Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Igor P. Fabrichniy"'
Autor:
Mikhail N. Tereshin, Tatiana D. Melikhova, Barbara Z. Eletskaya, Elena A. Ivanova, Lyudmila V. Onoprienko, Dmitry A. Makarov, Mikhail V. Razumikhin, Igor V. Myagkikh, Igor P. Fabrichniy, Vasiliy N. Stepanenko
Publikováno v:
Biomolecules, Vol 14, Iss 7, p 849 (2024)
Affinity chromatography is a widely used technique for antibody isolation. This article presents the successful synthesis of a novel affinity resin with a mutant form of protein A (BsrtA) immobilized on it as a ligand. The key aspect of the described
Externí odkaz:
https://doaj.org/article/6100060a32694edbbe8aefe96292da14
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 61:350-354
A recombinant form of an acetyl coenzyme A synthetase (ADP-forming) from Pyrococcus furiosus has been crystallized. Crystallization was accomplished by the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, wit
Autor:
Marko Tammenkoski, Igor P. Fabrichniy, Galina Ya. Kolomiytseva, Alexander A. Baykov, Anton B. Zyryanov, Anu Salminen, Reijo Lahti, Adrian Goldman
Publikováno v:
Biochemistry. 43:14395-14402
Family II pyrophosphatases (PPases), recently found in bacteria and archaebacteria, are Mn(2+)-containing metalloenzymes with two metal-binding subsites (M1 and M2) in the active site. These PPases can use a number of other divalent metal ions as the
Autor:
Michael C. Merckel, Anu Salminen, Reijo Lahti, Nisse Kalkkinen, Adrian Goldman, Igor P. Fabrichniy, Alexander A. Baykov
Publikováno v:
Structure. 9(4):289-297
Background: Streptococcus mutans pyrophosphatase (Sm-PPase) is a member of a relatively uncommon but widely dispersed sequence family (family II) of inorganic pyrophosphatases. A structure will answer two main questions: is it structurally similar to
Autor:
Vladimir N. Kasho, Pekka Pohjanjoki, A. Goldman, Barry S. Cooperman, Alexander A. Baykov, Reijo Lahti, Igor P. Fabrichniy
Publikováno v:
Journal of Biological Chemistry. 276:434-441
The pattern of yeast pyrophosphatase (Y-PPase) inhibition by fluoride suggests that it replaces active site Mg(2+)-bound nucleophilic water, for which two different locations were proposed previously. To localize the bound fluoride, we investigate he
Autor:
Pekka Pohjanjoki, Reijo Lahti, Alexander A. Baykov, and Anton B. Zyryanov, Igor P. Fabrichniy
Publikováno v:
Biochemistry. 39:11939-11947
The fluoride ion is a potent and specific inhibitor of cytoplasmic pyrophosphatase (PPase). Fluoride action on yeast PPase during PP(i) hydrolysis involves rapid and slow phases, the latter being only slowly reversible [Smirnova, I. N., and Baykov, A
Autor:
Barry S. Cooperman, Alexander A. Baykov, Pirkko Heikinheimo, Reijo Lahti, Igor P. Fabrichniy, Teppo Hyytiä, Victor Ya. Chernyak, Tiina A. Salminen, A. Goldman, Vladimir N. Kasho, Pasi Halonen, Valeriy Yu. Dudarenkov
Publikováno v:
Biochemistry. 36:7746-7753
Tyrosine 55 and lysine 104 are evolutionarily conserved residues that form a hydrogen bond in the active site of Escherichia coli inorganic pyrophosphatase (E-PPase). Here we used site-directed mutagenesis to examine their roles in structure stabiliz
Autor:
Reijo Lahti, Marko Tammenkoski, Lari Lehtiö, Igor P. Fabrichniy, Esko Oksanen, Alexander A. Baykov, Adrian Goldman, Anton B. Zyryanov
Publikováno v:
The Journal of biological chemistry. 282(2)
We report the first crystal structures of a family II pyrophosphatase complexed with a substrate analogue, imidodiphosphate (PNP). These provide new insights into the catalytic reaction mechanism of this enzyme family. We were able to capture the sub
The highly conserved picornavirus 2C proteins, thought to be involved in genome replication, contain three motifs found in NTPases/helicases of superfamily III. We report that human parechovirus 1 2C displays Mg 2+ -dependent ATP diphosphohydrolase a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea8a3a29f146916b2c8c5d59be156b30
https://europepmc.org/articles/PMC1346857/
https://europepmc.org/articles/PMC1346857/
Autor:
Igor P. Fabrichniy, Lari Lehtiö, Anu Salminen, Anton B. Zyryanov, Alexander A. Baykov, Reijo Lahti, Adrian Goldman
Publikováno v:
Biochemistry. 43(45)
Family II inorganic pyrophosphatases (PPases) constitute a new evolutionary group of PPases, with a different fold and mechanism than the common family I enzyme; they are related to the "DHH" family of phosphoesterases. Biochemical studies have shown