Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Erika V. Soriano"'
Publikováno v:
Chem. Commun.. 47:2273-2275
This communication describes the development of a thiamin sensor based on the bacterial thiamin binding protein. A triple mutant (C48S, C50S, S62C) of TbpA was labeled on C62 with N-[2-(L-maleimidyl)ethyl]-7-(diethylamino)coumarin-3-carboxamide (MDCC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42ffc4a086631a7149c242b2d2b7e1f5
https://doi.org/10.1039/c0cc04228e
https://doi.org/10.1039/c0cc04228e
Autor:
Pieter C. Dorrestein, Jennie M. Sanders, Yang Zhang, Ethan C. Settembre, Tadhg P. Begley, Keri L. Colabroy, Erika V. Soriano, Steven E. Ealick
Quinolinate synthase (QS) catalyzes the condensation of iminoaspartate and dihydroxyacetone phosphate to form quinolinate, the universal precursor for the de novo biosynthesis of nicotinamide adenine dinucleotide. QS has been difficult to characteriz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc66f7c543169400f7c34b962d74f379
https://europepmc.org/articles/PMC3760129/
https://europepmc.org/articles/PMC3760129/
Autor:
Jeremiah Hanes, Kanagalaghatta R. Rajashankar, Tadhg P. Begley, Erika V. Soriano, Steven E. Ealick, Shridhar Bale
Publikováno v:
Biochemistry. 47(5)
ATP-binding cassette (ABC) transporters are responsible for the transport of a wide variety of water-soluble molecules and ions into prokaryotic cells. In Gram-negative bacteria, periplasmic-binding proteins deliver ions or molecules such as thiamin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::979e089300c3a135828411f3725d628c
https://pubmed.ncbi.nlm.nih.gov/18177053
https://pubmed.ncbi.nlm.nih.gov/18177053
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 63(Pt 12)
Human deoxycytidine kinase (dCK) is involved in the nucleotide-biosynthesis salvage pathway and has also been shown to phosphorylate several antitumor and antiviral prodrugs. The structures of dCK alone and the dead-end complex of dCK with substrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b5d72de4e6b14fbe8d796deb9815a00
https://pubmed.ncbi.nlm.nih.gov/18084067
https://pubmed.ncbi.nlm.nih.gov/18084067
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
The crystal structures of two arginine decarboxylase mutant proteins provide insights into the mechanisms of pyruvoyl-group formation and the decarboxylation reaction.
Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step
Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc513def736a8d7329abd3afd290218a
https://pubmed.ncbi.nlm.nih.gov/18391404
https://pubmed.ncbi.nlm.nih.gov/18391404
Publikováno v:
Acta Crystallographica: Section D (Wiley-Blackwell). Dec2007, Vol. 63 Issue 12, p1201-1207. 7p. 1 Chart.