157-03-9Relevant articles and documents
Inhibition of Escherichia coli glucosamine synthetase by novel electrophilic analogues of glutamine - Comparison with 6-diazo-5-oxo-norleucine
Walker, Brian,Brown, Martin F.,Lynas, John F.,Martin,McDowell, Andrew,Badet, Bernard,Hill, Alan J.
, p. 2795 - 2798 (2000)
A series of electrophilic glutamine analogues based on 6-diazo-5-oxo-norleucine has been prepared, using novel synthetic routes, and evaluated as inhibitors of Escherichia coli. glucosamine synthetase. The γ-dimethylsulphonium salt analogue of glutamine was found to be one of the most potent inactivators of this enzyme yet reported, with an apparent second order rate constant (k2/K(i)) of 3.5 x 105 M-1 min-1. (C) 2000 Elsevier Science Ltd.
The Reaction of Lithium Trimethylsilyldiazomethane with Pyroglutamates - a Facile Synthesis of 6-Diazo-5-oxo-norleucine and Derivatives
Coutts, Ian G. C.,Saint, Robert E.
, p. 3242 - 3246 (2007/10/03)
The reaction of carbamate derivatives of pyroglutamic acid esters with the lithium salt of trimethylsilyldiazomethane below -100 deg C gives good yields of the corresponding substituted 6-diazo-5-oxo-norleucine esters; cleavage of Fmoc-substituted products provides a safe, convenient route to the parent acid.