Hexadeoxycycloheptaamylose-pyridoxamine, an artificial transaminase with a "deeper" binding pocket

Cycloheptaamylose was converted in four steps into a monosulfonylated, hexadeoxy derivative that, on treatment with pyridoxaminethiol, provided an artificial transaminase with activity similar to that found in the nondeoxygenated analogue. Characterization of the intermediate hexadeoxycycloheptaamylose was facilitated by the use of field-desorption mass spectrometry, which was uniquely able to distinguish between penta-, hexa-, and hepta-deoxycycloheptaamylose. A detailed description of experimental methods for the first time makes this modified binding-site available for general use in the design of enzyme mimics.