Antibody-catalyzed rearrangement of the peptide bond.
The generation of antibodies from a bifunctional cyclic phosphinate transition-state analog provided agents capable of efficiently catalyzing both steps of the overall conversion of a substrate containing an asparaginyl-glycyl sequence through a succinimide intermediate to the products aspartyl-glycyl and the rearranged isoaspartyl-glycyl sequence. This reaction provides a potential means in addition to amide cleavage for the deactivation of protein or peptide biological functions in vivo.
Gibbs
R A
RA
Department of Chemistry, Pennsylvania State University, University Park 16802.
Taylor
S
S
Benkovic
S J
SJ
D017151:Antibodies, Catalytic / Q000378:metabolism*; D001216:Asparagine / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004151:Dipeptides / Q000378:metabolism; D005998:Glycine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013388:Succinimides / Q000378:metabolism
D017151:Antibodies, Catalytic; D004151:Dipeptides; D010455:Peptides; D013388:Succinimides; C032620:succinimide; C077758:N-acetylasparaginylglycyl-(N-phenethyl)amide; D001224:Aspartic Acid; D001216:Asparagine; D005998:Glycine