A series of stereochemically and structurally diverse fluorogenic and chromogenic substrates for hydrolytic enzymes has been synthesized and used to characterize enzyme activity profiles of esterases, lipases, proteases, pepti- dases, phosphatases, and epoxide hydro- lases. The substrates used are particu- larly resilient to nonspecific reactions due to their mechanism of activation.The activities recorded with the individ- ual substrates are therefore remarkably reproducible, and enable us to use the overall pattern of activity as a specific fingerprint for the enzyme sample. Fin- gerprints of activity, and enantio- and stereoselectivity are displayed as arrays of color-scale squares that are easily analyzed visually. Such fingerprints might be useful for quality control, enzyme discovery, and possibly for addressing the issue of functional conver- gence in enzymes.
Enzyme fingerprints of activity and stereo- and enantioselectivity from fluorogenic and chromogenic substrate arrays
CROTTI, PAOLO;
2002-01-01
Abstract
A series of stereochemically and structurally diverse fluorogenic and chromogenic substrates for hydrolytic enzymes has been synthesized and used to characterize enzyme activity profiles of esterases, lipases, proteases, pepti- dases, phosphatases, and epoxide hydro- lases. The substrates used are particu- larly resilient to nonspecific reactions due to their mechanism of activation.The activities recorded with the individ- ual substrates are therefore remarkably reproducible, and enable us to use the overall pattern of activity as a specific fingerprint for the enzyme sample. Fin- gerprints of activity, and enantio- and stereoselectivity are displayed as arrays of color-scale squares that are easily analyzed visually. Such fingerprints might be useful for quality control, enzyme discovery, and possibly for addressing the issue of functional conver- gence in enzymes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
