Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Pekka Pohjanjoki"'
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c1f03ffaf0e7235bfb99c157c088d84
https://doi.org/10.1074/jbc.m007360200
https://doi.org/10.1074/jbc.m007360200
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36316886e76a755a6bf24f7fe7fbc1e2
https://doi.org/10.1021/bi000627u
https://doi.org/10.1021/bi000627u
Autor:
Anu Salminen, Reijo Lahti, Pekka Pohjanjoki, Alexey N. Parfenyev, Barry S. Cooperman, Alexander A. Baykov, Adrian Goldman, Toni Sivula
Publikováno v:
FEBS Letters. 454:75-80
Based on the primary structure, soluble inorganic pyrophosphatases can be divided into two families which exhibit no sequence similarity to each other. Family I, comprising most of the known pyrophosphatase sequences, can be further divided into prok
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1c906b7e69384eb78c01e76b246601a
https://doi.org/10.1016/s0014-5793(99)00779-6
https://doi.org/10.1016/s0014-5793(99)00779-6
Publikováno v:
Biochemistry. 37:1754-1761
Soluble inorganic pyrophosphatase (PPase) is one of the better understood phosphoryl-transfer enzymes and is distinctive in having four divalent metal ions at the active site. Here we determine pH profiles for wild-type Saccharomyces cerevisiae PPase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8268af82e95bf1e2e054312dfce59120
https://doi.org/10.1021/bi971771r
https://doi.org/10.1021/bi971771r
Autor:
Anton B. Zyryanov, Alexander A. Baykov, Alexander S. Shestakov, Vladimir N. Kasho, Adrian Goldman, Reijo Lahti, Pekka Pohjanjoki
Publikováno v:
The Journal of biological chemistry. 276(21)
Binding of pyrophosphate or two phosphate molecules to the pyrophosphatase (PPase) active site occurs at two subsites, P1 and P2. Mutations at P2 subsite residues (Y93F and K56R) caused a much greater decrease in phosphate binding affinity of yeast P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc5aab7e38cb292c8912e596e4b4c305
https://pubmed.ncbi.nlm.nih.gov/11279052
https://pubmed.ncbi.nlm.nih.gov/11279052
Autor:
Erkka Lehtihuhta, Igor P. Fabrichniy, Pekka Pohjanjoki, A. Goldman, Maria V. Turkina, Vladimir N. Kasho, Barry S. Cooperman, Reijo Lahti, Georgiy A. Belogurov, Alexander A. Baykov
Publikováno v:
Biochemistry. 39(45)
Five catalytic functions of yeast inorganic pyrophosphatase were measured over wide pH ranges: steady-state PP(i) hydrolysis (pH 4. 8-10) and synthesis (6.3-9.3), phosphate-water oxygen exchange (pH 4. 8-9.3), equilibrium formation of enzyme-bound PP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b650f29087fab8115c5d3d5f1ddfba4b
https://pubmed.ncbi.nlm.nih.gov/11076535
https://pubmed.ncbi.nlm.nih.gov/11076535
Autor:
A. Goldman, Reijo Lahti, Barry S. Cooperman, Irina S. Efimova, Anu Salminen, Alexander A. Baykov, Pekka Pohjanjoki, Natalia N. Magretova, Jukka Lapinniemi
Publikováno v:
The Journal of biological chemistry. 274(6)
Recent crystallographic studies on Escherichia coli inorganic pyrophosphatase (E-PPase) have identified three Mg2+ ions/enzyme hexamer in water-filled cavities formed by Asn24, Ala25, and Asp26 at the trimer-trimer interface (Kankare, J., Salminen, T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4977c9ee29077481ed8ae8375a5c5349
https://pubmed.ncbi.nlm.nih.gov/9920869
https://pubmed.ncbi.nlm.nih.gov/9920869
Autor:
Alexander A. Baykov, Adrian Goldman, Pirkko Heikinheimo, Pekka Pohjanjoki, Reijo Lahti, Anne Helminen, Merja J. Tasanen, Barry S. Cooperman
Publikováno v:
European journal of biochemistry. 239(1)
We report the expression and initial characterization of 19 active-site variants of Saccharomyces cerevisiae inorganic pyrophosphatase (PPase), including measurements of thermostability, oligomeric structure and specific activity at pH 7.2. 13 of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16cb836f46802d459ad1fb32f6edc8c9
https://pubmed.ncbi.nlm.nih.gov/8706698
https://pubmed.ncbi.nlm.nih.gov/8706698