Ziegler, Karl and Diener, Annette and Herpin, Carine and Richter, Ralf and Deutzmann, Rainer and Lockau, Wolfgang (1998) Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). EUROPEAN JOURNAL OF BIOCHEMISTRY, 254 (1). pp. 154-159. ISSN 0014-2956
Full text not available from this repository.Abstract
Cyanophycin (multi-L-arginyl-poly-L-aspartate), a water-insoluble reserve polymer of cyanobacteria, is a product of nonribosomal peptide synthesis. The purification of cyanophycin synthetase of the cyanobacterium Anabaena variabilis is described. In sodium dodecylsulfate/polyacrylamide gel electrophoresis, the enzyme preparation shows one band with an apparent molecular mass of 100 kDa. The native enzyme has an apparent molecular mass of approximately 230 kDa, as determined by size-exclusion chromatography, suggesting that the active form is a homodimer. During catalysis, ATP is converted to ADP, The gene coding for cyanophycin synthetase has been identified in the sequenced genome of Synechocystis sp. PCC 6803. The C-terminal 60% of the deduced amino acid sequence of cyanophycin synthetase show sequence similarity to enzymes of the superfamily of ligases involved in the biosynthesis of murein and of folyl-poly(gamma-glutamate). Cells of Escherichia coli harbouring the gene on a plasmid express active synthetase and accumulate cyanophycin-like material. The results prove that a single enzyme catalyzes the de novo synthesis of cyanophycin.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ALGA ANABAENA-CYLINDRICA; GRANULE POLYPEPTIDE; PROTEINS; ACID; non-ribosomal peptide synthesis; cyanobacteria; cyanophycin synthetase; purification; heterologous expression |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 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: | 24 Feb 2023 07:52 |
| Last Modified: | 24 Feb 2023 07:52 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49807 |
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