Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody
The crystal structures of catalytic antibody D2.3 Fab with the two enantiomers, 7D and 7L, which represent transition state analogues for the hydrolysis of the corresponding esters, 6D and 6L, were determined to better understand remarkable reactivity dif
D'Souza, Lawrence J.,Gigant, Benoit,Knossow, Marcel,Green, Bernard S.
p. 2114 - 2115
(2007/10/03)
Mapping of the active site of rat kidney γ-glutamyl transpeptidase using activated esters and their amide derivatives
The enzyme γ-glutamyl transpeptidase (GGT), implicated in many physiological processes, catalyses the transfer of a γ-glutamyl from a donor substrate to an acyl acceptor substrate, usually an amino acid or a peptide. In order to investigate which moieties of the donor substrate are necessary for recognition by GGT, the structure of the well-recognized substrate L-γ-glutamyl-p-nitroanilide was modified. Several activated esters and their amide derivatives were synthesized and used as substrates. Kinetic (Km and Vmax) and inhibition constants (Ki) were measured and reveal that almost the entire γ-glutamyl moiety is necessary for recognition in the binding site of the donor substrate. The implied presence of certain complementary amino acids in this substrate binding site will allow the more rational design of various substrate analogues and inhibitors.
Castonguay, Roselyne,Lherbet, Christian,Keillor, Jeffrey W.
p. 4185 - 4191
(2007/10/03)
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