| Literature DB >> 12879214 |
Birgit Niehues1, Ralf Jossek, Uwe Kramer, Anne Koch, Martin Jarling, Werner Schröder, Hermann Pape.
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.Entities:
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Year: 2003 PMID： 12879214 DOI： 10.1007/s00203-003-0575-y
Source DB: PubMed Journal: Arch Microbiol ISSN： 0302-8933 Impact factor: 2.552