Post-translational peptide bond formation during concanavalin A processing in vitro
- 15 December 1996
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 320 (3), 865-870
- https://doi.org/10.1042/bj3200865
Abstract
Post-translational processing of concanavalin A (Con A) is complex, involving deglycosylation, proteolytic cleavage on the carboxy group side of asparagine residues and formation of a peptide bond de novo. This has been studied with the 125I-labelled Con A glycoprotein precursor as a substrate for processing in vitro. Extracts of immature jackbean cotyledons and the commercially available purified preparation of asparaginylendopeptidase were able to catalyse the above processes. The processing resulted in the conversion of the 33.5 kDa inactive glycoprotein precursor into an active lectin. Processing activity was maximal at approx. pH 5.5. Evidence to support processing at authentic sites was obtained by observation of the release of 125I at positions in the sequence where tyrosine residues were present.Keywords
This publication has 35 references indexed in Scilit:
- In vitro splicing of concanavalin A is catalyzed by asparaginyl endopeptidaseNature Structural & Molecular Biology, 1994
- In vitro protein splicing of purified precursor and the identification of a branched intermediateCell, 1993
- Amino acid sequence and variant forms of favin, a lectin from Vicia faba.Journal of Biological Chemistry, 1982
- Almond glycopeptidase acting on aspartylglycosylamine linkages. Multiplicity and substrate specificityBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- The chemical characterization of favin, a lectin isolated from Vicia faba.Journal of Biological Chemistry, 1979
- The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3.Journal of Biological Chemistry, 1975
- The covalent and three-dimensional structural of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2.Journal of Biological Chemistry, 1975
- The binding properties of dimeric and tetrameric concanavalin A. Binding of ligands to noninteracting macromolecular acceptors.1973
- The molecular weight and stability of concanavalin ABiochimica et Biophysica Acta (BBA) - Protein Structure, 1972
- Protein-carbohydrate interactionBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967