Legumain Forms from Plants and Animals Differ in Their Specificity
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Vitalie I. Rotari
Abstract
We purified forms of legumain from a plant source (seeds of kidney bean, Phaseolus vulgaris) and a mammal (kidney of pig, Sus scropha) for comparison of their properties. Both forms were found to be stable only under moderately acidic pH conditions, and were maximally active at about pH 6; the plant enzyme was somewhat less stable and had a slightly higher pH optimum. With benzyloxycarbonylXaa AlaAsnaminomethylcoumarylamide substrates, the two forms of legumain showed distinctly different specificities for the P3 residue, the plant legumain preferring amino acids with bulky hydrophobic side chains because of lower K values. Both forms of legumain were highly specific for hydrolysis of asparaginyl bonds in the arylamide substrates and in neurotensin. Aspartyl bonds were hydrolysed about 100-fold more slowly with lower pH optima. Potential substrates containing other amino acids structurally similar to asparagine were not hydrolysed. There were clear differences in specificity of hydrolysis of protein substrates. The plant legumain differed from pig legumain in its action on tetanus toxoid Cfragment, cleaving at Asn[97] but not at Asn[337], and produced more extensive digestion of phaseolin. The plant form of legumain was much more weakly inhibited by eggwhite cystatin than was the mammalian form.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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Artikel in diesem Heft
- Biological Activity of Mammalian Transcriptional Repressors
- Cloning and Characterisation of Chlorophyll Synthase from Avena sativa
- DNA Damage by 3,6-Dihydropyrazine-2,5-Dipropanoic Acid, the Cyclic Dimerization Product of 5-Aminolevulinic Acid
- Chicken Erythrocyte Pyrimidine 5-Nucleotidase: Purification and Characterization of the Subclass I Enzyme
- Coenzymes Q9 and Q10, Vitamin E and Peroxidation in Rat Synaptic and Non-Synaptic Occipital Cerebral Cortex Mitochondria during Ageing
- Membrane Activity of (Cys48Ser) Lung Surfactant Protein B Increases with Dimerisation
- Participation of Residue F552 in Domain III of the Protective Antigen in the Biological Activity of Anthrax Lethal Toxin
- Purification of Chrysancorin, a Novel Antifungal Protein with Mitogenic Activity from Garland Chrysanthemum Seeds
- Legumain Forms from Plants and Animals Differ in Their Specificity
- Assignment of the Complete Disulphide Bridge Pattern in the Human Recombinant Follitropin β -Chain
- The Small GTPase Ras Is Involved in Growth Factor-Regulated Expression of the α1 Integrin Subunit in PC12 Cells
- The Mouse Gap Junction Gene Connexin29 Is Highly Expressed in Sciatic Nerve and Regulated during Brain Development
- A Selenocysteine-Containing Peroxiredoxin from the Strictly Anaerobic Organism Eubacterium acidaminophilum
- Characterization of C-Terminally Truncated Human Tissue Inhibitor of Metalloproteinases-4 Expressed in Pichia pastoris
