Determination of Francisella tularensis AcpB Acid Phosphatase Substrate Preferences
| Autor: | Clara Vu, Evan Crowe, Ricardo Valladares, Ekaterina Kuznetsova, Claudio F. Gonzalez |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
musculoskeletal diseases
chemistry.chemical_classification biology Physiology Phosphatase Acid phosphatase Cell Biology biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Microbiology Pathogenesis chemistry.chemical_compound Metabolic pathway Enzyme Biosynthesis chemistry biology.protein bacteria Francisella skin and connective tissue diseases Francisella tularensis Biotechnology |
| Zdroj: | Microbial Physiology. 19:198-203 |
| ISSN: | 2673-1673 2673-1665 |
| Popis: | The Francisella speciesencode 4 main acid phosphatases (Acp) that are potentially involved in pathogenesis through currently unknown mechanisms. Only 2 of these enzymes, AcpA and AcpC, have been biochemically characterized to date. In this work we describe the catalytic properties of Francisella tularensis AcpB utilizing an array of 120 phosphorylated substrates. In contrast to most acid phosphatases, the purified enzyme showed a narrow range of substrate preferences, with the highest affinity towards thiamine phosphate (Km = 150 µM). Francisella species do not possess a thiamine biosynthetic pathway even though vitamin B1 is indispensable in numerous cellular functions. Consequently, thiamine should be incorporated from the environment, in this case, from the host cell. Our results suggested that AcpB could provide the hydrolytic activity necessary to transform the nontransportable phosphorylated vitamin B1 present in tissues to a form that can be absorbed by the intracellular pathogen. |
| Databáze: | OpenAIRE |
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