Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis.
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.
Niehues
Birgit
B
Westfälische Wilhelms-Universität, Institut für Mikrobiologie, Corrensstrasse 3, 48149, Münster, Germany.
Jossek
Ralf
R
Kramer
Uwe
U
Koch
Anne
A
Jarling
Martin
M
Schröder
Werner
W
Pape
Hermann
H
D007700:Kinetics; D008320:Maltose / Q000378:metabolism*; D008848:Micromonosporaceae / Q000201:enzymology*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry / Q000302:isolation & purification*; D013379:Substrate Specificity; D013403:Sugar Phosphates / Q000378:metabolism
D013403:Sugar Phosphates; C080751:maltose 1-phosphate; D008320:Maltose; D017853:Phosphotransferases (Alcohol Group Acceptor); C100489:maltokinase