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Volumn 190, Issue 2, 2008, Pages 159-168

Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: Purification of sulfoacetaldehyde dehydrogenase

Author keywords

Assimilation of taurine nitrogen; DUF81; Sulfoacetaldehyde dehydrogenase; Sulfoacetate exporter; Taurine; Taurine:pyruvate aminotransferase

Indexed keywords

ABC TRANSPORTER; ACETIC ACID DERIVATIVE; ALDEHYDE DEHYDROGENASE; AMINO ACID; AMINOTRANSFERASE; MONOMER; NITROGEN; TAURINE; TETRAMER;

EID: 47349097845     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-008-0386-2     Document Type: Article
Times cited : (31)

References (60)
  • 1
    • 0000570450 scopus 로고
    • Taurine in marine invertebrates
    • JA Allen MR Garrett 1971 Taurine in marine invertebrates Adv Mar Biol 9 205 253
    • (1971) Adv Mar Biol , vol.9 , pp. 205-253
    • Allen, J.A.1    Garrett, M.R.2
  • 4
    • 34249073405 scopus 로고    scopus 로고
    • Roseovarius sp. strain 217: Aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase
    • MI Baldock K Denger THM Smits AM Cook 2007 Roseovarius sp. strain 217: aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase FEMS Microbiol Lett 271 202 206
    • (2007) FEMS Microbiol Lett , vol.271 , pp. 202-206
    • Baldock, M.I.1    Denger, K.2    Smits, T.H.M.3    Cook, A.M.4
  • 5
    • 0000288758 scopus 로고
    • The marine gram-negative eubacteria: Genera Photobacterium, Beneckea, Alteromonas, Pseudomonas and Alcaligenes
    • Springer Berlin
    • Baumann P, Baumann L (1981) The marine gram-negative eubacteria: genera Photobacterium, Beneckea, Alteromonas, Pseudomonas and Alcaligenes. In: Starr MP, Stolp H, Trüper HG, Balows A, Schlegel H-G (eds) The prokaryotes. Springer, Berlin, pp 1302-1331
    • (1981) The Prokaryotes , pp. 1302-1331
    • Baumann, P.1    Baumann, L.2    Starr, M.P.3    Stolp, H.4    Trüper, H.G.5    Balows, A.6    Schlegel, H.-G.7
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M Bradford 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
  • 8
    • 1942473591 scopus 로고    scopus 로고
    • Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans
    • (Reading, UK)
    • Brüggemann C, Denger K, Cook AM, Ruff J (2004) Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans. Microbiology (Reading, UK) 150:805-816
    • (2004) Microbiology , vol.150 , pp. 805-816
    • Brüggemann, C.1    Denger, K.2    Cook, A.M.3    Ruff, J.4
  • 9
    • 0032988794 scopus 로고    scopus 로고
    • Rhodococcus spp. utilize taurine (2-aminoethanesulfonate) as sole source of carbon, energy, nitrogen and sulfur for aerobic respiratory growth
    • C-C Chien ER Leadbetter W Godchaux III 1999 Rhodococcus spp. utilize taurine (2-aminoethanesulfonate) as sole source of carbon, energy, nitrogen and sulfur for aerobic respiratory growth FEMS Microbiol Lett 176 333 337
    • (1999) FEMS Microbiol Lett , vol.176 , pp. 333-337
    • Chien, C.-C.1    Leadbetter, E.R.2    Godchaux III, W.3
  • 11
    • 84934442484 scopus 로고    scopus 로고
    • Metabolism of taurine in microorganisms: A primer in molecular diversity?
    • AM Cook K Denger 2006 Metabolism of taurine in microorganisms: a primer in molecular diversity? Adv Exp Med Biol 583 3 13
    • (2006) Adv Exp Med Biol , vol.583 , pp. 3-13
    • Cook, A.M.1    Denger, K.2
  • 12
    • 0019719787 scopus 로고
    • S-Triazines as nitrogen sources for bacteria
    • AM Cook R Hütter 1981 s-Triazines as nitrogen sources for bacteria J Agric Food Chem 29 1135 1143
    • (1981) J Agric Food Chem , vol.29 , pp. 1135-1143
    • Cook, A.M.1    Hütter, R.2
  • 13
    • 0018133572 scopus 로고
    • Metabolite concentrations in Alcaligenes eutrophus H16 and a mutant defective in poly-β-hydroxybutyrate synthesis
    • AM Cook HG Schlegel 1978 Metabolite concentrations in Alcaligenes eutrophus H16 and a mutant defective in poly-β-hydroxybutyrate synthesis Arch Microbiol 119 231 235
    • (1978) Arch Microbiol , vol.119 , pp. 231-235
    • Cook, A.M.1    Schlegel, H.G.2
  • 14
    • 0032032354 scopus 로고    scopus 로고
    • Conversion of taurine into N-chlorotaurine (taurine chloramine) and sulphoacetaldehyde in response to oxidative stress
    • C Cunningham KF Tipton HBF Dixon 1998 Conversion of taurine into N-chlorotaurine (taurine chloramine) and sulphoacetaldehyde in response to oxidative stress Biochem J 330 939 945
    • (1998) Biochem J , vol.330 , pp. 939-945
    • Cunningham, C.1    Tipton, K.F.2    Dixon, H.B.F.3
  • 15
    • 0035878925 scopus 로고    scopus 로고
    • Sulfoacetaldehyde sulfo-lyase [EC 4.4.1.12] from Desulfonispora thiosulfatigenes: Purification, properties and primary sequence
    • K Denger J Ruff U Rein AM Cook 2001 Sulfoacetaldehyde sulfo-lyase [EC 4.4.1.12] from Desulfonispora thiosulfatigenes: purification, properties and primary sequence Biochem J 357 581 586
    • (2001) Biochem J , vol.357 , pp. 581-586
    • Denger, K.1    Ruff, J.2    Rein, U.3    Cook, A.M.4
  • 16
    • 3142707324 scopus 로고    scopus 로고
    • Rhodococcus opacus expresses the xsc gene to utilize taurine as a carbon source or as a nitrogen source but not as a sulfur source
    • K Denger J Ruff D Schleheck AM Cook 2004 Rhodococcus opacus expresses the xsc gene to utilize taurine as a carbon source or as a nitrogen source but not as a sulfur source Microbiology 150 1859 1867
    • (2004) Microbiology , vol.150 , pp. 1859-1867
    • Denger, K.1    Ruff, J.2    Schleheck, D.3    Cook, A.M.4
  • 17
  • 18
    • 33750957249 scopus 로고    scopus 로고
    • Genome-enabled analysis of the utilization of taurine as sole source of carbon or nitrogen by Rhodobacter sphaeroides 2.4.1
    • K Denger THM Smits AM Cook 2006 Genome-enabled analysis of the utilization of taurine as sole source of carbon or nitrogen by Rhodobacter sphaeroides 2.4.1 Microbiology 152 3167 3174
    • (2006) Microbiology , vol.152 , pp. 3167-3174
    • Denger, K.1    Smits, T.H.M.2    Cook, A.M.3
  • 19
    • 0025817783 scopus 로고
    • Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system
    • J Desomer M Crespi M Van Montagu 1991 Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system Mol Microbiol 5 2115 2124
    • (1991) Mol Microbiol , vol.5 , pp. 2115-2124
    • Desomer, J.1    Crespi, M.2    Van Montagu, M.3
  • 20
    • 0030770813 scopus 로고    scopus 로고
    • Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli
    • E Eichhorn JR van der Ploeg MA Kertesz T Leisinger 1997 Characterization of α-ketoglutarate-dependent taurine dioxygenase from Escherichia coli J Biol Chem 272 23031 23036
    • (1997) J Biol Chem , vol.272 , pp. 23031-23036
    • Eichhorn, E.1    Van Der Ploeg, J.R.2    Kertesz, M.A.3    Leisinger, T.4
  • 21
    • 0034015228 scopus 로고    scopus 로고
    • Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems
    • E Eichhorn JR van der Ploeg T Leisinger 2000 Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems J Bacteriol 182 2687 2795
    • (2000) J Bacteriol , vol.182 , pp. 2687-2795
    • Eichhorn, E.1    Van Der Ploeg, J.R.2    Leisinger, T.3
  • 22
    • 33947441549 scopus 로고
    • Erythrina alkaloids. XIV. Isolation and characterization of erysothiovine and erysothiopine, new alkaloids containing sulfur
    • K Folkers F Koniuszy J Shavel 1944 Erythrina alkaloids. XIV. Isolation and characterization of erysothiovine and erysothiopine, new alkaloids containing sulfur J Amer Chem Soc 66 1083 1087
    • (1944) J Amer Chem Soc , vol.66 , pp. 1083-1087
    • Folkers, K.1    Koniuszy, F.2    Shavel, J.3
  • 24
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • J Gough K Karplus R Hughey C Chothia 2001 Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure J Mol Biol 313 903 919
    • (2001) J Mol Biol , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 25
    • 0023776626 scopus 로고
    • The biosynthesis of sulfoquinovosyldiacylglycerol: Studies with groundnut (Arachis hypogaea) leaves
    • SD Gupta PS Sastry 1988 The biosynthesis of sulfoquinovosyldiacylglycerol: studies with groundnut (Arachis hypogaea) leaves Arch Biochem Biophys 260 125 133
    • (1988) Arch Biochem Biophys , vol.260 , pp. 125-133
    • Gupta, S.D.1    Sastry, P.S.2
  • 26
    • 0026595620 scopus 로고
    • Physiological actions of taurine
    • RJ Huxtable 1992 Physiological actions of taurine Physiol Rev 72 101 163
    • (1992) Physiol Rev , vol.72 , pp. 101-163
    • Huxtable, R.J.1
  • 27
    • 0012016405 scopus 로고
    • Bacterial degradation of taurine
    • K Ikeda H Yamada S Tanaka 1963 Bacterial degradation of taurine Biochem J 54 312 316
    • (1963) Biochem J , vol.54 , pp. 312-316
    • Ikeda, K.1    Yamada, H.2    Tanaka, S.3
  • 29
    • 0028307260 scopus 로고
    • Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid
    • F Junker JA Field F Bangerter K Ramsteiner H-P Kohler CL Joannou JR Mason T Leisinger AM Cook 1994 Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid Biochem J 300 429 436
    • (1994) Biochem J , vol.300 , pp. 429-436
    • Junker, F.1    Field, J.A.2    Bangerter, F.3    Ramsteiner, K.4    Kohler, H.-P.5    Joannou, C.L.6    Mason, J.R.7    Leisinger, T.8    Cook, A.M.9
  • 30
    • 0034057728 scopus 로고    scopus 로고
    • The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313
    • A Kahnert P Vermeij C Wietek P James T Leisinger MA Kertesz 2000 The ssu locus plays a key role in organosulfur metabolism in Pseudomonas putida S-313 J Bacteriol 182 2869 2878
    • (2000) J Bacteriol , vol.182 , pp. 2869-2878
    • Kahnert, A.1    Vermeij, P.2    Wietek, C.3    James, P.4    Leisinger, T.5    Kertesz, M.A.6
  • 31
    • 0034010828 scopus 로고    scopus 로고
    • Riding the sulfur cycle - Metabolism of sulfonates and sulfate esters in Gram-negative bacteria
    • MA Kertesz 2000 Riding the sulfur cycle - metabolism of sulfonates and sulfate esters in Gram-negative bacteria FEMS Microbiol Rev 24 135 175
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 135-175
    • Kertesz, M.A.1
  • 32
    • 0031451030 scopus 로고    scopus 로고
    • Metabolism of sulfoacetate by environmental Aureobacterium sp. and Comamonas acidovorans isolates
    • JE King JP Quinn 1997 Metabolism of sulfoacetate by environmental Aureobacterium sp. and Comamonas acidovorans isolates Microbiology 143 3907 3912
    • (1997) Microbiology , vol.143 , pp. 3907-3912
    • King, J.E.1    Quinn, J.P.2
  • 33
    • 0015024004 scopus 로고
    • Formation of sulfoacetaldehyde from taurine in bacterial extracts
    • H Kondo H Anada K Ohsawa M Ishimoto 1971 Formation of sulfoacetaldehyde from taurine in bacterial extracts J Biochem 69 621 623
    • (1971) J Biochem , vol.69 , pp. 621-623
    • Kondo, H.1    Anada, H.2    Ohsawa, K.3    Ishimoto, M.4
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature (London, UK) 227 680 685
    • (1970) Nature (London, UK) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0033694757 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia
    • H Laue AM Cook 2000 Biochemical and molecular characterization of taurine:pyruvate aminotransferase from the anaerobe Bilophila wadsworthia Eur J Biochem 267 6841 6848
    • (2000) Eur J Biochem , vol.267 , pp. 6841-6848
    • Laue, H.1    Cook, A.M.2
  • 36
    • 0033862434 scopus 로고    scopus 로고
    • Purification, properties and primary structure of alanine dehydrogenase involved in taurine metabolism in the anaerobe Bilophila wadsworthia
    • H Laue AM Cook 2000 Purification, properties and primary structure of alanine dehydrogenase involved in taurine metabolism in the anaerobe Bilophila wadsworthia Arch Microbiol 174 162 167
    • (2000) Arch Microbiol , vol.174 , pp. 162-167
    • Laue, H.1    Cook, A.M.2
  • 37
    • 0030980121 scopus 로고    scopus 로고
    • Taurine reduction in anaerobic respiration of Bilophila wadsworthia RZATAU
    • H Laue K Denger AM Cook 1997 Taurine reduction in anaerobic respiration of Bilophila wadsworthia RZATAU Appl Environ Microbiol 63 2016 2021
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2016-2021
    • Laue, H.1    Denger, K.2    Cook, A.M.3
  • 38
    • 33745726449 scopus 로고    scopus 로고
    • Identification of Bilophila wadsworthia in enrichment cultures by specific PCR which targets the taurine:pyruvate aminotransferase gene
    • H Laue THM Smits U Schumacher M Claros R Hartemink AM Cook 2006 Identification of Bilophila wadsworthia in enrichment cultures by specific PCR which targets the taurine:pyruvate aminotransferase gene FEMS Microbiol Lett 261 74 79
    • (2006) FEMS Microbiol Lett , vol.261 , pp. 74-79
    • Laue, H.1    Smits, T.H.M.2    Schumacher, U.3    Claros, M.4    Hartemink, R.5    Cook, A.M.6
  • 39
    • 0015526513 scopus 로고
    • The metabolism of glyceryl [35S]sulfoquinovoside by the coral tree, Erythrina crista-galli, and alfalfa, Medicago sativa
    • RF Lee AA Benson 1972 The metabolism of glyceryl [35S]sulfoquinovoside by the coral tree, Erythrina crista-galli, and alfalfa, Medicago sativa Biochim Biophys Acta 261 35 37
    • (1972) Biochim Biophys Acta , vol.261 , pp. 35-37
    • Lee, R.F.1    Benson, A.A.2
  • 40
    • 0026655335 scopus 로고
    • Aldehyde dehydrogenases and their role in carcinogenesis
    • R Lindahl 1992 Aldehyde dehydrogenases and their role in carcinogenesis Crit Rev Biochem Mol Biol 27 283 335
    • (1992) Crit Rev Biochem Mol Biol , vol.27 , pp. 283-335
    • Lindahl, R.1
  • 41
    • 8544268158 scopus 로고
    • Nutrition and metabolism of marine bacteria VIII: Tricarboxylic acid cycle enzymes in a marine bacterium and their response to inorganic salts
    • RA MacLeod A Hori 1960 Nutrition and metabolism of marine bacteria VIII: tricarboxylic acid cycle enzymes in a marine bacterium and their response to inorganic salts J Bacteriol 80 464 471
    • (1960) J Bacteriol , vol.80 , pp. 464-471
    • MacLeod, R.A.1    Hori, A.2
  • 42
    • 0001288726 scopus 로고
    • Sulfocarbohydrate metabolism 1. Bacterial production and utilization of sulfoacetate
    • HL Martelli AA Benson 1964 Sulfocarbohydrate metabolism 1. Bacterial production and utilization of sulfoacetate Biochim Biophys Acta 93 169 171
    • (1964) Biochim Biophys Acta , vol.93 , pp. 169-171
    • Martelli, H.L.1    Benson, A.A.2
  • 43
    • 0014944837 scopus 로고
    • Biochemistry of sulfonic compounds III. Formation of a two-carbon compound during the oxidation of sulfoacetate by a Pseudomonas strain
    • HL Martelli SM Sousa 1970 Biochemistry of sulfonic compounds III. Formation of a two-carbon compound during the oxidation of sulfoacetate by a Pseudomonas strain Biochim Biophys Acta 208 110 115
    • (1970) Biochim Biophys Acta , vol.208 , pp. 110-115
    • Martelli, H.L.1    Sousa, S.M.2
  • 44
    • 0343464778 scopus 로고
    • Erythrina alkaloids
    • Pelletier SW (ed) Van Nostrand Reihhold, New York
    • Mondon A (1970) Erythrina alkaloids. In: Pelletier SW (ed) Chemistry of the alkaloids. Van Nostrand Reihhold, New York, pp 173-198
    • (1970) Chemistry of the Alkaloids , pp. 173-198
    • Mondon, A.1
  • 45
    • 0016279265 scopus 로고
    • Rhodopseudomonas globiformis, sp. n., a new species of the Rhodospirillaceae
    • N Pfennig 1974 Rhodopseudomonas globiformis, sp. n., a new species of the Rhodospirillaceae Arch Microbiol 100 197 206
    • (1974) Arch Microbiol , vol.100 , pp. 197-206
    • Pfennig, N.1
  • 46
    • 25644459307 scopus 로고    scopus 로고
    • Functional genomics and expression analysis of the Corynebacterium glutamicum fpr2-cysIXHDNYZ gene cluster involved in assimilatory sulphate reduction
    • C Rückert DJ Koch DA Rey A Albersmeier S Mormann A Pühler J Kalinowski 2005 Functional genomics and expression analysis of the Corynebacterium glutamicum fpr2-cysIXHDNYZ gene cluster involved in assimilatory sulphate reduction BMC Genomics 6 121
    • (2005) BMC Genomics , vol.6 , pp. 121
    • Rückert, C.1    Koch, D.J.2    Rey, D.A.3    Albersmeier, A.4    Mormann, S.5    Pühler, A.6    Kalinowski, J.7
  • 47
    • 0037440030 scopus 로고    scopus 로고
    • Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: Purification from Alcaligenes defragrans and gene clusters in taurine degradation
    • J Ruff K Denger AM Cook 2003 Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation Biochem J 369 275 285
    • (2003) Biochem J , vol.369 , pp. 275-285
    • Ruff, J.1    Denger, K.2    Cook, A.M.3
  • 49
    • 0347307731 scopus 로고
    • Sulfonic acids in algae
    • Japanese-society-of-plant-physiologists (ed) The University of Tokyo Press, Tokyo
    • Shibuya I, Yagi T, Benson AA (1963) Sulfonic acids in algae. In: Japanese-society-of-plant-physiologists (ed) Studies on microalgae and photosynthetic bacteria. The University of Tokyo Press, Tokyo, pp 627-636
    • (1963) Studies on Microalgae and Photosynthetic Bacteria , pp. 627-636
    • Shibuya, I.1    Yagi, T.2    Benson, A.A.3
  • 50
    • 0023082772 scopus 로고
    • Sulfate: Turbidimetric and nephelometric methods
    • B Sörbo 1987 Sulfate: turbidimetric and nephelometric methods Methods Enzymol 143 3 6
    • (1987) Methods Enzymol , vol.143 , pp. 3-6
    • Sörbo, B.1
  • 51
    • 23844434411 scopus 로고    scopus 로고
    • Isethionate as a product from taurine during nitrogen-limited growth of Klebsiella oxytoca TAU-N1
    • K Styp von Rekowski K Denger AM Cook 2005 Isethionate as a product from taurine during nitrogen-limited growth of Klebsiella oxytoca TAU-N1 Arch Microbiol 183 325 330
    • (2005) Arch Microbiol , vol.183 , pp. 325-330
    • Styp Von Rekowski, K.1    Denger, K.2    Cook, A.M.3
  • 53
    • 0029815280 scopus 로고    scopus 로고
    • Identification of sulfate starvation-regulated genes in Escherichia coli: A gene cluster involved in the utilization of taurine as a sulfur source
    • JR van der Ploeg M Weiss E Saller H Nashimoto N Saito MA Kertesz T Leisinger 1996 Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source J Bacteriol 178 5438 5446
    • (1996) J Bacteriol , vol.178 , pp. 5438-5446
    • Van Der Ploeg, J.R.1    Weiss, M.2    Saller, E.3    Nashimoto, H.4    Saito, N.5    Kertesz, M.A.6    Leisinger, T.7
  • 55
    • 33645539868 scopus 로고    scopus 로고
    • The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine
    • S Weinitschke K Denger THM Smits K Hollemeyer AM Cook 2006 The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine Microbiology 152 1179 1186
    • (2006) Microbiology , vol.152 , pp. 1179-1186
    • Weinitschke, S.1    Denger, K.2    Smits, T.H.M.3    Hollemeyer, K.4    Cook, A.M.5
  • 56
    • 17644420662 scopus 로고    scopus 로고
    • Sulfoacetaldehyde is excreted quantitatively by Acinetobacter calcoaceticus SW1 during growth with taurine as sole source of nitrogen
    • Weinitschke S, Styp von Rekowski K, Denger K, Cook AM (2005) Sulfoacetaldehyde is excreted quantitatively by Acinetobacter calcoaceticus SW1 during growth with taurine as sole source of nitrogen. Microbiology 151:1285-1290
    • (2005) Microbiology , vol.151 , pp. 1285-1290
    • Weinitschke, S.1    Von Styp Rekowski, K.2    Denger, K.3    Cook, A.M.4
  • 57
    • 0023841769 scopus 로고
    • Cysteinesulfonate and β-sulfopyruvate metabolism. Partitioning between decarboxylation, transamination, and reduction pathways
    • CL Weinstein OW Griffith 1988 Cysteinesulfonate and β-sulfopyruvate metabolism. Partitioning between decarboxylation, transamination, and reduction pathways J Biol Chem 263 3735 3743
    • (1988) J Biol Chem , vol.263 , pp. 3735-3743
    • Weinstein, C.L.1    Griffith, O.W.2
  • 59
    • 38749102812 scopus 로고    scopus 로고
    • The GntR-like regulator TauR activates expression of taurine utilization genes in Rhodobacter capsulatus
    • J Wiethaus B Schubert Y Pfander F Narberhaus B Masepohl 2008 The GntR-like regulator TauR activates expression of taurine utilization genes in Rhodobacter capsulatus J Bacteriol 190 487 493
    • (2008) J Bacteriol , vol.190 , pp. 487-493
    • Wiethaus, J.1    Schubert, B.2    Pfander, Y.3    Narberhaus, F.4    Masepohl, B.5
  • 60
    • 0036848921 scopus 로고    scopus 로고
    • Unusual organic osmolytes in deep-sea animals: Adaptations to hydrostatic pressure and other perturbants
    • PH Yancey WR Blake J Conley 2002 Unusual organic osmolytes in deep-sea animals: adaptations to hydrostatic pressure and other perturbants Comp Biochem Physiol A Mol Integr Physiol 133 667 676
    • (2002) Comp Biochem Physiol a Mol Integr Physiol , vol.133 , pp. 667-676
    • Yancey, P.H.1    Blake, W.R.2    Conley, J.3


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