메뉴 건너뛰기




Volumn 1767, Issue 12, 2007, Pages 1401-1411

Identification of amino acid residues participating in the energy coupling and proton transport of Streptomyces coelicolor A3(2) H+-pyrophosphatase

Author keywords

Energy coupling; H+ pyrophosphatase; Proton pump; Random mutagenesis

Indexed keywords

ALANINE; AMINO ACID; GLYCINE; HYDROGEN; INORGANIC PYROPHOSPHATASE; PHENYLALANINE; PROLINE; THREONINE; VALINE;

EID: 36549050793     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.09.007     Document Type: Article
Times cited : (14)

References (44)
  • 2
    • 0031806558 scopus 로고    scopus 로고
    • A pyrophosphate synthase gene: molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum
    • Baltscheffsky M., Nadanaciva S., and Schultz A. A pyrophosphate synthase gene: molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum. Biochim. Biophys. Acta 1364 (1998) 301-306
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 301-306
    • Baltscheffsky, M.1    Nadanaciva, S.2    Schultz, A.3
  • 4
    • 0035209342 scopus 로고    scopus 로고
    • +-pyrophosphatases: from the evolutionary backwaters into the mainstream
    • +-pyrophosphatases: from the evolutionary backwaters into the mainstream. Trends Plant Sci. 6 (2001) 206-211
    • (2001) Trends Plant Sci. , vol.6 , pp. 206-211
    • Drozdowicz, Y.M.1    Rea, A.2
  • 5
    • 0024306480 scopus 로고
    • Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean
    • Maeshima M., and Yoshida S. Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean. J. Biol. Chem. 264 (1989) 20068-20073
    • (1989) J. Biol. Chem. , vol.264 , pp. 20068-20073
    • Maeshima, M.1    Yoshida, S.2
  • 7
    • 0032555653 scopus 로고    scopus 로고
    • Presence of a plant-like proton-pumping pyrophosphatase in acidocalcisomes of Trypanosoma cruzi
    • Scott D.A., de Souza W., Benchimol M., Zhong L., Lu G.G., Moreno S.N.J., and Docampo R. Presence of a plant-like proton-pumping pyrophosphatase in acidocalcisomes of Trypanosoma cruzi. J. Biol. Chem. 273 (1998) 22151-22158
    • (1998) J. Biol. Chem. , vol.273 , pp. 22151-22158
    • Scott, D.A.1    de Souza, W.2    Benchimol, M.3    Zhong, L.4    Lu, G.G.5    Moreno, S.N.J.6    Docampo, R.7
  • 9
    • 10944262311 scopus 로고    scopus 로고
    • +-pyrophosphatase of Rhodospirillum rubrum is predominantly located in polyphosphate-rich acidocalcisomes
    • +-pyrophosphatase of Rhodospirillum rubrum is predominantly located in polyphosphate-rich acidocalcisomes. J. Biol. Chem. 279 (2004) 51193-51202
    • (2004) J. Biol. Chem. , vol.279 , pp. 51193-51202
    • Seufferheld, M.1    Lea, C.R.2    Vieira, M.3    Oldfield, E.4    Docampo, R.5
  • 10
    • 0032725586 scopus 로고    scopus 로고
    • A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate-energized pumps
    • Drozdowicz Y.M., Lu Y.P., Patel V., Fitz-Gibbon S., Miller J.H., and Rea P.A. A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate-energized pumps. FEBS Lett. 460 (1999) 505-512
    • (1999) FEBS Lett. , vol.460 , pp. 505-512
    • Drozdowicz, Y.M.1    Lu, Y.P.2    Patel, V.3    Fitz-Gibbon, S.4    Miller, J.H.5    Rea, P.A.6
  • 11
  • 14
    • 0031992095 scopus 로고    scopus 로고
    • +-pyrophosphatase and its developmental expression in growing hypocotyls of mung bean
    • +-pyrophosphatase and its developmental expression in growing hypocotyls of mung bean. Plant Physiol. 116 (1998) 589-597
    • (1998) Plant Physiol. , vol.116 , pp. 589-597
    • Nakanishi, Y.1    Maeshima, M.2
  • 15
    • 0000933998 scopus 로고
    • Dynamics of tonoplast proton pumps and other tonoplast proteins of Mesembryanthemum crystallinum L. during the induction of crassulacean acid metabolism
    • Bremberger C., and Lüttge U. Dynamics of tonoplast proton pumps and other tonoplast proteins of Mesembryanthemum crystallinum L. during the induction of crassulacean acid metabolism. Planta 188 (1992) 575-580
    • (1992) Planta , vol.188 , pp. 575-580
    • Bremberger, C.1    Lüttge, U.2
  • 17
    • 3843077423 scopus 로고    scopus 로고
    • Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics
    • López-Marqués R.L., Pérez-Castiñeira J.R., Losada M., and Serrano A. Differential regulation of soluble and membrane-bound inorganic pyrophosphatases in the photosynthetic bacterium Rhodospirillum rubrum provides insights into pyrophosphate-based stress bioenergetics. J. Bacteriol. 186 (2004) 5418-5426
    • (2004) J. Bacteriol. , vol.186 , pp. 5418-5426
    • López-Marqués, R.L.1    Pérez-Castiñeira, J.R.2    Losada, M.3    Serrano, A.4
  • 20
    • 0028893719 scopus 로고
    • 634 for inhibition by maleimides but not catalysis
    • 634 for inhibition by maleimides but not catalysis. J. Biol. Chem. 270 (1995) 2630-2635
    • (1995) J. Biol. Chem. , vol.270 , pp. 2630-2635
    • Kim, E.J.1    Zhen, R.G.2    Rea, P.A.3
  • 21
    • 0030868387 scopus 로고    scopus 로고
    • +-pyrophosphatase by N, N′-dicyclohexylcarbodiimide
    • +-pyrophosphatase by N, N′-dicyclohexylcarbodiimide. J. Biol. Chem. 272 (1997) 22340-22348
    • (1997) J. Biol. Chem. , vol.272 , pp. 22340-22348
    • Zhen, R.G.1    Kim, E.J.2    Rea, P.A.3
  • 27
    • 0037147233 scopus 로고    scopus 로고
    • +-pyrophosphatase of Carboxydothermus hydrogenoformans
    • +-pyrophosphatase of Carboxydothermus hydrogenoformans. J. Biol. Chem. 277 (2002) 49651-49654
    • (2002) J. Biol. Chem. , vol.277 , pp. 49651-49654
    • Belogurov, G.A.1    Lahti, R.2
  • 28
    • 4544273344 scopus 로고    scopus 로고
    • +-pyrophosphatase of Streptomyces coelicolor determined by cysteine-scanning mutagenesis
    • +-pyrophosphatase of Streptomyces coelicolor determined by cysteine-scanning mutagenesis. J. Biol. Chem. 279 (2004) 35106-35112
    • (2004) J. Biol. Chem. , vol.279 , pp. 35106-35112
    • Mimura, H.1    Nakanishi, Y.2    Hirono, M.3    Maeshima, M.4
  • 30
    • 21244505069 scopus 로고    scopus 로고
    • +-pyrophosphatase of Streptomyces coelicolor and its implication in redox control and structure
    • +-pyrophosphatase of Streptomyces coelicolor and its implication in redox control and structure. FEBS Lett. 579 (2005) 3625-3631
    • (2005) FEBS Lett. , vol.579 , pp. 3625-3631
    • Mimura, H.1    Nakanishi, Y.2    Maeshima, M.3
  • 32
    • 0032052278 scopus 로고    scopus 로고
    • An improved PCR-mutagenesis strategy for two-site mutagenesis or sequence swapping between related genes
    • Kirsch R.D., and Joly E. An improved PCR-mutagenesis strategy for two-site mutagenesis or sequence swapping between related genes. Nucleic Acids Res. 26 (1998) 1848-1850
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1848-1850
    • Kirsch, R.D.1    Joly, E.2
  • 33
    • 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.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 24644433425 scopus 로고    scopus 로고
    • +-pyrophosphatase of Streptomyces coelicolor expressed in Escherichia coli
    • +-pyrophosphatase of Streptomyces coelicolor expressed in Escherichia coli. J. Biochem. 138 (2005) 183-191
    • (2005) J. Biochem. , vol.138 , pp. 183-191
    • Hirono, M.1    Mimura, H.2    Nakanishi, Y.3    Maeshima, M.4
  • 38
    • 0037151064 scopus 로고    scopus 로고
    • +-pyrophosphatase of Rhodospirillum rubrum: high yield expression in Escherichia coli and identification of the Cys residues responsible for inactivation by mersalyl
    • +-pyrophosphatase of Rhodospirillum rubrum: high yield expression in Escherichia coli and identification of the Cys residues responsible for inactivation by mersalyl. J. Biol. Chem. 277 (2002) 22209-22214
    • (2002) J. Biol. Chem. , vol.277 , pp. 22209-22214
    • Belgurov, G.A.1    Turkina, M.V.2    Penttinen, A.3    Huopalahti, S.4    Baykov, A.A.5    Lahti, R.6
  • 42
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie J.U. Solving the membrane protein folding problem. Nature 438 (2005) 581-589
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 43
    • 13844310859 scopus 로고    scopus 로고
    • Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution
    • Liu K., Kozono D., Kato Y., Agre P., Hazama A., and Yasui M. Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 2192-2197
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2192-2197
    • Liu, K.1    Kozono, D.2    Kato, Y.3    Agre, P.4    Hazama, A.5    Yasui, M.6
  • 44
    • 0027520803 scopus 로고
    • The computed free energy change of hydrolysis of inorganic pyrophosphate and ATP: apparent significance for inorganic-pyrophosphate-driven reactions of intermediary metabolism
    • Davies J.M., Poole R.J., and Sanders D. The computed free energy change of hydrolysis of inorganic pyrophosphate and ATP: apparent significance for inorganic-pyrophosphate-driven reactions of intermediary metabolism. Biochim. Biophys. Acta 1141 (1993) 29-36
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 29-36
    • Davies, J.M.1    Poole, R.J.2    Sanders, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.