TAILIEUCHUNG - Báo cáo khoa học: The 3-ureidopropionase of Caenorhabditis elegans, an enzyme involved in pyrimidine degradation

Pyrimidines are important metabolites in all cells. Levels of cellular pyrimi-dines are controlled by multiple mechanisms, with one of these comprising the reductive degradation pathway. In the model invertebrateCaenorhabditis elegans, two of the three enzymes of reductive pyrimidine degradation have previously been characterized. | ễFEBS Journal The 3-ureidopropionase of Caenorhabditis elegans an enzyme involved in pyrimidine degradation Tim Janowitz Irene Ajonina Markus Perbandt Christian Woltersdorf Patrick Hertel Eva Liebau and Ulrike Gigengack Institut fur Zoophysiologie Westfalische Wilhelms-Universitat Munster Germany Keywords b-alanine biochemical characterization GFP fusion protein nucleotides Correspondence T. Janowitz Institut fur Zoophysiologie Westfalische Wilhelms-Universitat Hindenburgplatz 55 D-48143 Munster Germany Fax 49 251 8321766 Tel 49 251 8321710 E-mail Note To prevent confusion and ambiguity in the present study we use the terms 3-ureido-propionase instead of b-alanine synthase and ureido to refer to a carbamoylaminogroup. Other common nomenclatures are given in parenthesis where appropriate Received 19 February 2010 revised 23 July 2010 accepted 3 August 2010 doi Pyrimidines are important metabolites in all cells. Levels of cellular pyrimidines are controlled by multiple mechanisms with one of these comprising the reductive degradation pathway. In the model invertebrate Caenorhabditis elegans two of the three enzymes of reductive pyrimidine degradation have previously been characterized. The enzyme catalysing the final step of pyrimidine breakdown 3-ureidopropionase b-alanine synthase had only been identified based on homology. We therefore cloned and functionally expressed the 3-ureidopropionase of C. elegans as hexahistidine fusion protein. The purified recombinant enzyme readily converted the two pyrimidine degradation products 3-ureidopropionate and 2-methyl-3-urei-dopropionate. The enzyme showed a broad pH optimum between pH and . Activity was highest at approximately 40 C although the half-life of activity was only 65 s at that temperature. The enzyme showed clear Michaelis-Menten kinetics with a Km of 147 26 pM and a Vmax of U-mg protein-1. The quaternary structure of the recombinant enzyme was

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