메뉴 건너뛰기




Volumn 188, Issue 23, 2006, Pages 8153-8159

Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

FLAVINE MONONUCLEOTIDE; FLAVINE MONONUCLEOTIDE REDUCTASE; QUERCETIN; SULFUR; UNSPECIFIC MONOOXYGENASE;

EID: 33751560654     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00966-06     Document Type: Article
Times cited : (47)

References (30)
  • 1
    • 0025916089 scopus 로고
    • Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism
    • Anderson, K. S., E. W. Miles, and K. A. Johnson. 1991. Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism. J. Biol. Chem. 266:8020-8033.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8020-8033
    • Anderson, K.S.1    Miles, E.W.2    Johnson, K.A.3
  • 2
    • 0019321483 scopus 로고
    • Circular dichroism studies of acyl-CoA dehydrogenase and electron transfer flavoprotein
    • Auer, H. E., and F. E. Frerman. 1980. Circular dichroism studies of acyl-CoA dehydrogenase and electron transfer flavoprotein. J. Biol. Chem. 255:8157-8163.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8157-8163
    • Auer, H.E.1    Frerman, F.E.2
  • 3
    • 0011897224 scopus 로고
    • A progress report on studies of the activation of molecular oxygen by dihydroflavins
    • V. Massey and C. H. Williams (ed.), Elsevier North-Holland, Inc., New York, N.Y.
    • Bruice, T. C. 1982. A progress report on studies of the activation of molecular oxygen by dihydroflavins, p. 265-277. In V. Massey and C. H. Williams (ed.), Flavins and flavoproteins. Elsevier North-Holland, Inc., New York, N.Y.
    • (1982) Flavins and Flavoproteins , pp. 265-277
    • Bruice, T.C.1
  • 5
    • 0033578717 scopus 로고    scopus 로고
    • Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli
    • Eichhorn, E., J. R. van der Ploeg, and T. Leisinger. 1999. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 247:26639-26646.
    • (1999) J. Biol. Chem. , vol.247 , pp. 26639-26646
    • Eichhorn, E.1    Van Der Ploeg, J.R.2    Leisinger, T.3
  • 6
    • 0029664970 scopus 로고    scopus 로고
    • The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions
    • Fisher, A. J., T. B. Thompson, J. B. Thoden, T. O. Baldwin, and I. Rayment. 1996. The 1.5-Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271:21956-21968.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21956-21968
    • Fisher, A.J.1    Thompson, T.B.2    Thoden, J.B.3    Baldwin, T.O.4    Rayment, I.5
  • 7
    • 18844452128 scopus 로고    scopus 로고
    • Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme
    • Gao, B., and H. R. Ellis. 2005. Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme. Biochem. Biophys. Res. Commun. 331:1137-1145.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1137-1145
    • Gao, B.1    Ellis, H.R.2
  • 8
    • 33644652961 scopus 로고    scopus 로고
    • Functional analysis of acyl-CoA dehydrogenase catalytic residue mutants using surface plasmon resonance and circular dichroism
    • Goetzman, E. S., M. He, T. V. Nguyen, and J. Vockley. 2006. Functional analysis of acyl-CoA dehydrogenase catalytic residue mutants using surface plasmon resonance and circular dichroism. Mol. Gen. Metabol. 87:233-242.
    • (2006) Mol. Gen. Metabol. , vol.87 , pp. 233-242
    • Goetzman, E.S.1    He, M.2    Nguyen, T.V.3    Vockley, J.4
  • 9
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang, X., H. M. Holden, and F. M. Raushel. 2001. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70: 149-180.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 10
    • 0024297340 scopus 로고
    • Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
    • Hyde, C. C., S. A. Ahmed, E. A. Padlan, E. W. Miles, and D. R. Davies. 1988. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263:17857-17871.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.C.1    Ahmed, S.A.2    Padlan, E.A.3    Miles, E.W.4    Davies, D.R.5
  • 11
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 12
    • 0035852823 scopus 로고    scopus 로고
    • Differential transfers of reduced flavin cofactor and product by bacterial flavin reductase to luciferase
    • Jeffers, C. E., and S.-C. Tu. 2001. Differential transfers of reduced flavin cofactor and product by bacterial flavin reductase to luciferase. Biochemistry 40:1749-1754.
    • (2001) Biochemistry , vol.40 , pp. 1749-1754
    • Jeffers, C.E.1    Tu, S.-C.2
  • 13
    • 0346736498 scopus 로고    scopus 로고
    • Complex formation between Vibrio harveyi luciferase and monomeric NADPH:FMN oxidoreductase
    • Jeffers, C. E., J. C. Nichols, and S.-C. Tu. 2003. Complex formation between Vibrio harveyi luciferase and monomeric NADPH:FMN oxidoreductase. Biochemistry 42:529-534.
    • (2003) Biochemistry , vol.42 , pp. 529-534
    • Jeffers, C.E.1    Nichols, J.C.2    Tu, S.-C.3
  • 14
    • 24944534515 scopus 로고    scopus 로고
    • Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase
    • Kantz, A., F. Chin, N. Nallamothu, T. Nguyen, and G. T. Gassner. 2005. Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase. Arch. Biochem. Biophys. 442:102-116.
    • (2005) Arch. Biochem. Biophys. , vol.442 , pp. 102-116
    • Kantz, A.1    Chin, F.2    Nallamothu, N.3    Nguyen, T.4    Gassner, G.T.5
  • 15
    • 0034010828 scopus 로고    scopus 로고
    • Riding the sulfur cycle - Metabolism of sulfonates and sulfate esters in gram-negative bacteria
    • Kertesz, M. A. 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
  • 16
    • 0027411687 scopus 로고
    • Proteins induced by sulfate limitation in Escherichia coli, Pseudomonas putida, or Staphylococcus aureus
    • Kertesz, M. A., T. Leisinger, and A. M. Cook. 1993. Proteins induced by sulfate limitation in Escherichia coli, Pseudomonas putida, or Staphylococcus aureus. J. Bacteriol. 175:1187-1190.
    • (1993) J. Bacteriol. , vol.175 , pp. 1187-1190
    • Kertesz, M.A.1    Leisinger, T.2    Cook, A.M.3
  • 17
    • 2442536096 scopus 로고    scopus 로고
    • Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between sequential active sites
    • Kim, J., and F. M. Raushel. 2004. Perforation of the tunnel wall in carbamoyl phosphate synthetase derails the passage of ammonia between sequential active sites. Biochemistry 43:5334-5340.
    • (2004) Biochemistry , vol.43 , pp. 5334-5340
    • Kim, J.1    Raushel, F.M.2
  • 18
    • 0032514724 scopus 로고    scopus 로고
    • Mechanism of reduced flavin transfer from Vibrio harveyi NADPH:FMN oxidoreductase to luciferase
    • Lei, B., and S.-C. Tu. 1998. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH:FMN oxidoreductase to luciferase. Biochemistry 37:14623-14629.
    • (1998) Biochemistry , vol.37 , pp. 14623-14629
    • Lei, B.1    Tu, S.-C.2
  • 19
    • 0038746745 scopus 로고    scopus 로고
    • 2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase
    • 2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. Biochemistry 42:7509-7517.
    • (2003) Biochemistry , vol.42 , pp. 7509-7517
    • Louie, T.M.1    Xie, X.S.2    Xun, L.3
  • 20
    • 0010142265 scopus 로고    scopus 로고
    • Tryptophan synthase: A multienzyme complex with an intramolecular tunnel
    • Miles, E. W. 2001. Tryptophan synthase: a multienzyme complex with an intramolecular tunnel. Chem. Rec. I:140-151.
    • (2001) Chem. Rec. , vol.1 , pp. 140-151
    • Miles, E.W.1
  • 21
    • 0034595290 scopus 로고    scopus 로고
    • Synchronization of the three reaction centers within carbamoyl phosphate synthetase
    • Miles, B. W., and F. M. Raushel. 2000. Synchronization of the three reaction centers within carbamoyl phosphate synthetase. Biochemistry 39:5051-5056.
    • (2000) Biochemistry , vol.39 , pp. 5051-5056
    • Miles, B.W.1    Raushel, F.M.2
  • 22
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles, E. W., S. Rhee, and D. R. Davies. 1999. The molecular basis of substrate channeling. J. Biol. Chem. 274:12193-12196.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12193-12196
    • Miles, E.W.1    Rhee, S.2    Davies, D.R.3
  • 23
    • 0025895417 scopus 로고
    • Physiological significance of metabolic channelling
    • Ovadi, J. 1991. Physiological significance of metabolic channelling. J. Theor. Biol. 152:1-22.
    • (1991) J. Theor. Biol. , vol.152 , pp. 1-22
    • Ovadi, J.1
  • 25
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P. A. 1987. Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56:89-124.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 26
    • 0037131277 scopus 로고    scopus 로고
    • Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia
    • Thoden, J. B., X. Huang, F. M. Raushel, and H. M. Holden. 2002. Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia. J. Biol. Chem. 277:39722-39727.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39722-39727
    • Thoden, J.B.1    Huang, X.2    Raushel, F.M.3    Holden, H.M.4
  • 27
    • 0035205486 scopus 로고    scopus 로고
    • Reduced flavin: Donor and acceptor enzymes and mechanisms of channeling
    • Tu, S.-C. 2001. Reduced flavin: donor and acceptor enzymes and mechanisms of channeling. Antioxid. Redox Signal. 3:881-897.
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 881-897
    • Tu, S.-C.1
  • 28
    • 0034927394 scopus 로고    scopus 로고
    • Sulfonate-sulfur metabolism and its regulation in Escherichia coli
    • van der Ploeg, J. R., E. Eichhorn, and T. Leisinger. 2001. Sulfonate-sulfur metabolism and its regulation in Escherichia coli. Arch. Microbiol. 176:1-8.
    • (2001) Arch. Microbiol. , vol.176 , pp. 1-8
    • Van Der Ploeg, J.R.1    Eichhorn, E.2    Leisinger, T.3
  • 29
    • 0032856359 scopus 로고    scopus 로고
    • The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl
    • van Der Ploeg, J. R., R. Iwanicka-Nowicka, T. Bykowski, M. M. Hryniewicz, and T. Leisinger. 1999. The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl. J. Biol. Chem. 274:29358-29365.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29358-29365
    • Van Der Ploeg, J.R.1    Iwanicka-Nowicka, R.2    Bykowski, T.3    Hryniewicz, M.M.4    Leisinger, T.5
  • 30
    • 0017831143 scopus 로고
    • Chemical approaches to the study of enzymes catalyzing redox transformations
    • Walsh, C. 1978. Chemical approaches to the study of enzymes catalyzing redox transformations. Annu. Rev. Biochem. 47:881-931.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 881-931
    • Walsh, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.