PHOTOREGULATION OF α‐CHYMOTRYPSIN ACTIVITY IN ORGANIC MEDIA: EFFECTS OF BIOIMPRINTING

Itamar Willner*, Mazzi Lion‐Dagan, Shai Rubin, Johann Wonner, Franz Effenberger, Peter Bäuerle

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Abstract α‐Chymotrypsin exhibits photoswitchable activities in an organic solvent after covalent modification of the protein backbone with thiophenefulgide active ester (2). The thiophenefulgide‐modified α‐chymotrypsin exhibits reversible photoisomerizable properties between states (3)‐E and (3)‐C. The modified α‐chymotrypsin, where nine lysine residues are substituted by thiophenefulgide units, retains 60% of the activity of the native enzyme. The activities of thiophenefulgide‐modified α‐chymotrypsin toward esterification of N‐acetyl‐L‐phenylalanine (4) by ethanol in cyclohexane are controlled by the configuration of the attached photoisomerizable component and by prior bioimprinting of the protein backbone with the reaction substrate (4). The esterification of (4) in cyclohexane using bioimprinted (3)‐C is two‐fold faster than in the presence of (3)‐E. In the presence of a nonbioimprinted enzyme, esterification of (4) by (3)‐C is five‐fold faster than with (3)‐E. The activity of bioimprinted (3)‐E toward esterification of (4) is 4.5‐fold higher than that of nonbioimprinted (3)‐E. Switchable cyclic esterification of (4) is accomplished by sequential photoisomerization of the thiophenefulgide‐modified α‐chymotrypsin between states (3)‐C and (3)‐E.

Original languageEnglish
Pages (from-to)491-496
Number of pages6
JournalPhotochemistry and Photobiology
Volume59
Issue number4
DOIs
StatePublished - Apr 1994

Fingerprint

Dive into the research topics of 'PHOTOREGULATION OF α‐CHYMOTRYPSIN ACTIVITY IN ORGANIC MEDIA: EFFECTS OF BIOIMPRINTING'. Together they form a unique fingerprint.

Cite this