Abstract
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.
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Niehues, B., Jossek, R., Kramer, U. et al. Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis . Arch Microbiol 180, 233–239 (2003). https://doi.org/10.1007/s00203-003-0575-y
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DOI: https://doi.org/10.1007/s00203-003-0575-y