TY - JOUR
T1 - PHOTOREGULATION OF α‐CHYMOTRYPSIN ACTIVITY IN ORGANIC MEDIA
T2 - EFFECTS OF BIOIMPRINTING
AU - Willner, Itamar
AU - Lion‐Dagan, Mazzi
AU - Rubin, Shai
AU - Wonner, Johann
AU - Effenberger, Franz
AU - Bäuerle, Peter
PY - 1994/4
Y1 - 1994/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0028409712&partnerID=8YFLogxK
U2 - 10.1111/j.1751-1097.1994.tb05070.x
DO - 10.1111/j.1751-1097.1994.tb05070.x
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C2 - 8022894
AN - SCOPUS:0028409712
SN - 0031-8655
VL - 59
SP - 491
EP - 496
JO - Photochemistry and Photobiology
JF - Photochemistry and Photobiology
IS - 4
ER -