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Research article

Isoaspartyl dipeptidase activity of plant-type asparaginases

Mahdi HEJAZI, Kirill PIOTUKH, Jens MATTOW, Rainer DEUTZMANN, Rudolf VOLKMER-ENGERT, Wolfgang LOCKAU
Biochemical Journal May 15, 2002, 364 (1) 129-136; DOI: 10.1042/bj3640129
Mahdi HEJAZI
Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany
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Kirill PIOTUKH
Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany
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Jens MATTOW
Department Immunologie, Max-Planck-Institut für Infektionsbiologie, Schumannstr. 21–22, D-10117 Berlin, Germany
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Rainer DEUTZMANN
Biochemie I, Universität Regensburg, Universitätsstr. 31, D-95053 Regensburg, Germany
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Rudolf VOLKMER-ENGERT
Medizinische Immunologie, Universitätsklinikum Charité, Schumannstr. 20–21, D-10117 Berlin, Germany
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Wolfgang LOCKAU
Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestr. 117, D-10115 Berlin, Germany
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Abstract

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.

  • cyanophycin
  • glycosylasparaginase
  • isoaspartyl dipeptidase
  • N-terminal nucleophile hydrolase
  • plant-type asparaginase

Footnotes

  • Abbreviations used: Ana. 7120, Anabaena sp. PCC 7120; α-SU, α-subunits; A. thaliana, Arabidopsis thaliana strain Landsberg erecta; CyanoBase, database covering the genomes of Syn. 6803 and Ana. 7120; GlcNAc-Asn, N4-(2-acetamido-2-deoxy-β-d-glucopyranosyl)-l-asparagine; MALDI—TOF-MS, matrix-assisted laser-desorption ionization—time-of-flight mass spectrometry; ORF, open reading frame; PCC, Pasteur culture collection; Syn. 6803, Synechocystis sp. PCC 6803.

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May 2002

Volume: 364 Issue: 1

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Isoaspartyl dipeptidase activity of plant-type asparaginases
Mahdi HEJAZI, Kirill PIOTUKH, Jens MATTOW, Rainer DEUTZMANN, Rudolf VOLKMER-ENGERT, Wolfgang LOCKAU
Biochemical Journal May 2002, 364 (1) 129-136; DOI: 10.1042/bj3640129
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Isoaspartyl dipeptidase activity of plant-type asparaginases
Mahdi HEJAZI, Kirill PIOTUKH, Jens MATTOW, Rainer DEUTZMANN, Rudolf VOLKMER-ENGERT, Wolfgang LOCKAU
Biochemical Journal May 2002, 364 (1) 129-136; DOI: 10.1042/bj3640129

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Keywords

cyanophycin
glycosylasparaginase
isoaspartyl dipeptidase
N-terminal nucleophile hydrolase
plant-type asparaginase

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