Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii
| Autor: | Erika V. Soriano, Steven E. Ealick, Anthony E. Pegg, Diane E. McCloskey, Cynthia Kinsland |
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| Rok vydání: | 2007 |
| Předmět: |
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Molecular Methanococcus Arginine Decarboxylation Carboxy-Lyases Mutant Molecular Conformation Serine X-Ray Diffraction Structural Biology pyruvoyl Cloning Molecular decarboxylation autoprocessing Pyruvates chemistry.chemical_classification Binding Sites biology General Medicine arginine decarboxylase Lyase biology.organism_classification Research Papers Amino acid chemistry Biochemistry Mutagenesis Mutation Arginine decarboxylase Crystallization serinolysis |
| Zdroj: | Acta Crystallographica Section D: Biological Crystallography |
| ISSN: | 0907-4449 |
| Popis: | The crystal structures of two arginine decarboxylase mutant proteins provide insights into the mechanisms of pyruvoyl-group formation and the decarboxylation reaction. Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 Å resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction. |
| Databáze: | OpenAIRE |
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