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J Biol Chem, Vol. 273, Issue 5, 2684-2691, January 30, 1998
From the Department of Bacteriology, University of Wisconsin,
Madison, Wisconsin 53706-1521
The cobD gene of Salmonella
typhimurium LT2 has been cloned, sequenced, and overexpressed.
The overexpressed protein had a molecular mass of ~40 kDa, in
agreement with the mass predicted by the deduced amino acid sequence
(40.8 kDa). Computer analysis of the deduced amino acid sequence of
CobD identified a consensus pyridoxal phosphate-binding motif. The role
of CobD in cobalamin biosynthesis in this bacterium has been
established. CobD was shown to decarboxylate L-threonine
O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate. We propose that the latter is a substrate in
the reaction catalyzed by the CbiB enzyme proposed to be responsible for the conversion of adenosylcobyric acid to adenosylcobinamide and
that the product of the reaction is adenosylcobinamide phosphate, not
adenosylcobinamide as previously thought. The implications of these
findings are discussed in light of the demonstrated kinase activity of
the CobU enzyme (O'Toole, G. A., and Escalante-Semerena, J. C. (1995) J. Biol. Chem. 270, 23560-23569)
responsible for the conversion of adenosylcobinamide to
adenosylcobinamide phosphate. These findings shed light on the strategy
used by this bacterium for the assimilation of exogenous
unphosphorylated cobinamide from its environment. To our knowledge,
CobD is the first enzyme reported to have
L-threonine-O-3-phosphate decarboxylase
activity, and computer analysis of its amino acid sequence suggests
that it may be a member of a new class of pyridoxal
phosphate-dependent decarboxylases.
CobD, a Novel Enzyme with
L-Threonine-O-3-phosphate Decarboxylase
Activity, Is Responsible for the Synthesis of
(R)-1-Amino-2-propanol O-2-Phosphate, a
Proposed New Intermediate in Cobalamin Biosynthesis in
Salmonella typhimurium LT2
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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