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 His 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 autoproteolytic 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.
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Research Article|
May 08 2002
Isoaspartyl dipeptidase activity of plant-type asparaginases
Mahdi HEJAZI;
Mahdi HEJAZI
∗Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany
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Kirill PIOTUKH;
Kirill PIOTUKH
∗Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany
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Jens MATTOW;
Jens MATTOW
†Department Immunologie, Max-Planck-Institut für Infektionsbiologie, Schumannstr. 21–22, D-10117 Berlin, Germany
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Rainer DEUTZMANN;
Rainer DEUTZMANN
‡Biochemie I, Universität Regensburg, Universitätsstr. 31, D-95053 Regensburg, Germany
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Rudolf VOLKMER-ENGERT;
Rudolf VOLKMER-ENGERT
§Medizinische Immunologie, Universitätsklinikum Charité, Schumannstr. 20–21, D-10117 Berlin, Germany
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Wolfgang LOCKAU
Wolfgang LOCKAU
1
∗Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany
1To whom correspondence should be addressed (e-mail wolfgang.lockau@biologie.hu-berlin.de).
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Publisher: Portland Press Ltd
Received:
October 26 2001
Revision Received:
February 01 2002
Accepted:
March 01 2002
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2002
2002
Biochem J (2002) 364 (1): 129–136.
Article history
Received:
October 26 2001
Revision Received:
February 01 2002
Accepted:
March 01 2002
Citation
Mahdi HEJAZI, Kirill PIOTUKH, Jens MATTOW, Rainer DEUTZMANN, Rudolf VOLKMER-ENGERT, Wolfgang LOCKAU; Isoaspartyl dipeptidase activity of plant-type asparaginases. Biochem J 15 May 2002; 364 (1): 129–136. doi: https://doi.org/10.1042/bj3640129
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