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Volumn 81, Issue 4, 2011, Pages 952-967

ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

5,6 DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; ADENOSYLCOBAMIDE; ALPHA 5,6 DIMETHYLBENZIMIDAZOLYL RIBOTIDE; ALPHA N GLYCOSIDIC RIBOTIDE; ALPHA O GLYCOSIDIC RIBOTIDE; ALPHA P CRESOLYL RIBOTIDE; ALPHA PHENOLYL RIBOTIDE; ALPHA RIBOTIDE; BACTERIAL ENZYME; COBAMAMIDE; DNA FRAGMENT; GENOMIC DNA; NICOTINIC ACID NUCLEOTIDE; NUCLEOSIDE; NUCLEOTIDE; PARA CRESOL; PHENOL; PHENOL DERIVATIVE; PHOSPHORIBOSYL GROUP; PHOSPHORIBOSYLTRANSFERASE; PROTEIN ARSAB; UNCLASSIFIED DRUG;

EID: 80051576390     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07741.x     Document Type: Article
Times cited : (42)

References (61)
  • 2
    • 43549115250 scopus 로고    scopus 로고
    • Identification and quantitation of cobalamin and cobalamin analogues in human feces
    • Allen, R.H., and Stabler, S.P. (2008) Identification and quantitation of cobalamin and cobalamin analogues in human feces. Am J Clin Nutr 87: 1324-1335.
    • (2008) Am J Clin Nutr , vol.87 , pp. 1324-1335
    • Allen, R.H.1    Stabler, S.P.2
  • 3
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., etal. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 20060008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 5
    • 0345311216 scopus 로고
    • Proton and C-13 Assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR
    • Bax, A., and Summers, M.F. (1986) Proton and C-13 Assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR. J Am Chem Soc 108: 2093-2094.
    • (1986) J Am Chem Soc , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 6
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G. (1951) Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol 62: 293-300.
    • (1951) J Bacteriol , vol.62 , pp. 293-300
    • Bertani, G.1
  • 7
    • 0347325071 scopus 로고    scopus 로고
    • Lysogeny at mid-twentieth century: P1, P2, and other experimental systems
    • Bertani, G. (2004) Lysogeny at mid-twentieth century: P1, P2, and other experimental systems. J Bacteriol 186: 595-600.
    • (2004) J Bacteriol , vol.186 , pp. 595-600
    • Bertani, G.1
  • 8
    • 0025076610 scopus 로고
    • Identification and quantitation of corrinoid precursors of cobalamin from Pseudomonas denitrificans by high-performance liquid chromatography
    • Blanche, F., Thibaut, D., Couder, M., and Muller, J.C. (1990) Identification and quantitation of corrinoid precursors of cobalamin from Pseudomonas denitrificans by high-performance liquid chromatography. Anal Biochem 189: 24-29.
    • (1990) Anal Biochem , vol.189 , pp. 24-29
    • Blanche, F.1    Thibaut, D.2    Couder, M.3    Muller, J.C.4
  • 9
    • 34250348569 scopus 로고    scopus 로고
    • A combined approach to improving large-scale production of tobacco etch virus protease
    • Blommel, P.G., and Fox, B.G. (2007) A combined approach to improving large-scale production of tobacco etch virus protease. Protein Expr Purif 55: 53-68.
    • (2007) Protein Expr Purif , vol.55 , pp. 53-68
    • Blommel, P.G.1    Fox, B.G.2
  • 10
    • 0021324642 scopus 로고
    • Plasmid insertion mutagenesis and lac gene fusion with mini-mu bacteriophage transposons
    • Castilho, B.A., Olfson, P., and Casadaban, M.J. (1984) Plasmid insertion mutagenesis and lac gene fusion with mini-mu bacteriophage transposons. J Bacteriol 158: 488-495.
    • (1984) J Bacteriol , vol.158 , pp. 488-495
    • Castilho, B.A.1    Olfson, P.2    Casadaban, M.J.3
  • 11
    • 0033534156 scopus 로고    scopus 로고
    • The three-dimensional structures of nicotinate mononucleotide:5,6- dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella typhimurium complexed with 5,6-dimethybenzimidazole and its reaction products determined to 1.9Å resolution
    • Cheong, C.G., Escalante-Semerena, J.C., and Rayment, I. (1999) The three-dimensional structures of nicotinate mononucleotide:5, 6- dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella typhimurium complexed with 5, 6-dimethybenzimidazole and its reaction products determined to 1.9Å resolution. Biochemistry 38: 16125-16135.
    • (1999) Biochemistry , vol.38 , pp. 16125-16135
    • Cheong, C.G.1    Escalante-Semerena, J.C.2    Rayment, I.3
  • 12
    • 0035813185 scopus 로고    scopus 로고
    • Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella enterica
    • Cheong, C.G., Escalante-Semerena, J.C., and Rayment, I. (2001) Structural investigation of the biosynthesis of alternative lower ligands for cobamides by nicotinate mononucleotide: 5, 6-dimethylbenzimidazole phosphoribosyltransferase from Salmonella enterica. J Biol Chem 276: 37612-37620.
    • (2001) J Biol Chem , vol.276 , pp. 37612-37620
    • Cheong, C.G.1    Escalante-Semerena, J.C.2    Rayment, I.3
  • 13
    • 33750965918 scopus 로고    scopus 로고
    • In meso structure of the cobalamin transporter, BtuB, at 1.95 Å resolution
    • Cherezov, V., Yamashita, E., Liu, W., Zhalnina, M., Cramer, W.A., and Caffrey, M. (2006) In meso structure of the cobalamin transporter, BtuB, at 1.95 Å resolution. J Mol Biol 364: 716-734.
    • (2006) J Mol Biol , vol.364 , pp. 716-734
    • Cherezov, V.1    Yamashita, E.2    Liu, W.3    Zhalnina, M.4    Cramer, W.A.5    Caffrey, M.6
  • 14
    • 73849135284 scopus 로고    scopus 로고
    • Functional analysis of the nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) enzyme, involved in the late steps of coenzyme B12 biosynthesis in Salmonella enterica
    • Claas, K.R., Parrish, J.R., Maggio-Hall, L.A., and Escalante-Semerena, J.C. (2010) Functional analysis of the nicotinate mononucleotide:5, 6-dimethylbenzimidazole phosphoribosyltransferase (CobT) enzyme, involved in the late steps of coenzyme B12 biosynthesis in Salmonella enterica. J Bacteriol 192: 145-154.
    • (2010) J Bacteriol , vol.192 , pp. 145-154
    • Claas, K.R.1    Parrish, J.R.2    Maggio-Hall, L.A.3    Escalante-Semerena, J.C.4
  • 15
    • 0014595487 scopus 로고
    • Evidence for two genes specifically involved in unsaturated fatty acid biosynthesis in Escherichia coli
    • Cronan, J.E., Jr, Birge, C.H., and Vagelos, P.R. (1969) Evidence for two genes specifically involved in unsaturated fatty acid biosynthesis in Escherichia coli. J Bacteriol 100: 601-604.
    • (1969) J Bacteriol , vol.100 , pp. 601-604
    • Cronan Jr, J.E.1    Birge, C.H.2    Vagelos, P.R.3
  • 16
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 18
    • 0014669720 scopus 로고
    • 12 biosynthesis. Enzymatic formation of a new adenylic acid, 7-α-D-ribofuranosyladenine 5'-phosphate
    • 12 biosynthesis. Enzymatic formation of a new adenylic acid, 7-α-D-ribofuranosyladenine 5'-phosphate. J Biol Chem 244: 1667-1671.
    • (1969) J Biol Chem , vol.244 , pp. 1667-1671
    • Friedmann, H.C.1    Fyfe, J.A.2
  • 19
    • 0009976032 scopus 로고
    • The formation of alpha-glycosidic 5'-nucleotides by a single displacement trans-N-glycosidase
    • Friedmann, H.C., and Harris, D.L. (1965) The formation of alpha-glycosidic 5'-nucleotides by a single displacement trans-N-glycosidase. J Biol Chem 240: 406-412.
    • (1965) J Biol Chem , vol.240 , pp. 406-412
    • Friedmann, H.C.1    Harris, D.L.2
  • 20
    • 70450197390 scopus 로고    scopus 로고
    • The cobinamide amidohydrolase (cobyric acid-forming) CbiZ enzyme: a critical activity of the cobamide remodelling system of Rhodobacter sphaeroides
    • Gray, M.J., and Escalante-Semerena, J.C. (2009) The cobinamide amidohydrolase (cobyric acid-forming) CbiZ enzyme: a critical activity of the cobamide remodelling system of Rhodobacter sphaeroides. Mol Microbiol 74: 1198-1210.
    • (2009) Mol Microbiol , vol.74 , pp. 1198-1210
    • Gray, M.J.1    Escalante-Semerena, J.C.2
  • 21
    • 77956640364 scopus 로고    scopus 로고
    • A new pathway for the synthesis of alpha-ribazole-phosphate in Listeria innocua
    • Gray, M.J., and Escalante-Semerena, J.C. (2010) A new pathway for the synthesis of alpha-ribazole-phosphate in Listeria innocua. Mol Microbiol 77: 1429-1438.
    • (2010) Mol Microbiol , vol.77 , pp. 1429-1438
    • Gray, M.J.1    Escalante-Semerena, J.C.2
  • 22
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 23
    • 0022430394 scopus 로고
    • 12-dependent rearrangements
    • 12-dependent rearrangements. Science 227: 869-875.
    • (1985) Science , vol.227 , pp. 869-875
    • Halpern, J.1
  • 24
    • 0026038362 scopus 로고
    • Plasmid transformation of Escherichia coli and other bacteria
    • Hanahan, D., Jessee, J., and Bloom, F.R. (1991) Plasmid transformation of Escherichia coli and other bacteria. Methods Enzymol 204: 63-113.
    • (1991) Methods Enzymol , vol.204 , pp. 63-113
    • Hanahan, D.1    Jessee, J.2    Bloom, F.R.3
  • 25
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter binding protein complex BtuCD-BtuF
    • Hvorup, R.N., Goetz, B.A., Niederer, M., Hollenstein, K., Perozo, E., and Locher, K.P. (2007) Asymmetry in the structure of the ABC transporter binding protein complex BtuCD-BtuF. Science 317: 1387-1390.
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 27
    • 0026681593 scopus 로고
    • Identification of 5,6-dimethylbenzimidazole as the Coα ligand of the cobamide synthesized by Salmonella typhimurium. Nutritional characterization of mutants defective in biosynthesis of the imidazole ring
    • Johnson, M.G., and Escalante-Semerena, J.C. (1992) Identification of 5, 6-dimethylbenzimidazole as the Coα ligand of the cobamide synthesized by Salmonella typhimurium. Nutritional characterization of mutants defective in biosynthesis of the imidazole ring. J Biol Chem 267: 13302-13305.
    • (1992) J Biol Chem , vol.267 , pp. 13302-13305
    • Johnson, M.G.1    Escalante-Semerena, J.C.2
  • 28
    • 0033979881 scopus 로고    scopus 로고
    • Salmonella typhimurium forms adenylcobamide and 2-methyladenylcobamide, but no detectable cobalamin during strictly anaerobic growth
    • Keck, B., and Renz, P. (2000) Salmonella typhimurium forms adenylcobamide and 2-methyladenylcobamide, but no detectable cobalamin during strictly anaerobic growth. Arch Microbiol 173: 76-77.
    • (2000) Arch Microbiol , vol.173 , pp. 76-77
    • Keck, B.1    Renz, P.2
  • 29
    • 1542616353 scopus 로고    scopus 로고
    • Chromosomal fragmentation in dUTPase-deficient mutants of Escherichia coli and its recombinational repair
    • Kouzminova, E.A., and Kuzminov, A. (2004) Chromosomal fragmentation in dUTPase-deficient mutants of Escherichia coli and its recombinational repair. Mol Microbiol 51: 1279-1295.
    • (2004) Mol Microbiol , vol.51 , pp. 1279-1295
    • Kouzminova, E.A.1    Kuzminov, A.2
  • 30
    • 0348012973 scopus 로고    scopus 로고
    • The cofactor of tetrachloroethene reductive dehalogenase of Dehalospirillum multivorans is Norpseudo-B12, a new type of natural corrinoid
    • Kräutler, B., Fieber, W., Osterman, S., Fasching, M., Ongania, K.-H., Gruber, K., etal. (2003) The cofactor of tetrachloroethene reductive dehalogenase of Dehalospirillum multivorans is Norpseudo-B12, a new type of natural corrinoid. Helv Chim Acta 86: 3698-3716.
    • (2003) Helv Chim Acta , vol.86 , pp. 3698-3716
    • Kräutler, B.1    Fieber, W.2    Osterman, S.3    Fasching, M.4    Ongania, K.-H.5    Gruber, K.6
  • 31
    • 0032716102 scopus 로고    scopus 로고
    • In vitro synthesis of the nucleotide loop of cobalamin by Salmonella typhimurium enzymes
    • Maggio-Hall, L.A., and Escalante-Semerena, J.C. (1999) In vitro synthesis of the nucleotide loop of cobalamin by Salmonella typhimurium enzymes. Proc Natl Acad Sci USA 96: 11798-11803.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11798-11803
    • Maggio-Hall, L.A.1    Escalante-Semerena, J.C.2
  • 32
    • 0033287696 scopus 로고    scopus 로고
    • 12 (cobalamin)-dependent enzymes
    • 12 (cobalamin)-dependent enzymes. Essays Biochem 34: 139-154.
    • (1999) Essays Biochem , vol.34 , pp. 139-154
    • Marsh, E.N.1
  • 33
    • 0001375592 scopus 로고
    • Sporomusa, a new genus of Gram-negative anaerobic-bacteria including Sporomusa-Sphaeroides spec-nov and Sporomusa-Ovata spec-nov
    • Möller, B., Ossmer, R., Howard, B.H., Gottschalk, G., and Hippe, H. (1984) Sporomusa, a new genus of Gram-negative anaerobic-bacteria including Sporomusa-Sphaeroides spec-nov and Sporomusa-Ovata spec-nov. Arch Microbiol 139: 388-396.
    • (1984) Arch Microbiol , vol.139 , pp. 388-396
    • Möller, B.1    Ossmer, R.2    Howard, B.H.3    Gottschalk, G.4    Hippe, H.5
  • 34
    • 0027294598 scopus 로고
    • Analysis of mutants of defective in the synthesis of the nucleotide loop of cobalamin
    • O'Toole, G.A., Rondon, M.R., and Escalante-Semerena, J.C. (1993) Analysis of mutants of defective in the synthesis of the nucleotide loop of cobalamin. J Bacteriol 175: 3317-3326.
    • (1993) J Bacteriol , vol.175 , pp. 3317-3326
    • O'Toole, G.A.1    Rondon, M.R.2    Escalante-Semerena, J.C.3
  • 35
    • 67649631301 scopus 로고    scopus 로고
    • Biochemical characterization of the GTP:adenosylcobinamide-phosphate guanylyltransferase (CobY) enzyme of the hyperthermophilic archaeon Methanocaldococcus jannaschii
    • Otte, M.M., and Escalante-Semerena, J.C. (2009) Biochemical characterization of the GTP:adenosylcobinamide-phosphate guanylyltransferase (CobY) enzyme of the hyperthermophilic archaeon Methanocaldococcus jannaschii. Biochemistry 48: 5882-5889.
    • (2009) Biochemistry , vol.48 , pp. 5882-5889
    • Otte, M.M.1    Escalante-Semerena, J.C.2
  • 36
    • 0031466511 scopus 로고    scopus 로고
    • 1H-NMR structure analysis and kinetic studies with (R)-methylmalonyl-CoA mutase, glycerol dehydratase, and diol dehydratase
    • 1H-NMR structure analysis and kinetic studies with (R)-methylmalonyl-CoA mutase, glycerol dehydratase, and diol dehydratase. Eur J Biochem 250: 303-307.
    • (1997) Eur J Biochem , vol.250 , pp. 303-307
    • Poppe, L.1    Stupperich, E.2    Hull, W.E.3    Buckel, T.4    Rétey, J.5
  • 37
    • 0029320145 scopus 로고
    • A versatile quick-prep of genomic DNA from gram-positive bacteria
    • Pospiech, A., and Neumann, B. (1995) A versatile quick-prep of genomic DNA from gram-positive bacteria. Trends Genet 11: 217-218.
    • (1995) Trends Genet , vol.11 , pp. 217-218
    • Pospiech, A.1    Neumann, B.2
  • 38
    • 0002449548 scopus 로고    scopus 로고
    • Biosynthesis of the 5,6-dimethylbenzimidazole moiety of cobalamin and of other bases found in natural corrinoids
    • Banerjee, R. (ed.). New York: John Wiley & Sons.
    • 12. Banerjee, R. (ed.). New York: John Wiley & Sons, pp. 557-575.
    • (1999) 12 , pp. 557-575
    • Renz, P.1
  • 39
    • 41549104836 scopus 로고    scopus 로고
    • Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli
    • Rocco, C.J., Dennison, K.L., Klenchin, V.A., Rayment, I., and Escalante-Semerena, J.C. (2008) Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli. Plasmid 59: 231-237.
    • (2008) Plasmid , vol.59 , pp. 231-237
    • Rocco, C.J.1    Dennison, K.L.2    Klenchin, V.A.3    Rayment, I.4    Escalante-Semerena, J.C.5
  • 40
    • 0024075956 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium
    • Roof, D.M., and Roth, J.R. (1988) Ethanolamine utilization in Salmonella typhimurium. J Bacteriol 170: 3855-3863.
    • (1988) J Bacteriol , vol.170 , pp. 3855-3863
    • Roof, D.M.1    Roth, J.R.2
  • 41
    • 0033567082 scopus 로고    scopus 로고
    • A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase
    • Shibata, N., Masuda, J., Tobimatsu, T., Toraya, T., Suto, K., Morimoto, Y., and Yasuoka, N. (1999) A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase. Structure Fold Des 7: 997-1008.
    • (1999) Structure Fold Des , vol.7 , pp. 997-1008
    • Shibata, N.1    Masuda, J.2    Tobimatsu, T.3    Toraya, T.4    Suto, K.5    Morimoto, Y.6    Yasuoka, N.7
  • 42
    • 77956220623 scopus 로고    scopus 로고
    • Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates
    • Shibata, N., Tamagaki, H., Hieda, N., Akita, K., Komori, H., Shomura, Y., etal. (2010) Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates. J Biol Chem 285: 26484-26493.
    • (2010) J Biol Chem , vol.285 , pp. 26484-26493
    • Shibata, N.1    Tamagaki, H.2    Hieda, N.3    Akita, K.4    Komori, H.5    Shomura, Y.6
  • 43
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai, V.J., Celic, I., Cole, R.N., Boeke, J.D., and Escalante-Semerena, J.C. (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298: 2390-2392.
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 44
    • 0345240510 scopus 로고
    • Biosynthesis of para-cresolyl cobamide in Sporomusa ovata
    • Stupperich, E., and Eisinger, H.J. (1989a) Biosynthesis of para-cresolyl cobamide in Sporomusa ovata. Arch Microbiol 151: 372-377.
    • (1989) Arch Microbiol , vol.151 , pp. 372-377
    • Stupperich, E.1    Eisinger, H.J.2
  • 45
    • 0242718727 scopus 로고
    • Function and the biosynthesis of unusual corrinoids by a novel activation mechanism of aromatic compounds in anaerobic bacteria
    • Stupperich, E., and Eisinger, H.J. (1989b) Function and the biosynthesis of unusual corrinoids by a novel activation mechanism of aromatic compounds in anaerobic bacteria. Adv Space Res 9: 117-125.
    • (1989) Adv Space Res , vol.9 , pp. 117-125
    • Stupperich, E.1    Eisinger, H.J.2
  • 46
    • 0027244833 scopus 로고
    • Corrinoid-dependent methyl transfer reactions are involved in methanol and 3,4-dimethoxybenzoate metabolism by Sporomusa ovata
    • Stupperich, E., and Konle, R. (1993) Corrinoid-dependent methyl transfer reactions are involved in methanol and 3, 4-dimethoxybenzoate metabolism by Sporomusa ovata. Appl Environ Microbiol 59: 3110-3116.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3110-3116
    • Stupperich, E.1    Konle, R.2
  • 48
    • 0024835782 scopus 로고
    • Identification of phenolyl cobamide from the homoacetogenic bacterium Sporomusa ovata
    • Stupperich, E., Eisinger, H.J., and Kräutler, B. (1989) Identification of phenolyl cobamide from the homoacetogenic bacterium Sporomusa ovata. Eur J Biochem 186: 657-661.
    • (1989) Eur J Biochem , vol.186 , pp. 657-661
    • Stupperich, E.1    Eisinger, H.J.2    Kräutler, B.3
  • 50
    • 0026672422 scopus 로고
    • Purification and characterization of a methanol-induced cobamide-containing protein from Sporomusa ovata
    • Stupperich, E., Aulkemeyer, P., and Eckerskorn, C. (1992) Purification and characterization of a methanol-induced cobamide-containing protein from Sporomusa ovata. Arch Microbiol 158: 370-373.
    • (1992) Arch Microbiol , vol.158 , pp. 370-373
    • Stupperich, E.1    Aulkemeyer, P.2    Eckerskorn, C.3
  • 51
    • 0030859288 scopus 로고    scopus 로고
    • Purification and characterization of CobT, the nicotinate-mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase enzyme from Salmonella typhimurium LT2
    • Trzebiatowski, J.R., and Escalante-Semerena, J.C. (1997) Purification and characterization of CobT, the nicotinate-mononucleotide:5, 6-dimethylbenzimidazole phosphoribosyltransferase enzyme from Salmonella typhimurium LT2. J Biol Chem 272: 17662-17667.
    • (1997) J Biol Chem , vol.272 , pp. 17662-17667
    • Trzebiatowski, J.R.1    Escalante-Semerena, J.C.2
  • 52
    • 0028237621 scopus 로고
    • 1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole, an intermediate in the synthesis of the nucleotide loop of cobalamin
    • 1-(5-phospho-alpha-D-ribosyl)-5, 6-dimethylbenzimidazole, an intermediate in the synthesis of the nucleotide loop of cobalamin. J Bacteriol 176: 3568-3575.
    • (1994) J Bacteriol , vol.176 , pp. 3568-3575
    • Trzebiatowski, J.R.1    O'Toole, G.A.2    Escalante-Semerena, J.C.3
  • 53
    • 0033610894 scopus 로고    scopus 로고
    • CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2
    • Tsang, A.W., and Escalante-Semerena, J.C. (1998) CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5, 6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2. J Biol Chem 273: 31788-31794.
    • (1998) J Biol Chem , vol.273 , pp. 31788-31794
    • Tsang, A.W.1    Escalante-Semerena, J.C.2
  • 54
    • 0032885183 scopus 로고    scopus 로고
    • A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium
    • Van Bibber, M., Bradbeer, C., Clark, N., and Roth, J.R. (1999) A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium. J Bacteriol 181: 5539-5541.
    • (1999) J Bacteriol , vol.181 , pp. 5539-5541
    • Van Bibber, M.1    Bradbeer, C.2    Clark, N.3    Roth, J.R.4
  • 55
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel, H.J., and Bonner, D.M. (1956) Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem 218: 97-106.
    • (1956) J Biol Chem , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 56
    • 58749085019 scopus 로고    scopus 로고
    • New York: Greene Publishing Associates & Wiley Interscience.
    • Voytas, D. (2000) Agarose Gel Electrophoresis. New York: Greene Publishing Associates & Wiley Interscience.
    • (2000) Agarose Gel Electrophoresis
    • Voytas, D.1
  • 58
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way, J.C., Davis, M.A., Morisato, D., Roberts, D.E., and Kleckner, N. (1984) New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32: 369-379.
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5
  • 60
    • 0032492687 scopus 로고    scopus 로고
    • Evidence for axial coordination of 5,6-dimethylbenzimidazole to the cobalt atom of adenosylcobalamin bound to diol dehydratase
    • Yamanishi, M., Yamada, S., Muguruma, H., Murakami, Y., Tobimatsu, T., Ishida, A., etal. (1998) Evidence for axial coordination of 5, 6-dimethylbenzimidazole to the cobalt atom of adenosylcobalamin bound to diol dehydratase. Biochemistry 37: 4799-4803.
    • (1998) Biochemistry , vol.37 , pp. 4799-4803
    • Yamanishi, M.1    Yamada, S.2    Muguruma, H.3    Murakami, Y.4    Tobimatsu, T.5    Ishida, A.6
  • 61
    • 33947167675 scopus 로고    scopus 로고
    • 12 synthesis in Salmonella enterica: evidence that dephosphorylation of adenosylcobalamin-5'-phosphate by the CobC phosphatase is the last step of the pathway
    • 12 synthesis in Salmonella enterica: evidence that dephosphorylation of adenosylcobalamin-5'-phosphate by the CobC phosphatase is the last step of the pathway. J Bacteriol 189: 2210-2218.
    • (2007) J Bacteriol , vol.189 , pp. 2210-2218
    • Zayas, C.L.1    Escalante-Semerena, J.C.2


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