Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Tatiana I. Nazarova"'
Autor:
Anna V. Vlasova, S. A. Kurilova, Natalia N. Vorobyeva, Alexander A. Baykov, E. V. Rodina, Tatiana I. Nazarova, Viktor A. Anashkin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1865:129762
Background Previous studies have demonstrated the formation of stable complexes between inorganic pyrophosphatase (PPase) and three other Escherichia coli enzymes – cupin-type phosphoglucose isomerase (cPGI), class I fructose-1,6-bisphosphate aldol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1066cc7ef5bb302fa34dc07803d9cabe
https://doi.org/10.1016/j.bbagen.2020.129762
https://doi.org/10.1016/j.bbagen.2020.129762
Autor:
S. A. Kurilova, Galina Ya. Kolomijtseva, Natalia N. Vorobjeva, E. V. Rodina, Anastasia F. Petukhova, Alexander A. Baykov, Tatiana I. Nazarova
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1864:129601
Background Escherichia coli cells contain a homolog of presumed 5-keto-4-deoxyuronate isomerase (KduI) from pectin-degrading soil bacteria, but the catalytic activity of the E. coli protein (o-KduI) was never demonstrated. Methods The known three-dim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef8d9e74f0f388463cbe97a0ae3a45b2
https://doi.org/10.1016/j.bbagen.2020.129601
https://doi.org/10.1016/j.bbagen.2020.129601
Publikováno v:
FEBS Letters. 333:280-282
A segment of DNA encoding Saccharomyces cerevisiae inorganic pyrophosphatase (ppa gene) was amplified by the polymerase chain reaction. The pSCH1 and pSCB6 plasmids containing the ppa gene were obtained. Transformation of the E. coli BL21 strain with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30b69ffd76dcd89af993b68f1ea00806
https://doi.org/10.1016/0014-5793(93)80670-p
https://doi.org/10.1016/0014-5793(93)80670-p
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
Publikováno v:
FEBS Letters. 183:387-389
A baker's yeast inorganic pyrophosphatase derivative has been obtained in which one carboxyl group of each regulatory centre is converted to hydroxamate. This enzyme retains the capacity to hydrolyze the substrate while remaining a dimer. However, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acaf657bb999081405115bb52cff021c
https://doi.org/10.1016/0014-5793(85)80816-4
https://doi.org/10.1016/0014-5793(85)80816-4
Publikováno v:
FEBS Letters. (2):245-247
1. Introduction Baker’s yeast inorganic pyrophosphatase (EC 3.6.1 .I) is able to bind orthophosphate with a dissoci- ation constant of the order of 1 mM [l-3]. Despite the moderate strength of the binding, it results in formation of a chemical bond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39128dffb1210cfc8696e97c3f62ea6b