Discovery of the ammonium substrate site on glutamine synthetase, A third cation binding site
نویسندگان
چکیده
منابع مشابه
Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase.
Mixed-function oxidation of glutamine synthetase from Escherichia coli causes loss of catalytic activity. The inactivation correlates with the loss of 1 of 16 histidine residues/subunit (Levine, R.L. (1983) J. Biol. Chem. 258, 11823-11827). A cyanogen bromide peptide containing the oxidizable histidine has been isolated. Within the protein, the sequence is Met-His-Cys-His-Met. This hydrophilic ...
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A combination of a literature survey, structure-based virtual screening and synthesis of a small library was performed to identify hits to the potential antimycobacterial drug target, glutamine synthetase. The best inhibitor identified from the literature survey was (2S,5R)-2,6-diamino-5-hydroxyhexanoic acid (4, IC(50) of 610+/-15microM). In the virtual screening 46,400 compounds were docked an...
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Carbamyl phosphate synthetase from Escherichia coli, which is composed of a light and a heavy subunit, is inhibited with respect to its glutamine-dependent reactions by treatment with ~-2-amino-4-oxo-5-chloro[5-‘~C]pentanoic acid. This glutamine analog reacts with a glutamineor albizziinprotectable site on the light subunit to yield an enzyme covalently linked to a 4-oxo[W]norvaline moiety. The...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1995
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560041114