Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites.
The binding affinity of aspartate decarboxylase has been probed using MALDI-TOF spectrometry; adducts formed covalently in the active site were detected by MALDI-TOF mass spectrometry after incubation of the enzyme with a range of potential ligands in the presence of NaCNBH3; this has highighted key structural features which will aid design of potential inhibitors.
University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge, UK CB2 1EW.
Michael E
ME
Webb
Elaine
E
Stephens
Alison G
AG
Smith
Chris
C
Abell
D001665:Binding Sites; D001667:Binding, Competitive; D001894:Borohydrides / Q000737:chemistry / Q000378:metabolism; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013379:Substrate Specificity
D001894:Borohydrides; D008024:Ligands; C009282:sodium cyanoborohydride; D002262:Carboxy-Lyases; C019747:aspartate 4-decarboxylase