Zobrazeno 1 - 10
of 112
pro vyhledávání: '"Reijo Lahti"'
Autor:
Viktor A. Anashkin, Anu Salminen, Ekaterina Osipova, Svetlana A. Kurilova, Ilia D. Deltsov, Reijo Lahti, Alexander A. Baykov
Publikováno v:
ACS Omega, Vol 4, Iss 13, Pp 15549-15559 (2019)
Externí odkaz:
https://doaj.org/article/56628028b2654ce5956e7c075fa84932
Autor:
Anssi M. Malinen, Viktor A. Anashkin, Victor N. Orlov, Alexander V. Bogachev, Reijo Lahti, Alexander A. Baykov
Publikováno v:
Protein Science. 31
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae1a621630790a0f993ed637a4712995
https://doi.org/10.1002/pro.4394
https://doi.org/10.1002/pro.4394
Autor:
Anssi M, Malinen, Viktor A, Anashkin, Victor N, Orlov, Alexander V, Bogachev, Reijo, Lahti, Alexander A, Baykov
Publikováno v:
Protein science : a publication of the Protein Society. 31(9)
Membrane-bound pyrophosphatase (mPPase) found in microbes and plants is a membrane H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::79d1352b9427d8dcfc26eb76bb1495d9
https://pubmed.ncbi.nlm.nih.gov/36040263
https://pubmed.ncbi.nlm.nih.gov/36040263
Publikováno v:
Biochemical and Biophysical Research Communications. 517:266-271
Bacterial family II pyrophosphatases (PPases) are homodimeric enzymes, with the active site located between two catalytic domains. Some family II PPases additionally contain regulatory cystathionine β-synthase (CBS) domains and exhibit positive kine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbd5d2714490e027eea8643d3f6ed74c
https://doi.org/10.1016/j.bbrc.2019.07.056
https://doi.org/10.1016/j.bbrc.2019.07.056
Autor:
Ekaterina A. Osipova, Viktor A. Anashkin, Anu Salminen, S. A. Kurilova, Ilia D Deltsov, Reijo Lahti, Alexander A. Baykov
Publikováno v:
ACS Omega, Vol 4, Iss 13, Pp 15549-15559 (2019)
ACS Omega
ACS Omega
Inorganic pyrophosphatase containing regulatory cystathionine β-synthase (CBS) domains (CBS-PPase) is inhibited by adenosine monophosphate (AMP) and adenosine diphosphate and activated by adenosine triphosphate (ATP) and diadenosine polyphosphates;
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d254973c7809384c9a5fd7af7560594
https://doaj.org/article/56628028b2654ce5956e7c075fa84932
https://doaj.org/article/56628028b2654ce5956e7c075fa84932
Publikováno v:
Archives of biochemistry and biophysics. 692
A quarter of prokaryotic Family II inorganic pyrophosphatases (PPases) contain a regulatory insert comprised of two cystathionine β-synthase (CBS) domains and one DRTGG domain in addition to the two catalytic domains that form canonical Family II PP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82d2b971529a2337f792ed45c82d9e0e
https://pubmed.ncbi.nlm.nih.gov/32810477
https://pubmed.ncbi.nlm.nih.gov/32810477
Publikováno v:
Biochemistry (Moscow). 82:1079-1087
Cystathionine β-synthase (CBS) domains discovered 20 years ago can bind different adenosine derivatives (AMP, ADP, ATP, S-adenosylmethionine, NAD, diadenosine polyphosphates) and thus regulate the activities of numerous proteins. Mutations in CBS do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9be945e99298f7dc9f86a03a97ee261
https://doi.org/10.1134/s0006297917100017
https://doi.org/10.1134/s0006297917100017
Publikováno v:
FEBS Letters. 591:3225-3234
Inorganic pyrophosphatases (PPases) convert pyrophosphate (PPi ) to phosphate and are present in all cell types. Soluble PPases belong to three nonhomologous families, of which Family II is found in approximately a quarter of prokaryotic organisms, o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddb4f54cfd44f4704917332d1129a721
https://doi.org/10.1002/1873-3468.12877
https://doi.org/10.1002/1873-3468.12877
Publikováno v:
Biochemical Journal. 473:2097-2107
Many prokaryotic soluble PPases (pyrophosphatases) contain a pair of regulatory adenine nucleotide-binding CBS (cystathionine β-synthase) domains that act as ‘internal inhibitors’ whose effect is modulated by nucleotide binding. Although such re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c395b12ef51d23a3ad8b2a255e95b874
https://doi.org/10.1042/bcj20160293
https://doi.org/10.1042/bcj20160293
Publikováno v:
The Biochemical journal. 475(6)
Membrane-bound pyrophosphatases (mPPases), which couple pyrophosphate hydrolysis to transmembrane transport of H + and/or Na + ions, are divided into K + ,Na + -independent, Na + -regulated, and K + -dependent families. The first two families include
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97e8f0095a3035a8e53af1d873fb0758
https://pubmed.ncbi.nlm.nih.gov/29519958
https://pubmed.ncbi.nlm.nih.gov/29519958