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Papers In Press, published online ahead of print September 11, 2001
Applied Microbiology, Center for Chemistry and Chemical Engineering, Lund, Scania SE-221 00
Corresponding Author: ulrika.nilsson{at}tmb.lth.se
Lactococcus lactis splits phosphorylated trehalose by the action of inorganic phosphate- dependent trehalose 6-phosphate phosphorylase (TrePP) in a novel catabolic pathway. TrePP was found to catalyze the reversible conversion of trehalose 6-phosphate into beta-glucose 1-phosphate and glucose 6-phosphate by measuring intermediate sugar phosphates in cell extracts from trehalose-cultivated lactococci. According to native PAGE and SDS-PAGE, TrePP was shown to be a monomeric enzyme with a molecular mass of 94 kDa. Reaction kinetics suggested that the enzyme follows a ternary-complex mechanism with optimal phosphorolysis at 35 °C and pH 6.3. The equilibrium constants were found to be 0.026 and 0.032 at pH 6.3 and 7.0, respectively, favoring the formation of trehalose 6-phosphate. The Michaelis-Menten constants of TrePP for trehalose 6-phosphate, inorganic phosphate, beta-glucose 1-phosphate and glucose 6-phosphate were determined to be 6 mM, 32 mM, 0.9 mM, and 4 mM, respectively. The TrePP-encoding gene, designated trePP, was localized in a putative trehalose operon of L. lactis. This operon includes the gene encoding beta-phosphoglucomutase in addition to three open reading frames believed to encode a transcriptional regulator and two trehalose-specific phosphotransferase system components. The identity of trePP was confirmed by determining the N-terminal amino acid sequence of TrePP and by its overexpression in Escherichia coli and L. lactis, as well as the construction of a lactococcal trePP knockout mutant. Furthermore, both TrePP and beta-phosphoglucomutase activity were detected in Enterococcus faecalis cell extract, indicating that this bacterium exhibits the same trehalose assimilation route as L. lactis.
J. Biol. Chem, 10.1074/jbc.M108279200
Submitted on August 28, 2001
Revised on September 11, 2001
Accepted on September 11, 2001
Trehalose 6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis
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