Bernard Badet
Centre national de la recherche scientifique
27 Papers
324 Citations
Bernard Badet is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Glutamine & Glutamine amidotransferase. The author has an hindex of 15, co-authored 27 publications.
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Papers
Glucosamine-6-phosphate synthase from Escherichia coli yields two proteins upon limited proteolysis: identification of the glutamine amidohydrolase and 2R ketose/aldose isomerase-bearing domains based on their biochemical properties.
TL;DR: Data suggest the existence of a hinge structure essential for the catalytically efficient coupling between the ammonia generating domain and the sugar binding domain and support the model recently proposed by Mei and Zalkin in which purF-type amidotransferases contain a glutamine hydrolase domain of approximately 200 amino acids fused to an ammonia-transfer domain.
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Glucosamine-6-phosphate synthase from Escherichia coli: determination of the mechanism of inactivation by N3-fumaroyl-L-2,3-diaminopropionic derivatives.
TL;DR: A mechanistic investigation of the inactivation of Escherichia coli glucosamine-6-phosphate synthase by N3-(4-methoxyfumaroyl)-L-2,3-diaminopropionate (FMDP) was undertaken, and a pathway that is in perfect agreement with the biochemical results was proposed.
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Possible involvement of Lys603 from Escherichia coli glucosamine-6-phosphate synthase in the binding of its substrate fructose 6-phosphate
TL;DR: Among the lysines which belong to the sugar-binding domain this is the only one conserved between the three members of the purF, glutamine-dependent, amidotransferase subfamily which include the glucosamine-6-phosphate synthase from Escherichia coli, Saccharomyces cerevisiae and the Rhizobium nodulation protein NodM.
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Gamma-fluorinated analogues of glutamic acid and glutamine.
TL;DR: In this article, the synthesis of 4-fluoroglutamic analogues of glutamic acid and glutamine is extensively reviewed in the context of biological interest, and a number of synthesis methods are presented.
Ammonia channeling in bacterial glucosamine-6-phosphate synthase (Glms): Molecular dynamics simulations and kinetic studies of protein mutants.
Nicolas Floquet,Stephane Mouilleron,Rasha Daher,Bernard Maigret,Bernard Badet,Marie-Ange Badet-Denisot +5 more
TL;DR: A key role is suggested for Trp74, in the sealing of the hydrophobic channel connecting the two binding sites, as well as for the two Ala602 and Val605 residues, which form a narrow passage whose opening/closing constitutes an essential event in ammonia transfer.
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