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D-Alanine Metabolism in L. pneumophila Lens

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Description

Legionella pneumophila is the causative agent of Legionnaires disease, which replicates as an intracellular parasite of amoebae and persists in the environment as a free-living microbe (Ref.1 & 2). D-Alanine is a necessary precursor in the biosynthesis of cell wall in this bacterium. The naturally occurring L-Alanine isomer is racemized to its D-form through the action of a class of enzymes called AlRs (Alanine Racemase). This enzyme is ubiquitous among prokaryotes and with very few exceptions are absent in eukaryotes (Ref.3).

AlR belongs to the class of Isomerase enzymes, catalyzing the the racemization of L-Alanine and D-Alanine, using Pyridoxal 5 -Phosphate (Vitamin-B6) as a cofactor, which is the first step in D-Alanine metabolism (Ref.4 & 5). . L-Alanine is also a product [...]

References:

1.Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity.
Cazalet C, Rusniok C, Bruggemann H, Zidane N, Magnier A, Ma L, Tichit M, Jarraud S, Bouchier C, Vandenesch F, Kunst F, Etienne J, Glaser P, Buchrieser C.
Nat Genet. 2004 Nov; 36(11):1165-73
2.Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product.
Noda M, Matoba Y, Kumagai T, Sugiyama M.
J Biol Chem. 2004 Oct 29; 279(44):46153-61
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