Intramolecular distances between tryptophan residues and the active-site serine residue in alkaline bacterial proteinases as measured by fluorescence energy-transfer studies.
Singlet-singlet energy transfer from the tryptophan residues to an active-site-serine-bound 5-dimethylaminonaphthalene-1-sulphonyl group was investigated in four subtilisins. The transfer distances for subtilisin Novo and mesentericopeptidase are 1.93 +/- 0.20 nm (19.3 +/- 2.0 A) and 1.81 +/- 0.20 nm (18.1 +/- 2.0 A) respectively. The positions of the indole groups in the three-dimensional structures of the two pairs of proteinases, namely subtilisin Novo and mesentericopeptidase on the one hand and subtilisins Carlsberg and DY on the other, are essentially identical.
D001665:Binding Sites; D003619:Dansyl Compounds / Q000494:pharmacology; D010450:Endopeptidases; D004735:Energy Transfer; D007700:Kinetics; D011480:Protease Inhibitors; D012694:Serine / Q000032:analysis; D012697:Serine Endopeptidases; D013050:Spectrometry, Fluorescence; D013381:Subtilisins / Q000037:antagonists & inhibitors; D014364:Tryptophan / Q000032:analysis
D003619:Dansyl Compounds; D011480:Protease Inhibitors; C016338:dansyl fluoride; D012694:Serine; D014364:Tryptophan; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013381:Subtilisins; C021553:mesentericopeptidase