Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis
| Autor: | Hermann Pape, Martin Jarling, Anne Koch, Uwe Kramer, Werner Schröder, Ralf Jossek, Birgit Niehues |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_classification
Molecular mass Kinase Micromonosporaceae General Medicine Maltose Maltokinase Biology Biochemistry Microbiology Substrate Specificity Phosphotransferase Kinetics Phosphotransferases (Alcohol Group Acceptor) chemistry.chemical_compound Enzyme chemistry Genetics Phosphorylation Sugar Phosphates Molecular Biology Gene |
| Zdroj: | Archives of Microbiology. 180:233-239 |
| ISSN: | 1432-072X 0302-8933 |
| DOI: | 10.1007/s00203-003-0575-y |
| Popis: | Crude extracts of Actinoplanes missouriensis and related strains catalyze the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. The enzyme of A. missouriensis responsible for this reaction was purified and characterized. This protein has an estimated molecular mass of 57 kDa and it is most likely a monomer. The K(m) value was 2.6 mM for maltose and 0.54 mM for ATP. Only maltose acted effectively as phosphoryl-group acceptor, and ATP was not replaceable as phosphoryl-group donor. Tryptic peptides of the enzyme were sequenced, and the sequences of these peptides will allow construction of degenerate primers to identify the gene coding for this unique kinase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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