Zobrazeno 1 - 10
of 12
pro vyhledávání: '"V. A. Sklyankina"'
Publikováno v:
Molecular Biology. 39:625-630
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5311f8acf704b31376fb101c4fdb08ed
https://doi.org/10.1007/s11008-005-0078-9
https://doi.org/10.1007/s11008-005-0078-9
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccb72fc8353341a54450346e12cecbca
https://doi.org/10.1016/s0014-5793(97)00650-9
https://doi.org/10.1016/s0014-5793(97)00650-9
Autor:
Sergei D. Varfolomeyev, Olga Grigorjeva, Svetlana M. Avaeva, Vladimir Mitkevich, V. A. Sklyankina
Publikováno v:
FEBS letters. 464(3)
Escherichia coli inorganic pyrophosphatase (PPase) is a hexamer of identical subunits. This work shows that trimeric form of PPase exhibits the interaction of the active sites in catalysis. Some trimer subunits demonstrate high substrate binding affi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a7da49ed0c35e03a77e615c834eaa68
https://pubmed.ncbi.nlm.nih.gov/10618499
https://pubmed.ncbi.nlm.nih.gov/10618499
Publikováno v:
Biochemistry. Biokhimiia. 64(2)
Magnesium-supported PPi hydrolysis by the mutant Asp-67Asn E. coli pyrophosphatase at saturating PPi and metal-activator concentrations in the presence of NaF is followed by a gradual decrease in the initial rate of PPi hydrolysis. The reaction occur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b4fe7737ea5a05e49546085311ccb971
https://pubmed.ncbi.nlm.nih.gov/10187907
https://pubmed.ncbi.nlm.nih.gov/10187907
Autor:
S M, Avaeva, E V, Rodina, N N, Vorobyeva, S A, Kurilova, T I, Nazarova, V A, Sklyankina, V Y, Oganessyan, V R, Samygina, E H, Harutyunyan
Publikováno v:
Biochemistry. Biokhimiia. 63(6)
The three-dimensional structures of four mutant E. coli inorganic pyrophosphatases (PPases) with single Asp--Asn substitutions at positions 42, 65, 70, and 97 were solved at 1.95, 2.15, 2.10, and 2.20 A resolution, respectively. Asp-42--Asn and Asp-6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::de80f67f6cbe295f8bccb4a66e178594
https://pubmed.ncbi.nlm.nih.gov/9668207
https://pubmed.ncbi.nlm.nih.gov/9668207
Autor:
S M, Avaeva, E V, Rodina, N N, Vorobyeva, S A, Kurilova, T I, Nazarova, V A, Sklyankina, V Y, Oganessyan, E H, Harutyunyan
Publikováno v:
Biochemistry. Biokhimiia. 63(5)
The three-dimensional structures of E. coli inorganic pyrophosphatase (PPase) and its complexes with Mn2+ in a high affinity site and with Mg2+ in high and low affinity sites determined by authors in 1994-1996 at 1.9-2.2 A resolution are compared. Me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5a190cea49622c979be5b5afba64e680
https://pubmed.ncbi.nlm.nih.gov/9632898
https://pubmed.ncbi.nlm.nih.gov/9632898
Autor:
V. A. Sklyankina, Svetlana M. Avaeva
Publikováno v:
European journal of biochemistry. 191(1)
The hexameric inorganic pyrophosphatase (PPase) is irreversibly inactivated by phosphoric acid monoesters. The inactivation kinetics are consistent with the formation of a dissociable complex of the phosphoric acid monoester with the enzyme, followed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a417baf14ecc2bdeee38f4028538e4e9
https://pubmed.ncbi.nlm.nih.gov/2165905
https://pubmed.ncbi.nlm.nih.gov/2165905
Autor:
A. V. Kuznetsov, N.P. Bakuleva, V. A. Sklyankina, T. I. Nazarova, A. A. Komissarov, Svetlana M. Avaeva
Publikováno v:
Chemistry of Natural Compounds. 18:350-355
By the peptide map method, a phosphorylated peptide has been isolated from a tryptic hydrolysate of phosphorylated yeast inorganic pyrophosphatase (I), and this is a direct proof of the formation of a covalent bond between (I) and phosphate in the co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::070bde8f2521735b47705f31c63316bf
https://doi.org/10.1007/bf00580466
https://doi.org/10.1007/bf00580466
Publikováno v:
Journal of Molecular Catalysis. 47:307-314
Inorganic pyrophosphatases of baker's yeast and E. coli are oligomers built of chemically identical subunits. Both enzymes are active in the monomeric state. Each subunit has an active and an allosteric site linked by hetero- and homotropic interacti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1fe003ec4ded54b38d179526774523e8
https://doi.org/10.1016/0304-5102(88)85055-7
https://doi.org/10.1016/0304-5102(88)85055-7
Publikováno v:
FEBS Letters. (2):269-272
Baker’s yeast pyrophosphatase (EC 3.6.1.1) displays half-of-the-sites reactivity with respect to the inhibitors, phosphoric acid monoesters [ 1,2]. The enzyme catalyzes the hydrolysis and synthesis of inorganic pyrophosphate. It is a dimeric protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77872ab1161d9bb8a0865d941f11618b