Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Santosh Shivakumaraswamy"'
Autor:
Lionel Ballut, Sébastien Violot, Frédéric Galisson, Isabelle R. Gonçalves, Juliette Martin, Santosh Shivakumaraswamy, Loïc Carrique, Hemalatha Balaram, Nushin Aghajari
Publikováno v:
Biomolecules, Vol 12, Iss 7, p 871 (2022)
Glutamine amidotransferases, enzymes that transfer nitrogen from Gln to various cellular metabolites, are modular, with the amidotransferase (GATase) domain hydrolyzing Gln, generating ammonia and the acceptor domain catalyzing the addition of nitrog
Externí odkaz:
https://doaj.org/article/e14715547f034e78a813fc741f41d19d
Autor:
Lionel Ballut, Sébastien Violot, Frédéric Galisson, Isabelle R. Gonçalves, Juliette Martin, Santosh Shivakumaraswamy, Loïc Carrique, Hemalatha Balaram, Nushin Aghajari
Publikováno v:
Biomolecules; Volume 12; Issue 7; Pages: 871
Glutamine amidotransferases, enzymes that transfer nitrogen from Gln to various cellular metabolites, are modular, with the amidotransferase (GATase) domain hydrolyzing Gln, generating ammonia and the acceptor domain catalyzing the addition of nitrog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec83a66b85f496d3fd3d1b5cf730119
https://doi.org/10.3390/biom12070871
https://doi.org/10.3390/biom12070871
Autor:
Thomas E. Wales, Aleksandra Pajak, Alžběta Roeselová, Santosh Shivakumaraswamy, Steven Howell, F. Ulrich Hartl, John R. Engen, David Balchin
The cellular environment is critical for efficient protein maturation, but how proteins fold during biogenesis remains poorly understood. We used hydrogen/deuterium exchange (HDX) mass spectrometry (MS) to define, at peptide resolution, the cotransla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33c19d7da51045713204ed5d76c4b002
https://doi.org/10.1101/2022.09.23.509153
https://doi.org/10.1101/2022.09.23.509153
Autor:
Santosh Shivakumaraswamy, Sanjeev Kumar, Asutosh Bellur, Satya Dev Polisetty, Hemalatha Balaram
Publikováno v:
Biochemistry. 61(18)
Guanosine 5'-monophosphate (GMP) synthetases, enzymes that catalyze the conversion of xanthosine 5'-monophosphate (XMP) to GMP, are composed of two different catalytic units, which are either two domains of a polypeptide chain or two subunits that as
Autor:
Nivedita Pandey, Sébastien Violot, Nushin Aghajari, Hemalatha Balaram, Lionel Ballut, Santosh Shivakumaraswamy
Publikováno v:
ChemBioChem
ChemBioChem, Wiley-VCH Verlag, 2020, 21 (19), pp.2805-2817. ⟨10.1002/cbic.202000158⟩
ChemBioChem, Wiley-VCH Verlag, 2020, 21 (19), pp.2805-2817. ⟨10.1002/cbic.202000158⟩
GMP synthetase catalyzes the substitution of the C2 oxo-group of the purine base in XMP with an amino-group generating GMP, the last step in the biosynthesis of GMP. This reaction involves a series of catalytic events that include hydrolysis of Gln g
Autor:
Santosh Shivakumaraswamy, Sanjeev Kumar, Asutosh Bellur, Satya Dev Polisetty, Hemalatha Balaram
Guanosine 5’-monophosphate (GMP) synthetases, enzymes that catalyze the conversion of xanthosine 5’-monophosphate (XMP) to GMP are comprised of two different catalytic units, which are either two domains of a polypeptide chain or two subunits tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc5934313b7e3a441897cec2c0532e4d
https://doi.org/10.1101/2022.02.27.481963
https://doi.org/10.1101/2022.02.27.481963
Publikováno v:
Protein engineering, designselection : PEDS. 30(8)
The carbohydrate esterase family 7 (CE7) enzymes catalyze the deacetylation of acetyl esters of a broad range of alcohols and is unique in its activity towards cephalosporin C. The CE7 fold contains a conserved N-terminal extension that distinguishes
Autor:
Sébastien Violot, Hemalatha Balaram, Santosh Shivakumaraswamy, Raphaël Terreux, Bauke W. Dijkstra, Lakshmi Prasoona Thota, Nushin Aghajari, R. Haser, Lionel Ballut
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 73:C248-C248