Proteinase inhibitors from desert locust, Schistocerca gregaria: engineering of both P1 and P1′ residues converts a potent chymotrypsin inhibitor to a potent trypsin inhibitor
- 1 September 1999
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1434 (1) , 143-150
- https://doi.org/10.1016/s0167-4838(99)00167-3
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Engineering the S1‘ Subsite of Trypsin: Design of a Protease Which Cleaves between Dibasic ResiduesBiochemistry, 1998
- Purification of a Novel, Heat-Stable Serine Protease Inhibitor Protein from Ovaries of the Desert Locust,Schistocerca gregariaBiochemical and Biophysical Research Communications, 1997
- Solution Structure of PMP-C: A New Fold in the Group of Small Serine Proteinase InhibitorsJournal of Molecular Biology, 1996
- Serine Protease Inhibition by Insect Peptides Containing a Cysteine Knot and a Triple-stranded β-SheetJournal of Biological Chemistry, 1995
- Solution Structure of PMP-D2, a 35-Residue Peptide Isolated from the Insect Locusta migratoriaBiochemistry, 1994
- Mapping the S' subsites of serine proteases using acyl transfer to mixtures of peptide nucleophilesBiochemistry, 1993
- Insect immunity: Two proteinase inhibitors from hemolymph of Locusta migratoriaBiochemical and Biophysical Research Communications, 1992
- Isolation and structural determination of three peptides from the insect Locusta migratoriaEuropean Journal of Biochemistry, 1992
- Enzymic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitorBiochemistry, 1969