Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii

Erika V. Soriano, Diane E. McCloskey, Cynthia Kinsland, Anthony E. Pegg, Steven E. Ealick

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)377-382
Number of pages6
JournalActa Crystallographica Section D: Biological Crystallography
Volume64
Issue number4
DOIs
StatePublished - Mar 19 2008

All Science Journal Classification (ASJC) codes

  • Structural Biology

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