Hejazi, Mahdi and Piotukh, Kirill and Mattow, Jens and Deutzmann, Rainer and Volkmer-Engert, Rudolf and Lockau, Wolfgang (2002) Isoaspartyl dipeptidase activity of plant-type asparaginases. BIOCHEMICAL JOURNAL, 364. pp. 129-136. ISSN 0264-6021, 1470-8728
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Recombinant plant-type asparaginases from the cyanobacteria Synechocystis sp, PCC (Pasteur culture collection) 6803 and Anabaena sp. PCC 7120, from Escherichia coli and from the plant Arabidopsis thaliana were expressed in E. coli with either an N-terminal or a C-terminal I lis tag, and purified. Although each of the four enzymes is encoded by a single gene, their mature forms consist of two protein subunits that are generated by auto-proteolytic cleavage of the primary translation products at the Gly-Thr bond within the sequence GTI/VG. The enzymes not only deamidated asparagine but also hydrolysed a range of isoaspartyl dipeptides. As various isoaspartyl peptides are known to arise from proteolytic degradation of post-translationally altered proteins containing isoaspartyl residues, and from depolymerization of the cyanobacterial reserve polymer multi-L-arginyl-poly-L-aspartic acid (cyanophycin), plant-type asparaginases may not only function in asparagine catabolism but also in the final steps of protein and cyanophycin degradation. The properties of these enzymes are compared with those of the sequence-related glycosylasparaginases.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | N-TERMINAL NUCLEOPHILE; MOLECULAR-CLONING; CYANOPHYCIN; GLYCOSYLASPARAGINASE; HYDROLYSIS; PROTEINS; ENZYME; GENE; PURIFICATION; PEPTIDES; cyanophycin; glycosylasparaginase; isoaspartyl dipeptidase; N-terminal nucleophile hydrolase; plant-type asparaginase |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Rainer Deutzmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 26 Oct 2021 08:41 |
| Last Modified: | 26 Oct 2021 08:41 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40250 |
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