Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis

@article{Niehues2003IsolationAC,
  title={Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis},
  author={Birgit Niehues and R. Jossek and U. Kramer and A. Koch and M. Jarling and W. Schröder and H. Pape},
  journal={Archives of Microbiology},
  year={2003},
  volume={180},
  pages={233-239}
}
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 Km 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… Expand

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