Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Svetlana M. Avaeva"'
Publikováno v:
Biochemistry (Moscow). 70:848-857
Sequence alignment of inorganic pyrophosphatases (PPases) isolated from the different organisms shows that glycine residues Gly100 and Gly147 are conservative. These residues are located in flexible segments of a polypeptide chain that have similar s
Autor:
T. I. Nazarova, N. N. Vorobyeva, Ju. S. Skoblov, E. V. Rodina, Svetlana M. Avaeva, Ju. P. Vainonen, S. A. Kurilova
Publikováno v:
Biochemistry (Moscow). 70:69-78
Soluble inorganic pyrophosphatase from Escherichia coli (E-PPase) is a hexamer forming under acidic conditions the active trimers. We have earlier found that the hydrolysis of a substrate (MgPPi) by the trimers as well as a mutant E-PPase Asp26Ala di
Publikováno v:
Russian Journal of Bioorganic Chemistry. 28:385-391
The conditions were found for obtaining trimeric, dimeric, and monomeric forms of the Escherichia coli inorganic pyrophosphatase from its native hexameric form. Interconversions of the oligomers were studied, and rate constants for their dissociation
Autor:
S. A. Kurilova, Konstantin M. Polyakov, V. R. Samygina, Alexander Popov, T. I. Nazarova, Victor S. Lamzin, Svetlana M. Avaeva, N. N. Vorobyeva, E. V. Rodina
Publikováno v:
Journal of Molecular Biology. 314:633-645
Two structures of Escherichia coli soluble inorganic pyrophosphatase (EPPase) complexed with calcium pyrophosphate (CaPPi-EPPase) and with Ca2+ (Ca2+-EPPase) have been solved at 1.2 and 1.1 A resolution, respectively. In the presence of Mg2+, this en
Autor:
S. A. Kurilova, Yuliya P. Vainonen, E. V. Rodina, Nataliya N. Vorobyeva, T. I. Nazarova, Svetlana M. Avaeva
Publikováno v:
European Journal of Biochemistry. 268:3851-3857
Excess of Mg2+ ions is known to inhibit the soluble inorganic pyrophosphatases (PPases). In contrast, the mutant Escherichia coli inorganic pyrophosphatase Asp42-->Asn is three times more active than native and retains its activity at high Mg2+ conce
Publikováno v:
Russian Journal of Bioorganic Chemistry. 27:27-33
The interaction of inorganic pyrophosphatase from E. coli with inorganic phosphate (Pi) was studied in a wide concentration range of phosphate. The apoenzyme gives two inactive compounds with Pi, a product of phosphorylation of the carboxylic group o
Autor:
T. I. Nazarova, E. V. Rodina, Yu. P. Vainonen, N. N. Vorobyeva, Svetlana M. Avaeva, S. A. Kurilova
Publikováno v:
Russian Chemical Bulletin. 50:1877-1884
The kinetics of hydrolysis of the inorganic (PPi) and organic (ATP) substrates by Escherichia coli inorganic pyrophosphatase (PPase) and its mutant forms with Asp42 replaced by Ala, Asn, or Glu was studied. The Mn2+ or Zn2+ ions were used as activato
Autor:
Zbygnew Dauter, V. A. Sklyankina, Robert Huber, Timothy Mather, S. A. Kurilova, Vaheh Yu. Oganessyan, N. N. Vorobyeva, Olga Grigorjeva, Svetlana M. Avaeva, Keith S. Wilson, T. I. Nazarova, E. V. Rodina, E.H. Harutyunyan
Publikováno v:
FEBS Letters. 410:502-508
The three-dimensional structure of inorganic pyrophosphatase from Escherichia coli complexed with sulfate was determined at 2.2 A resolution using Patterson's search technique and refmed to an R-factor of 19.2%. Sulfate may be regarded as a structura
Autor:
Svetlana M. Avaeva, Natalya N. Oganessyan, Vaheh Yu. Oganessyan, S. A. Kurilova, Tatyana I. Nazarova, Robert Huber, N. N. Vorobyeva, E.H. Harutyunyan, Timothy Mather
Publikováno v:
Biochemistry. 36:7754-7760
Crystalline holo inorganic pyrophosphatase from Escherichia coli was grown in the presence of 250 mM MgCl2. The crystal structure has been solved by Patterson search techniques and refined to an R-factor of 17.6% at 1.9 A resolution. The upper estima
Autor:
V.Yu. Oganessyan, E.H. Harutyunyan, Svetlana M. Avaeva, S. A. Kurilova, A.N. Popov, N. N. Vorobyeva, T. I. Nazarova, A.A. Lebedev
Publikováno v:
FEBS Letters. 348:301-304
An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described. The inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asy