PMID: 8590630Oct 1, 1995Paper

The baculovirus cysteine protease has a cathepsin B-like S2-subsite specificity

Biological Chemistry Hoppe-Seyler
D Brömme, K Okamoto

Abstract

Autographa californica nuclear polyhedrosis virus (AcNPV) encodes a functional cysteine protease of the papain family which is expressed after infection in Spodoptera fruglperda Sf9 cells. The protease displays an inhibition profile typical for cysteine proteases and is highly active against synthetic peptide substrates. The pH optimum of the bell-shaped pH-activity curve is between 5.0 and 5.5. The best substrate tested is Z-Arg-Arg-MCA which is specific for cathepsin B. The specificity constant (Kcat/Km) of AcNPV protease for this substrate is approximately two times higher than for human cathepsin B. In contrast to human cathepsins, AcNPV protease does not exhibit a discriminating specificity towards neutral hydrophobic residues in the P2 position. These substrates are hydrolysed at a ten-fold lower rate than the P2 arginine containing substrate. The pH activity profile against the Z-Arg-Arg-MCA substrate reveals a pK of 5.35 which can be assigned to a glutamate residue in the S2 subsite pocket. Like in cathepsin B, this residue facilitates the binding of positively charged P2 residues in the primary binding pocket. In this respect, the AcNPV protease resembles cathepsin B more than cathepsins L and S.

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Citations

Aug 24, 1999·Biotechnology and Bioengineering·P E CruzM J Carrondo
Sep 22, 1999·Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research·M GowenI Kola
Dec 4, 2003·Bioscience, Biotechnology, and Biochemistry·Tatsuya KatoEnoch Y Park
Dec 1, 1995·Die Naturwissenschaften·P Bohley
Aug 5, 2015·Journal of Orthopaedic Research : Official Publication of the Orthopaedic Research Society·Eiji KozawaYoshihiro Nishida
Mar 23, 2004·The Journal of Immunology : Official Journal of the American Association of Immunologists·Stéphanie ZundelNicole M Thielens

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