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J. Biol. Chem., Vol. 276, Issue 46, 42707-42713, November 16, 2001
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From the Applied Microbiology, Center for Chemistry and Chemical
Engineering, Lund Institute of Technology, Lund University, P.O.
Box 124, Lund SE-221 00, Sweden
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
Trehalose-6-phosphate Phosphorylase Is Part of a Novel
Metabolic Pathway for Trehalose Utilization in Lactococcus
lactis*
-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, -glucose 1-phosphate, and glucose 6-phosphate were determined to be 6, 32, 0.9, 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 -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 -phosphoglucomutase activity were detected in Enterococcus faecalis cell extract, indicating
that this bacterium exhibits the same trehalose assimilation route as
L. lactis.
*
This work was supported by European Community Program
Contract FAIR-CT98-4267.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 46 46 222 3412;
Fax: 46 46 222 4203; E-mail: Peter.Radstrom@tmb.lth.se.
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