. 42:349-353. http://dx.doi.org/10.1111/j.1432-1033.1974.tb03346.x.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 349-353
    • Jollès-Bergeret, B.1
  • 39
    • 0041927513 scopus 로고    scopus 로고
    • The NIST mass spectral search program
    • Windows software version 1.6d. National Institute of Standards and Technology, Gaithersburg, MD
    • Stein S, Levitsky A, Fateev O, Mallard G. 1998. The NIST mass spectral search program, Windows software version 1.6d. National Institute of Standards and Technology, Gaithersburg, MD.
    • (1998)
    • Stein, S.1    Levitsky, A.2    Fateev, O.3    Mallard, G.4
  • 40
    • 0036435830 scopus 로고    scopus 로고
    • Separation and identification of organic acid-coenzyme A thioesters using liquid chromatography/electrospray ionization-mass spectrometry
    • Dalluge JJ, Gort S, Hobson R, Selifonova O, Amore F, Gokarn R. 2002. Separation and identification of organic acid-coenzyme A thioesters using liquid chromatography/electrospray ionization-mass spectrometry. Anal. Bioanal. Chem. 374:835-840. http://dx.doi.org/10.1007/s00216-002-1554-x.
    • (2002) Anal. Bioanal. Chem. , vol.374 , pp. 835-840
    • Dalluge, J.J.1    Gort, S.2    Hobson, R.3    Selifonova, O.4    Amore, F.5    Gokarn, R.6
  • 41
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218. http://dx.doi.org/10.1016/S0022-2836(61)80047-8.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 42
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria
    • Simon R, Priefer U, Pühler A. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Biotechnology 1:784-791. http://dx.doi.org/10.1038/nbt1183-784.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 45
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach ME, Elzer PH, Hill DS, Robertson GT, Farris MA, Roop RM, II, Peterson KM. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176. http://dx.doi.org/10.1016/0378-1119(95)00584-1.
    • (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, R.M.6    Peterson, K.M.7
  • 46
    • 7344231484 scopus 로고
    • Colloidal dispersion of chloroplast material
    • Milner HW, Lawrence NS, French CS. 1950. Colloidal dispersion of chloroplast material. Science 111:633-634. http://dx.doi.org/10.1126/science.111.2893.633.
    • (1950) Science , vol.111 , pp. 633-634
    • Milner, H.W.1    Lawrence, N.S.2    French, C.S.3
  • 47
    • 0014216733 scopus 로고
    • Succinyl coenzyme A synthetase from Escherichia coli. I. Purification and properties
    • Gibson J, Upper CD, Gunsalus IC. 1967. Succinyl coenzyme A synthetase from Escherichia coli. I. Purification and properties. J. Biol. Chem. 242: 2474-2477.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2474-2477
    • Gibson, J.1    Upper, C.D.2    Gunsalus, I.C.3
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 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. http://dx.doi.org/10.1016/0003 -2697(76)90527-3.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 50
    • 37949019335 scopus 로고
    • Succinic thiokinase. II. Kinetic studies: initial velocity, product inhibition, and effect of arsenate
    • Cha S, Parks RE. 1964. Succinic thiokinase. II. Kinetic studies: initial velocity, product inhibition, and effect of arsenate. J. Biol. Chem. 239: 1968-1977.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1968-1977
    • Cha, S.1    Parks, R.E.2
  • 51
    • 0028073454 scopus 로고
    • Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB
    • Chistoserdova LV, Lidstrom ME. 1994. Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB. J. Bacteriol. 176:7398-7404.
    • (1994) J. Bacteriol. , vol.176 , pp. 7398-7404
    • Chistoserdova, L.V.1    Lidstrom, M.E.2
  • 52
    • 0025924637 scopus 로고
    • In vivo 13C and 15N NMR studies of methylamine metabolism in Pseudomonas species MA
    • Jones JG, Bellion E. 1991. In vivo 13C and 15N NMR studies of methylamine metabolism in Pseudomonas species MA. J. Biol. Chem. 266:11705- 11713.
    • (1991) J. Biol. Chem. , vol.266
    • Jones, J.G.1    Bellion, E.2
  • 53
    • 0018786483 scopus 로고
    • Substrate-dependent dissociation of malate thiokinase
    • Elwell M, Hersh LB. 1979. Substrate-dependent dissociation of malate thiokinase. J. Biol. Chem. 254:2434-2438.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2434-2438
    • Elwell, M.1    Hersh, L.B.2
  • 54
    • 0016174011 scopus 로고
    • Malate thiokinase. The reaction mechanism as determined by initial rate studies
    • Hersh LB. 1974. Malate thiokinase. The reaction mechanism as determined by initial rate studies. J. Biol. Chem. 249:6264-6271.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6264-6271
    • Hersh, L.B.1
  • 55
    • 0015857926 scopus 로고
    • Malate adenosine triphosphate lyase. Separation of the reaction into a malate thiokinase and malyl coenzyme A lyase
    • Hersh LB. 1973. Malate adenosine triphosphate lyase. Separation of the reaction into a malate thiokinase and malyl coenzyme A lyase. J. Biol. Chem. 248:7295-7303.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7295-7303
    • Hersh, L.B.1
  • 56
    • 0019887773 scopus 로고
    • Half-of-the-sites reactivity in the malate thiokinase reaction
    • Hersh LB, Peet M. 1981. Half-of-the-sites reactivity in the malate thiokinase reaction. J. Biol. Chem. 256:1732-1737.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1732-1737
    • Hersh, L.B.1    Peet, M.2
  • 57
    • 84875500949 scopus 로고    scopus 로고
    • A novel 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis strain DPN7T acting as a key enzyme during catabolism of 3,3=-dithiodipropionic acid is a member of the acyl-CoA dehydrogenase superfamily
    • Schürmann M, Deters A, Wübbeler JH, Steinbüchel A. 2013. A novel 3-sulfinopropionyl coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis strain DPN7T acting as a key enzyme during catabolism of 3,3=-dithiodipropionic acid is a member of the acyl-CoA dehydrogenase superfamily. J. Bacteriol. 195:1538-1551. http://dx.doi.org/10.1128/JB.02105-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 1538-1551
    • Schürmann, M.1    Deters, A.2    Wübbeler, J.H.3    Steinbüchel, A.4
  • 58
    • 0025365339 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 8
    • Bachmann BJ. 1990. Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev. 54:130-197.
    • (1990) Microbiol. Rev. , vol.54 , pp. 130-197
    • Bachmann, B.J.1


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