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Kinetic studies of papain: Effect of P3′ substituents and donor/acceptor pairs of intramolecularly quenched fluorogenic substrates

✍ Scribed by Carlos García-Echeverría; Daniel H. Rich

Book ID
104633107
Publisher
Springer Netherlands
Year
1995
Tongue
English
Weight
417 KB
Volume
2
Category
Article
ISSN
1573-3149

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✦ Synopsis

Two series of intramolecularly quenched fluorogenic oligopeptide substrates with the general sequences DABCYL-Lys-Phe-GIy-GIy-AIa-Xxx-EDANS and Abz-Lys-Phe-Gly-Gly-Ala-Xxx-Tyr(m-NO2)-NH 2 have been used to explore the effect of P3' substituents and donor/acceptor pairs on the kinetic parameters for papain-catalyzed hydrolysis. The steady-state constants are moderately affected by amino acid or fluorophore/quencher replacement. No correlation between the hydrophobicity of the P3' substituent and the kinetic parameters was found.

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Internally quenched fluorogenic protease
Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containingortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs
✍ Izaura Yoshico Hirata; Maria Helena Sedenho Cezari; Clovis Ryuichi Nakaie; Paulo 📂 Article 📅 1995 🏛 Springer Netherlands 🌐 English ⚖ 660 KB

A general procedure, using the commonly employed solid-phase peptide synthesis methodology for obtaining internally quenched fluorogenic peptides with ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs, is presented. The essential feature of this procedure is the synthesis of an N~-Boc